DCTN1 encodes p150Glued, the largest subunit of dynactin, the multiprotein complex that activates cytoplasmic dynein-1. p150Glued forms, with DCTN2 and DCTN3, the shoulder of the Arp1-filament-based dynactin complex and projects a long coiled-coil arm ending in an N-terminal CAP-Gly and basic domain. Through these regions it binds dynein intermediate chain, microtubules (preferentially tyrosinated) and plus-end tracking proteins EB1 and CLIP-170, so that dynactin, together with a cargo adaptor such as BICD2 or HOOK3, converts dynein into an ultra-processive minus-end-directed motor and loads it at microtubule plus ends. Dynein-dynactin transports vesicles, endosomes, lysosomes, retromer carriers and other organelles, drives retrograde axonal transport, and pulls on the nuclear envelope in nuclear positioning, neuronal nucleokinesis and prophase nuclear envelope breakdown. In mitosis p150Glued localizes to kinetochores, spindle poles and the cell cortex, where cortical dynein-dynactin positions and orients the spindle. A separate centrosomal pool at mother-centriole subdistal appendages anchors microtubules and supports centriole cohesion and primary cilium formation. The neuron-enriched full-length isoform (with CAP-Gly domain) also acts directly on microtubules, promoting nucleation and suppressing catastrophe. CAP-Gly domain mutations cause Perry syndrome and distal hereditary motor neuronopathy, and DCTN1 variants are associated with ALS susceptibility.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000132 establishment of mitotic spindle orientation | IBA GO_REF:0000033 | ACCEPT | Summary: IBA for establishment of mitotic spindle orientation; dynein-dynactin anchored at the cell cortex pulls on astral microtubules to orient the spindle, and human p150Glued has direct experimental support. Reason: The PAINT node placement is consistent with conserved cortical dynein-dynactin function in spindle positioning (yeast, worm and human data). Human DCTN1 carries its own IMP (PMID:22327364), so the IBA reflects inherited function. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Plays a role in metaphase spindle orientation PMID:22327364 We find that this signal comprises the spindle-pole-localized polo-like kinase (Plk1), which regulates dynein localization by controlling the interaction between dynein-dynactin and its upstream cortical targeting factors NuMA and LGN. |
| GO:0000132 establishment of mitotic spindle orientation | IMP PMID:22327364 Chromosome- and spindle-pole-derived signals generate an int... | ACCEPT | Summary: Spindle orientation IMP in human cells; Plk1 controls cortical dynein-dynactin (including p150) and hence spindle position/orientation. Reason: Full text shows asymmetric cortical dynactin/p150 localization and that dynein-dynactin at the cortex is controlled to orient the spindle. UniProt summarises this as a role in metaphase spindle orientation. Supporting Evidence: PMID:22327364 We find that this signal comprises the spindle-pole-localized polo-like kinase (Plk1), which regulates dynein localization by controlling the interaction between dynein-dynactin and its upstream cortical targeting factors NuMA and LGN. file:human/DCTN1/DCTN1-uniprot.txt Plays a role in metaphase spindle orientation |
| GO:0000278 mitotic cell cycle | NAS PMID:1828535 Homology of a 150K cytoplasmic dynein-associated polypeptide... | MARK AS OVER ANNOTATED | Summary: NAS to the broad term mitotic cell cycle from the original cloning paper of p150Glued. Reason: The 1991 paper cloned the dynein-associated 150K polypeptide and only speculated about dynein roles in mitosis; more specific, experimentally supported mitotic processes (spindle orientation, prophase nuclear envelope breakdown) are annotated separately. The generic cell-cycle term adds little. Supporting Evidence: PMID:1828535 It is thought to be responsible for retrograde axonal transport and other aspects of organelle motility and may have a role in the poleward movement of mitotic chromosomes. |
| GO:0000776 kinetochore | IBA GO_REF:0000033 | ACCEPT | Summary: Kinetochore localization (IBA) of dynactin during mitosis is well established; dynein-dynactin is recruited to kinetochores by RZZ/Spindly. Reason: Consistent with experimental data in human cells (IDA rows from PMID:19468067 and PMID:23027904). Supporting Evidence: PMID:19468067 The recruitment of dynein/dynactin to KTs is dependent on the conserved Rod/Zw10/Zwilch (RZZ) complex PMID:23027904 Accordingly, we found that p150Glued is absent from kinetochores in nocodazole-arrested cells overexpressing high levels of GFP-NuMA(1β705)-CAAX |
| GO:0000776 kinetochore | IDA PMID:19468067 Mitotic control of kinetochore-associated dynein and spindle... | ACCEPT | Summary: Kinetochore IDA from the human Spindly study, in which dynein/dynactin at kinetochores is the object of analysis. Reason: The paper examines Spindly-dependent kinetochore recruitment of dynein/dynactin in human cells; kinetochore is a bona fide mitotic location of dynactin. Supporting Evidence: PMID:19468067 The recruitment of dynein/dynactin to KTs is dependent on the conserved Rod/Zw10/Zwilch (RZZ) complex |
| GO:0000776 kinetochore | IDA PMID:23027904 Cortical dynein is critical for proper spindle positioning i... | ACCEPT | Summary: Kinetochore IDA; p150Glued staining at kinetochores is displaced when dynein is redirected to the cortex. Reason: Immunostaining of p150Glued in HeLa cells supports kinetochore localization. Supporting Evidence: PMID:23027904 Accordingly, we found that p150Glued is absent from kinetochores in nocodazole-arrested cells overexpressing high levels of GFP-NuMA(1β705)-CAAX |
| GO:0000922 spindle pole | IBA GO_REF:0000033 | ACCEPT | Summary: Spindle pole (IBA) localization of dynactin, consistent with its role in focusing microtubule minus ends at mitotic poles. Reason: Supported by human IDA data (PMID:14718566, PMID:25774020). Supporting Evidence: PMID:14718566 detected by localizations of NuMA and the p150 component of dynactin PMID:25774020 Entering into mitosis, p150(glued) was robustly enriched in the mitotic spindle nearby the spindle poles but not in the centrosome. |
| GO:0000922 spindle pole | IDA PMID:14718566 TOGp, the human homolog of XMAP215/Dis1, is required for cen... | ACCEPT | Summary: Spindle pole IDA; p150 is used in this study as a spindle-pole marker whose localization depends on TOGp. Reason: The abstract directly reports p150 dynactin localization at spindle poles. Supporting Evidence: PMID:14718566 detected by localizations of NuMA and the p150 component of dynactin |
| GO:0000922 spindle pole | IEA GO_REF:0000107 | ACCEPT | Summary: Spindle pole IEA (Ensembl Compara ortholog transfer); consistent with human experimental data. Reason: Redundant with IDA/IBA but correct. Supporting Evidence: PMID:25774020 Entering into mitosis, p150(glued) was robustly enriched in the mitotic spindle nearby the spindle poles but not in the centrosome. |
| GO:0005515 protein binding | IPI PMID:12857853 Interactions between the evolutionarily conserved, actin-rel... | REMOVE | Summary: Interaction with Arp1/ACTR1B within the dynactin complex (Arp11 characterization). Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:12857853 The dynein activator dynactin is a multiprotein complex with distinct microtubule- and cargo-binding domains. |
| GO:0005515 protein binding | IPI PMID:15107855 The Bardet-Biedl protein BBS4 targets cargo to the pericentr... | REMOVE | Summary: Interaction with BBS4, which acts as an adaptor recruiting PCM1 to p150Glued at centriolar satellites. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:15107855 where it functions as an adaptor of the p150(glued) subunit of the dynein transport machinery to recruit PCM1 file:human/DCTN1/DCTN1-deep-research-falcon.md Many organelle and mitotic functions are established for dynactin as a whole and should not be over-annotated as independent p150βcargo interactions. |
| GO:0005515 protein binding | IPI PMID:17139249 GSK-3beta-regulated interaction of BICD with dynein is invol... | REMOVE | Summary: Interaction with BICD1 in the context of GSK-3beta regulated dynein-BICD binding. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:17139249 BICD is known to form a complex with dynein-dynactin and to function in the intracellular vesicle trafficking. |
| GO:0005515 protein binding | IPI PMID:17532294 FBXL5 interacts with p150Glued and regulates its ubiquitinat... | REMOVE | Summary: Interaction with the F-box protein FBXL5, which regulates p150Glued ubiquitination and turnover. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:17532294 FBXL5 binds to p150(Glued)in vitro and in vivo. |
| GO:0005515 protein binding | IPI PMID:17828275 CLIP170 autoinhibition mimics intermolecular interactions wi... | REMOVE | Summary: Structural study of the CLIP-170 zinc knuckle interaction with the p150Glued CAP-Gly domain. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:17828275 autoinhibitory interactions within CLIP170 use the same binding determinants as CLIP170's intermolecular interactions with p150(Glued). |
| GO:0005515 protein binding | IPI PMID:17828275 CLIP170 autoinhibition mimics intermolecular interactions wi... | REMOVE | Summary: Structural study of the CLIP-170 interaction with the p150Glued CAP-Gly domain (isoform-specific partner row). Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:17828275 autoinhibitory interactions within CLIP170 use the same binding determinants as CLIP170's intermolecular interactions with p150(Glued). |
| GO:0005515 protein binding | IPI PMID:17828277 Structure-function relationship of CAP-Gly domains. | REMOVE | Summary: CAP-Gly domain interaction with CLIP-170 EEY/F motifs. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:17828277 The CAP-Gly-EEY/F interaction is essential for the recruitment of the dynactin complex by CLIP170 and for activation of CLIP170. |
| GO:0005515 protein binding | IPI PMID:17828277 Structure-function relationship of CAP-Gly domains. | REMOVE | Summary: CAP-Gly domain interaction with EB1 (MAPRE1) C-terminal EEY/F motif. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:17828277 We demonstrate that the conserved GKNDG motif of CAP-Gly domains is responsible for targeting to the C-terminal EEY/F sequence motifs of CLIP170, EB proteins and microtubules. |
| GO:0005515 protein binding | IPI PMID:17932487 Interaction of tau protein with the dynactin complex. | MODIFY | Summary: IPI with tau (MAPT isoform); the N-terminal projection domain of tau binds the C-terminus of p150Glued. Reason: The interaction is specific and mapped, and GO has a dedicated term (tau protein binding). Replace generic protein binding with the informative binding term; this is non-core to DCTN1 function. Proposed replacements: tau protein binding Supporting Evidence: PMID:17932487 We show here for the first time that the N-terminal projection domain of tau binds to the C-terminus of the p150 subunit of the dynactin complex. |
| GO:0005515 protein binding | IPI PMID:18000879 Novel interaction partners of Bardet-Biedl syndrome proteins... | REMOVE | Summary: Yeast two-hybrid screen of BBS protein partners; BBS4 interaction. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:18000879 Applying yeast two-hybrid (Y2H) technology we found a series of novel, functionally potentially plausible binding partners of BBS1, BBS2, BBS4, and BBS7. |
| GO:0005515 protein binding | IPI PMID:18615096 Huntingtin phosphorylation acts as a molecular switch for an... | REMOVE | Summary: Interaction with HAP1 in the huntingtin phosphorylation/transport-direction study. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:18615096 When phosphorylated, huntingtin recruits kinesin-1 to the dynactin complex on vesicles and MTs. |
| GO:0005515 protein binding | IPI PMID:18922795 Huntingtin regulates RE1-silencing transcription factor/neur... | REMOVE | Summary: Co-immunoprecipitation with huntingtin in a RILP-p150Glued-huntingtin complex regulating REST nuclear trafficking. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:18922795 Coimmunoprecipitation analysis further showed a complex containing RILP, dynactin p150(Glued), and huntingtin. |
| GO:0005515 protein binding | IPI PMID:18922795 Huntingtin regulates RE1-silencing transcription factor/neur... | REMOVE | Summary: Interaction with RILP (REST-interacting LIM protein). Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:18922795 Coimmunoprecipitation of proteins in vitro expressed in a reticulocyte lysate system showed an interaction between REST/NRSF and RILP as well as between RILP and dynactin p150(Glued). |
| GO:0005515 protein binding | IPI PMID:19619496 The retromer coat complex coordinates endosomal sorting and ... | REMOVE | Summary: Interaction with the retromer sorting nexin SNX6. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:19619496 which is regulated through association of SNX5/SNX6 with the p150(glued) component of dynactin, an activator of the minus-end directed microtubule motor dynein file:human/DCTN1/DCTN1-deep-research-falcon.md Many organelle and mitotic functions are established for dynactin as a whole and should not be over-annotated as independent p150βcargo interactions. |
| GO:0005515 protein binding | IPI PMID:19619496 The retromer coat complex coordinates endosomal sorting and ... | REMOVE | Summary: Interaction with the retromer sorting nexin SNX5. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:19619496 which is regulated through association of SNX5/SNX6 with the p150(glued) component of dynactin, an activator of the minus-end directed microtubule motor dynein |
| GO:0005515 protein binding | IPI PMID:19935774 The retromer component SNX6 interacts with dynactin p150(Glu... | REMOVE | Summary: Interaction with SNX6, which recruits dynein-dynactin to retromer-coated endosomal tubules. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:19935774 recruitment of the motor complex to the membrane-associated retromer requires the SNX6-p150(Glued) interaction file:human/DCTN1/DCTN1-deep-research-falcon.md Many organelle and mitotic functions are established for dynactin as a whole and should not be over-annotated as independent p150βcargo interactions. |
| GO:0005515 protein binding | IPI PMID:20133940 Nucleoporin translocated promoter region (Tpr) associates wi... | REMOVE | Summary: Association of the nucleoporin Tpr with dynein and dynactin. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:20133940 we show association of another nucleoporin, termed Tpr (translocated promoter region), with the molecular motors dynein and dynactin |
| GO:0005515 protein binding | IPI PMID:20679239 Polo-like kinase 1 phosphorylation of p150Glued facilitates ... | REMOVE | Summary: Interaction with CLIP-170 in the Plk1-p150Glued study. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:20679239 Significantly, Plk1-mediated phosphorylation of p150(Glued) at Ser-179 positively regulates its accumulation at the nuclear envelope during prophase. |
| GO:0005515 protein binding | IPI PMID:20679239 Polo-like kinase 1 phosphorylation of p150Glued facilitates ... | REMOVE | Summary: Interaction with Plk1, which phosphorylates p150Glued at Ser-179. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:20679239 Significantly, Plk1-mediated phosphorylation of p150(Glued) at Ser-179 positively regulates its accumulation at the nuclear envelope during prophase. |
| GO:0005515 protein binding | IPI PMID:20719959 Par6 alpha interacts with the dynactin subunit p150 Glued an... | REMOVE | Summary: Interaction with Par6alpha, which controls centrosomal recruitment of p150Glued. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:20719959 Depletion of Par6Ξ± caused the mislocalization of p150(Glued) and centrosomal components that are critical for microtubule anchoring at the centrosome. |
| GO:0005515 protein binding | IPI PMID:20978158 A novel human dynactin-associated protein, dynAP, promotes a... | REMOVE | Summary: Interaction with dynAP (C18orf26), a dynactin-associated transmembrane protein. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:20978158 This protein was designated dynAP (dynactin-associated protein) because of its interaction with dynactin subunits that comprised a microtubule-based motor protein complex. |
| GO:0005515 protein binding | IPI PMID:22159412 Linking cytoplasmic dynein and transport of Rab8 vesicles to... | REMOVE | Summary: Interaction with the doublecortin-domain protein DCDC5 (DCDC1). Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:22159412 We show that DCDC5 interacts with cytoplasmic dynein and Rab8 |
| GO:0005515 protein binding | IPI PMID:22261744 Neuronal ceroid lipofuscinosis protein CLN3 interacts with m... | REMOVE | Summary: Interaction with the lysosomal membrane protein CLN3. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:22261744 CLN3 interacted with motor components driving both plus and minus end microtubular trafficking: tubulin, dynactin, dynein and kinesin-2. |
| GO:0005515 protein binding | IPI PMID:22777741 Tubulin-binding cofactor B is a direct interaction partner o... | REMOVE | Summary: Interaction with tubulin folding cofactor B (TBCB). Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:22777741 A yeast-two-hybrid screen for putative interacting proteins of dynactin p150(Glued) has revealed tubulin-folding cofactor B (TBCB). |
| GO:0005515 protein binding | IPI PMID:22797915 The centriolar satellite protein Cep131 is important for gen... | REMOVE | Summary: Interaction with the centriolar satellite protein CEP131. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:22797915 requires both an intact microtubule network and a functional dynein-dynactin transport system |
| GO:0005515 protein binding | IPI PMID:23524952 PtdIns(4)P regulates retromer-motor interaction to facilitat... | REMOVE | Summary: SNX6-p150Glued interaction, negatively regulated by PtdIns(4)P at the TGN. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:23524952 negatively regulates the protein-protein interaction between the p150(Glued) subunit of dynein-dynactin and the retromer component SNX6 |
| GO:0005515 protein binding | IPI PMID:23574715 The novel actin/focal adhesion-associated protein MISP is in... | REMOVE | Summary: Weak co-immunoprecipitation with MISP. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:23574715 Co-immunoprecipitation demonstrating that endogenous MISP co-precipitates with p150glued |
| GO:0005515 protein binding | IPI PMID:23874158 Dynactin subunit p150(Glued) is a neuron-specific anti-catas... | REMOVE | Summary: Interaction with EB1 (MAPRE1) in the anti-catastrophe study. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:23874158 Here, we demonstrate in vitro using assembly assays and TIRF microscopy, and in primary neurons using live-cell imaging, that p150(Glued) is a potent anti-catastrophe factor for microtubules. |
| GO:0005515 protein binding | IPI PMID:24867236 Cep126 is required for pericentriolar satellite localisation... | REMOVE | Summary: Interaction with the centrosomal protein CEP126. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:24867236 Cep126 full-length and the 1β967 truncation mutant interact with p150Glued. |
| GO:0005515 protein binding | IPI PMID:24997520 Reconstitution of a hierarchical +TIP interaction network co... | REMOVE | Summary: In vitro reconstitution: p150Glued is recruited to growing microtubule ends by EB1 and CLIP-170. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:24997520 a hierarchical recruitment mode targets the large dynactin subunit p150Glued to growing microtubule ends via EB1 and CLIP-170 |
| GO:0005515 protein binding | IPI PMID:25189619 HPS6 interacts with dynactin p150Glued to mediate retrograde... | REMOVE | Summary: Interaction with HPS6, which acts as a lysosomal cargo adaptor for dynein-dynactin. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:25189619 HPS6 directly interacts with the dynactin p150(Glued) subunit of the dynein-dynactin motor complex and acts as cargo adaptor for the retrograde motor file:human/DCTN1/DCTN1-deep-research-falcon.md Many organelle and mitotic functions are established for dynactin as a whole and should not be over-annotated as independent p150βcargo interactions. |
| GO:0005515 protein binding | IPI PMID:26269332 The Human Tau Interactome: Binding to the Ribonucleoproteome... | REMOVE | Summary: High-throughput tau interactome (crosslinking mass spectrometry). Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:26269332 Here we employed mild in vivo crosslinking, isobaric labeling, and tandem mass spectrometry to characterize molecular interactions of human tau in a neuroblastoma cell model. |
| GO:0005515 protein binding | IPI PMID:26496610 A human interactome in three quantitative dimensions organiz... | REMOVE | Summary: High-throughput HeLa GFP-pulldown interactome (EB1 partner). Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:26496610 Using quantitative proteomics, we detect specific interactions, estimate interaction stoichiometries, and measure cellular abundances of interacting proteins. |
| GO:0005515 protein binding | IPI PMID:26638075 A Dynamic Protein Interaction Landscape of the Human Centros... | REMOVE | Summary: BioID proximity map of the centrosome-cilium interface (ACTR1B). Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:26638075 we use proximity-dependent biotinylation (BioID) to map the centrosome-cilium interface |
| GO:0005515 protein binding | IPI PMID:26638075 A Dynamic Protein Interaction Landscape of the Human Centros... | REMOVE | Summary: BioID proximity map of the centrosome-cilium interface (EB1). Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:26638075 we use proximity-dependent biotinylation (BioID) to map the centrosome-cilium interface |
| GO:0005515 protein binding | IPI PMID:26972003 Ξ±-Tubulin Tyrosination and CLIP-170 Phosphorylation Regulate... | REMOVE | Summary: Interaction with CLIP-170 in the study of retrograde transport initiation in the distal axon. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:26972003 We find that phosphorylation of the cytoskeletal-organelle linker protein CLIP-170 and post-translational modifications of the microtubule track combine to precisely control the initiation of retrograde transport. |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | REMOVE | Summary: High-throughput ciliary/organelle interactome (EB1). Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:27173435 Known complexes include those in ciliary transport (IFT-A and -B, the BBSome and KIF3 complex), organellar organization/transport (the exocyst, dynactin and dynein) |
| GO:0005515 protein binding | IPI PMID:28394342 Regulation of spindle integrity and mitotic fidelity by BCCI... | REMOVE | Summary: Interaction with BCCIP isoform alpha in the spindle-integrity study. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:28394342 A fraction of mitotic dynein/dynactin is deposited to the cell cortex, and this deposition is essential to produce the motor force that buttresses and orients the spindle. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: High-throughput dual-cell-line interactome (ACTR1B). Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: OpenCell endogenous tagging interactome (EB1). Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. |
| GO:0005515 protein binding | IPI PMID:35314674 RUFY3 and RUFY4 are ARL8 effectors that promote coupling of ... | REMOVE | Summary: Interaction with the ARL8 effector RUFY3, which couples endolysosomes to dynein-dynactin. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:35314674 several lines of evidence suggest that the effects are more directly related to the ability of RUFY3/4 to couple endolysosomes to dynein-dynactin file:human/DCTN1/DCTN1-deep-research-falcon.md Many organelle and mitotic functions are established for dynactin as a whole and should not be over-annotated as independent p150βcargo interactions. |
| GO:0005515 protein binding | IPI PMID:35314674 RUFY3 and RUFY4 are ARL8 effectors that promote coupling of ... | REMOVE | Summary: Interaction with the ARL8 effector RUFY4, which couples endolysosomes to dynein-dynactin. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:35314674 several lines of evidence suggest that the effects are more directly related to the ability of RUFY3/4 to couple endolysosomes to dynein-dynactin |
| GO:0005515 protein binding | IPI PMID:9361024 Huntingtin-associated protein 1 (HAP1) interacts with the p1... | REMOVE | Summary: Interaction with huntingtin-associated protein 1 (HAP1). Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:9361024 HAP1 co-immunoprecipitated with p150 Glued from brain extracts, indicating that the interaction occurs in vivo |
| GO:0005515 protein binding | IPI PMID:9722614 Characterization of the p22 subunit of dynactin reveals the ... | REMOVE | Summary: Co-fractionation of dynactin subunits including p22 (DCTN3) with p150Glued. Generic protein binding. Reason: Generic protein binding is uninformative. The reported interaction is not disputed, but it does not identify a molecular function of DCTN1 beyond binding a partner; the functionally relevant activities (dynein activation, microtubule and tubulin binding) are captured by other terms. Supporting Evidence: PMID:9722614 p22 from brain cytosol binds to a dynein intermediate chain (DIC) column in a salt-dependent fashion as does p150Glued. |
| GO:0005635 nuclear envelope | IDA PMID:20679239 Polo-like kinase 1 phosphorylation of p150Glued facilitates ... | ACCEPT | Summary: Nuclear envelope localization of p150Glued during prophase, enhanced by Plk1 phosphorylation at Ser-179. Reason: Direct IDA in human cells. Dynein-dynactin on the nuclear envelope is also the force-coupling point for nuclear positioning and nucleokinesis (via nesprin/BICD2 and nucleoporin adaptors). Supporting Evidence: PMID:20679239 Significantly, Plk1-mediated phosphorylation of p150(Glued) at Ser-179 positively regulates its accumulation at the nuclear envelope during prophase. |
| GO:0005635 nuclear envelope | IEA GO_REF:0000044 | ACCEPT | Summary: Nuclear envelope (IEA from UniProt subcellular location mapping). Reason: Consistent with IDA (PMID:20679239). Supporting Evidence: PMID:20679239 Significantly, Plk1-mediated phosphorylation of p150(Glued) at Ser-179 positively regulates its accumulation at the nuclear envelope during prophase. |
| GO:0005737 cytoplasm | EXP PMID:17828277 Structure-function relationship of CAP-Gly domains. | ACCEPT | Summary: Cytoplasm; dynactin is a cytoplasmic complex acting on the microtubule cytoskeleton and membranous cargoes. Reason: Correct, if general; more specific locations (centrosome, microtubule plus ends, cell cortex, nuclear envelope) are annotated separately. |
| GO:0005737 cytoplasm | IDA PMID:18305234 Motor neuron disease occurring in a mutant dynactin mouse mo... | ACCEPT | Summary: Cytoplasm; dynactin is a cytoplasmic complex acting on the microtubule cytoskeleton and membranous cargoes. Reason: Correct, if general; more specific locations (centrosome, microtubule plus ends, cell cortex, nuclear envelope) are annotated separately. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: Cytoplasm; dynactin is a cytoplasmic complex acting on the microtubule cytoskeleton and membranous cargoes. Reason: Correct, if general; more specific locations (centrosome, microtubule plus ends, cell cortex, nuclear envelope) are annotated separately. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0005737 cytoplasm | TAS PMID:1828535 Homology of a 150K cytoplasmic dynein-associated polypeptide... | ACCEPT | Summary: Cytoplasm; dynactin is a cytoplasmic complex acting on the microtubule cytoskeleton and membranous cargoes. Reason: Correct, if general; more specific locations (centrosome, microtubule plus ends, cell cortex, nuclear envelope) are annotated separately. Supporting Evidence: PMID:1828535 a cytoplasmic dynein-associated polypeptide of relative molecular mass 150,000 (Mr 150K) |
| GO:0005813 centrosome | IDA PMID:20719959 Par6 alpha interacts with the dynactin subunit p150 Glued an... | ACCEPT | Summary: Centrosome localization of p150Glued, regulated by Par6alpha. Reason: Direct IDA in human cells. Supporting Evidence: PMID:20719959 Depletion of Par6Ξ± caused the mislocalization of p150(Glued) and centrosomal components that are critical for microtubule anchoring at the centrosome. |
| GO:0005813 centrosome | IDA PMID:21399614 Novel asymmetrically localizing components of human centroso... | ACCEPT | Summary: Centrosome IDA from a centrosome proteomics/localization screen in human cells. Reason: Consistent with extensive evidence for centrosomal dynactin; accepted deferring to curator for the specific localization data. Supporting Evidence: PMID:21399614 for proteins with a role in microtubule organization such as dynactins, and subunits of the Ξ³-TuRC and HAUS complexes |
| GO:0005813 centrosome | IDA PMID:23985322 Ste20-like protein kinase SLK (LOSK) regulates microtubule o... | ACCEPT | Summary: Centrosome IDA in the SLK kinase study (p150Glued phosphorylation regulates microtubule organization). Reason: Centrosomal p150Glued is well established; accepted. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Cytoplasm, cytoskeleton, microtubule organizing center, centrosome |
| GO:0005813 centrosome | IDA PMID:25774020 Cell Cycle-Dependent Localization of Dynactin Subunit p150 g... | ACCEPT | Summary: Centrosome IDA; p150Glued resides at the mother centriole in G1/S. Reason: Direct localization data. Supporting Evidence: PMID:25774020 Here we found that p150(glued) was located in the mother centriole during G1/S stage and its centrosomal residency was independent of microtubule transportation. |
| GO:0005813 centrosome | IEA GO_REF:0000044 | ACCEPT | Summary: Centrosome IEA; consistent with IDA. Reason: Redundant but correct. Supporting Evidence: PMID:25774020 Here we found that p150(glued) was located in the mother centriole during G1/S stage and its centrosomal residency was independent of microtubule transportation. |
| GO:0005814 centriole | IDA PMID:23213374 3D-structured illumination microscopy provides novel insight... | ACCEPT | Summary: Centriole IDA from 3D-SIM mapping of centriole architecture. Reason: p150Glued is a subdistal appendage component of the mother centriole; the localization is corroborated by PMID:23386061 and PMID:25774020. Supporting Evidence: PMID:23386061 Kif3a recruits p150(Glued) to the subdistal appendages of mother centrioles, critical for centrosomes to function as microtubule-organizing centres. PMID:25774020 Here we found that p150(glued) was located in the mother centriole during G1/S stage and its centrosomal residency was independent of microtubule transportation. |
| GO:0005814 centriole | IDA PMID:23386061 Kif3a interacts with Dynactin subunit p150 Glued to organize... | ACCEPT | Summary: Centriole IDA; Kif3a recruits p150Glued to subdistal appendages of the mother centriole. Reason: Direct evidence. Supporting Evidence: PMID:23386061 Kif3a recruits p150(Glued) to the subdistal appendages of mother centrioles, critical for centrosomes to function as microtubule-organizing centres. |
| GO:0005814 centriole | IDA PMID:25774020 Cell Cycle-Dependent Localization of Dynactin Subunit p150 g... | ACCEPT | Summary: Centriole IDA; p150Glued located at the mother centriole in G1/S. Reason: Direct evidence. Supporting Evidence: PMID:25774020 Here we found that p150(glued) was located in the mother centriole during G1/S stage and its centrosomal residency was independent of microtubule transportation. |
| GO:0005814 centriole | IEA GO_REF:0000120 | ACCEPT | Summary: Centriole IEA; consistent with IDA. Reason: Redundant but correct. Supporting Evidence: PMID:23386061 Kif3a recruits p150(Glued) to the subdistal appendages of mother centrioles, critical for centrosomes to function as microtubule-organizing centres. |
| GO:0005819 spindle | IDA PMID:25774020 Cell Cycle-Dependent Localization of Dynactin Subunit p150 g... | ACCEPT | Summary: Spindle IDA; p150Glued enriched on the mitotic spindle near poles. Reason: Direct evidence. Supporting Evidence: PMID:25774020 Entering into mitosis, p150(glued) was robustly enriched in the mitotic spindle nearby the spindle poles but not in the centrosome. |
| GO:0005819 spindle | IEA GO_REF:0000044 | ACCEPT | Summary: Spindle IEA; consistent with IDA. Reason: Redundant but correct. Supporting Evidence: PMID:25774020 Entering into mitosis, p150(glued) was robustly enriched in the mitotic spindle nearby the spindle poles but not in the centrosome. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1791092 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2213248 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2574840 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2574845 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3000310 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-3000319 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380272 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380283 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380294 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380303 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380311 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380316 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380455 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-380508 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5617816 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626220 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626223 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626227 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626228 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626681 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5626699 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5638009 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6809003 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-6809006 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8849350 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8849353 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853405 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-8853419 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9700179 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9700181 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9712078 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9712083 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9712084 | ACCEPT | Summary: Cytosol (Reactome TAS); dynactin is a soluble cytosolic complex that associates with microtubules, centrosomes and membranes. Reason: Reactome places DCTN1 in cytosolic dynein-dynactin events (e.g. mitotic, cilium/centrosome and COPI-independent Golgi-to-ER transport reactions). Correct, if general. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | ACCEPT | Summary: Cytoskeleton (IEA from UniProt subcellular location). Reason: Correct; p150Glued binds microtubules and associates with microtubule-organizing structures. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. |
| GO:0005874 microtubule | IDA PMID:21525035 PEX14 is required for microtubule-based peroxisome motility ... | ACCEPT | Summary: Microtubule IDA from the PEX14 peroxisome motility study. Reason: Microtubule association of p150Glued is well established (CAP-Gly and basic domain); accepted deferring to curator. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. |
| GO:0005874 microtubule | IDA PMID:22777741 Tubulin-binding cofactor B is a direct interaction partner o... | ACCEPT | Summary: Microtubule IDA; p150 localizes to the microtubule network, reduced by TBCB overexpression. Reason: Direct evidence. Supporting Evidence: PMID:22777741 overexpression of TBCB leads to the decreased localization of p150 to the microtubule network |
| GO:0005874 microtubule | IDA PMID:25774020 Cell Cycle-Dependent Localization of Dynactin Subunit p150 g... | ACCEPT | Summary: Microtubule IDA in U2OS cells. Reason: Consistent with direct microtubule binding. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Localizes to microtubule plus ends |
| GO:0005875 microtubule associated complex | IBA GO_REF:0000033 | MODIFY | Summary: IBA to microtubule associated complex; DCTN1 is specifically a subunit of dynactin, a child of this term. Reason: The parent term is correct but uninformative; GO:0005869 dynactin complex is_a microtubule associated complex and precisely describes the complex p150Glued belongs to (shoulder subunit with DCTN2/DCTN3). Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000431881 SUPPORTS TRANSFER Dynactin p150 family node; membership of the dynactin complex is inherited across the clade, so the transfer is sound, but the complex-level term chosen is the generic parent of dynactin complex. Proposed replacements: dynactin complex Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules PMID:25814576 On top sits the shoulder domain (7) from which emerges a long projection, corresponding to dynactinβs largest subunit p150Glued (DCTN1) (8). |
| GO:0005875 microtubule associated complex | IMP PMID:16505168 A motor neuron disease-associated mutation in p150Glued pert... | MODIFY | Summary: IMP to microtubule associated complex from the G59S study showing the mutant perturbs dynactin function. Reason: p150Glued is a subunit of dynactin; the specific child term dynactin complex is appropriate. Proposed replacements: dynactin complex Supporting Evidence: PMID:16505168 A motor neuron disease-associated mutation in p150Glued perturbs dynactin function PMID:25814576 On top sits the shoulder domain (7) from which emerges a long projection, corresponding to dynactinβs largest subunit p150Glued (DCTN1) (8). |
| GO:0005938 cell cortex | IDA PMID:23027904 Cortical dynein is critical for proper spindle positioning i... | ACCEPT | Summary: Cell cortex IDA; cortical p150Glued increases with Galphai/LGN overexpression. Reason: Direct evidence; cortical dynein-dynactin generates spindle-positioning forces. Supporting Evidence: PMID:23027904 overexpression of GΞ±i1-YFP or YFP-LGN leads to an increase and expansion of cortical p150Glued |
| GO:0005938 cell cortex | IDA PMID:23509069 MISP is a novel Plk1 substrate required for proper spindle o... | ACCEPT | Summary: Colocalizes with cell cortex (MISP study); MISP depletion alters cortical p150glued distribution. Reason: Direct observation. Supporting Evidence: PMID:23509069 Quantification of the percentage of metaphase cells with cortical accentuated and distributed p150glued |
| GO:0005938 cell cortex | IEA GO_REF:0000044 | ACCEPT | Summary: Cell cortex IEA; consistent with IDA. Reason: Redundant but correct. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Cytoplasm, cell cortex |
| GO:0007077 mitotic nuclear membrane disassembly | IMP PMID:20679239 Polo-like kinase 1 phosphorylation of p150Glued facilitates ... | KEEP AS NON CORE | Summary: Mitotic nuclear membrane disassembly; Plk1 phosphorylation of p150Glued promotes its nuclear-envelope accumulation and facilitates NEBD. Reason: Experimental support from human cells; dynein-dynactin pulling on the nuclear envelope helps tear it at prophase. This is a context-specific use of the dynein-activation core function. Supporting Evidence: PMID:20679239 Polo-like kinase 1 phosphorylation of p150Glued facilitates nuclear envelope breakdown during prophase. PMID:20679239 Significantly, Plk1-mediated phosphorylation of p150(Glued) at Ser-179 positively regulates its accumulation at the nuclear envelope during prophase. |
| GO:0007097 nuclear migration | IBA GO_REF:0000033 | ACCEPT | Summary: IBA to nuclear migration. Dynein-dynactin moves nuclei toward microtubule minus ends in fungi, worms and vertebrate neurons; in migrating neurons nesprin/SUN complexes anchor dynein/dynactin (including p150) at the nuclear envelope. Reason: The PAINT node (donors including C. elegans dnc-1) reflects conserved dynactin involvement in nuclear positioning. In mouse cortex, p150 co-precipitates with nesprin-1/2 and dynein/dynactin supplies the pulling force for nucleokinesis. DCTN1, as the dynein-binding and microtubule-binding subunit of the dynein activator, does part of the work of this process. Supporting Evidence: PMID:19874786 Our results indicate that the SUN-KASH complexes mediate the coupling between the nucleus and the centrosome, and provide anchors in the NE for cytoplasmic dynein/dynactin during neuronal migration. PMID:19874786 Second, the p150 subunit was consistently precipitated by antibodies against either Syne-1 or Syne-2 from the E17. PMID:39115447 the most membrane-proximal fragment (SR48-56), which contains three potential Spindly motifs, one potential CC1-box motif, and the LEWD motif, was sufficient for binding to dynein heavy chain (DHC), the dynactin subunit p150Glued, and kinesin heavy chain (KHC) PMID:15173193 There is a growing body of evidence that the dyneinβdynactin complex associates with nuclear membranes in many cell types, and these complexes coupled to the nucleus may move in a minus endβdirected fashion toward the centrosome. |
| GO:0007399 nervous system development | NAS PMID:17360970 Dynactin is required for coordinated bidirectional motility,... | MARK AS OVER ANNOTATED | Summary: NAS to nervous system development from a Drosophila Arp1 (dynactin) mutant study of axonal transport. Reason: The cited work concerns dynactin requirement for bidirectional axonal organelle transport in Drosophila, not a developmental role of human DCTN1. Nervous system development is a very broad downstream consequence. Supporting Evidence: PMID:17360970 To test directly and rigorously the hypothesis that dynactin is required to attach dynein to membranes, we used both a Drosophila mutant and RNA interference to generate organisms and cells lacking the critical dynactin subunit, actin-related protein 1. |
| GO:0007528 neuromuscular junction development | IMP PMID:18305234 Motor neuron disease occurring in a mutant dynactin mouse mo... | MARK AS OVER ANNOTATED | Summary: Neuromuscular junction development IMP from transgenic mice expressing mutant human p150Glued. Reason: This annotation derives from phenotypes of mice overexpressing disease-mutant human p150Glued (a gain-of-function/dominant model). The phenotype reflects neurodegeneration caused by the mutant protein, not a process in which normal DCTN1 performs a step. It is an indirect, organism-level consequence. Supporting Evidence: PMID:18305234 Neuronal expression of mutant, but not wild type, dynactin p150(Glued) causes motor neuron disease in these animals that are characterized by defects in vesicular transport in cell bodies of motor neurons, axonal swelling and axo-terminal degeneration. |
| GO:0008017 microtubule binding | IDA PMID:23874158 Dynactin subunit p150(Glued) is a neuron-specific anti-catas... | ACCEPT | Summary: Microtubule binding IDA; p150 N-terminal CAP-Gly/basic region binds microtubules and tubulin. Reason: Core activity of p150Glued, required for dynein-dynactin recruitment to microtubules and anti-catastrophe activity. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon PMID:23874158 Here, we demonstrate in vitro using assembly assays and TIRF microscopy, and in primary neurons using live-cell imaging, that p150(Glued) is a potent anti-catastrophe factor for microtubules. |
| GO:0008017 microtubule binding | IDA PMID:26972003 Ξ±-Tubulin Tyrosination and CLIP-170 Phosphorylation Regulate... | ACCEPT | Summary: Microtubule binding IDA in the tyrosination/CLIP-170 transport-initiation study. Reason: p150Glued preferentially binds tyrosinated microtubules; core activity. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Binds preferentially to tyrosinated microtubules than to detyrosinated file:human/DCTN1/DCTN1-uniprot.txt Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. |
| GO:0008017 microtubule binding | IEA GO_REF:0000120 | ACCEPT | Summary: Microtubule binding IEA (combined automated methods). Reason: Correct; core activity. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. |
| GO:0008017 microtubule binding | IMP PMID:16505168 A motor neuron disease-associated mutation in p150Glued pert... | ACCEPT | Summary: Microtubule binding IMP; the disease G59S CAP-Gly mutation reduces microtubule binding. Reason: Core activity supported by mutagenesis. Supporting Evidence: PMID:16505168 we observed the binding of only half of the mutant p150Glued polypeptide to microtubules, suggesting that some portion of the mutant protein population is unavailable for binding to microtubules. PMID:16505168 G59S p150Glued was cytoplasmically dispersed in COS7 cells 24β48 h after transfection, whereas wild-type p150Glued decorated microtubules. |
| GO:0010008 endosome membrane | IDA PMID:19564404 Cholesterol sensor ORP1L contacts the ER protein VAP to cont... | ACCEPT | Summary: Late endosome membrane; p150Glued is recruited to Rab7-RILP on late endosomes, controlled by ORP1L cholesterol sensing and VAP. Reason: Direct data in human cells; late endosomes/lysosomes are major dynein-dynactin cargoes. Supporting Evidence: PMID:19564404 VAP-A removes p150Glued from Rab7βRILP. |
| GO:0010457 centriole-centriole cohesion | IMP PMID:23386061 Kif3a interacts with Dynactin subunit p150 Glued to organize... | KEEP AS NON CORE | Summary: Centriole-centriole cohesion; p150Glued depletion phenocopies Kif3a loss, including loss of centriole cohesion. Reason: Supported by experimental data; this is a function of the subdistal-appendage pool of p150Glued rather than the dynein-activating core function. Supporting Evidence: PMID:23386061 Depletion of p150(Glued) phenocopies the effects of loss of Kif3a, indicating that Kif3a recruitment of p150(Glued) is critical for subdistal appendage formation. file:human/DCTN1/DCTN1-uniprot.txt Plays a role in centriole cohesion and subdistal appendage organization and function. |
| GO:0015630 microtubule cytoskeleton | IDA GO_REF:0000052 | ACCEPT | Summary: Microtubule cytoskeleton IDA (Human Protein Atlas immunofluorescence). Reason: Correct. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Binds to both dynein and microtubules providing a link between specific cargos, microtubules and dynein. |
| GO:0015631 tubulin binding | IDA PMID:23874158 Dynactin subunit p150(Glued) is a neuron-specific anti-catas... | ACCEPT | Summary: Tubulin binding IDA; the p150 N-terminus forms a stable complex with soluble tubulin via tubulin C-termini. Reason: Direct biochemical evidence; underlies neuronal anti-catastrophe activity. Supporting Evidence: PMID:23874158 Size exclusion chromatograms for p150 Nt run alone or pre-incubated with tubulin reveal that p150 forms a stable complex with tubulin. file:human/DCTN1/DCTN1-uniprot.txt Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | KEEP AS NON CORE | Summary: Membrane (HDA) from an NK cell membrane proteome. Reason: p150Glued is a peripheral protein recruited to membranous cargoes by adaptors; the membrane-fraction detection is plausible but not informative. Supporting Evidence: PMID:19946888 The remaining species were largely involved in cellular processes and molecular functions that could be predicted to be transiently associated with membranes. |
| GO:0019901 protein kinase binding | IPI PMID:17139249 GSK-3beta-regulated interaction of BICD with dynein is invol... | KEEP AS NON CORE | Summary: Protein kinase binding (GSK-3beta) from the BICD/GSK-3beta microtubule anchorage study. Reason: A binding term of limited functional information; the abstract states GSK-3beta regulates BICD binding to dynein but not dynactin. Kept, but not core. Supporting Evidence: PMID:17139249 Our data revealed that GSK-3beta is required for the binding of BICD to dynein but not to dynactin. |
| GO:0021517 ventral spinal cord development | IMP PMID:18305234 Motor neuron disease occurring in a mutant dynactin mouse mo... | MARK AS OVER ANNOTATED | Summary: Ventral spinal cord development IMP from mice expressing mutant human p150Glued. Reason: This annotation derives from phenotypes of mice overexpressing disease-mutant human p150Glued (a gain-of-function/dominant model). The phenotype reflects neurodegeneration caused by the mutant protein, not a process in which normal DCTN1 performs a step. It is an indirect, organism-level consequence. Motor neuron degeneration is not a developmental process. Supporting Evidence: PMID:18305234 Neuronal expression of mutant, but not wild type, dynactin p150(Glued) causes motor neuron disease in these animals that are characterized by defects in vesicular transport in cell bodies of motor neurons, axonal swelling and axo-terminal degeneration. |
| GO:0030424 axon | IBA GO_REF:0000033 | ACCEPT | Summary: Axon (IBA); dynactin functions in axons, where p150Glued stabilizes microtubules and initiates retrograde transport. Reason: Consistent with neuronal data. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Inhibits microtubule catastrophe by binding both to microtubules and to tubulin, leading to enhanced microtubule stability along the axon |
| GO:0030904 retromer complex | IDA PMID:19619496 The retromer coat complex coordinates endosomal sorting and ... | KEEP AS NON CORE | Summary: Colocalizes with retromer complex; SNX5/SNX6 retromer subunits bind p150Glued on endosomal tubules. Reason: Supported; retromer carriers are one class of dynein-dynactin cargo. Supporting Evidence: PMID:19619496 which is regulated through association of SNX5/SNX6 with the p150(glued) component of dynactin, an activator of the minus-end directed microtubule motor dynein |
| GO:0031116 positive regulation of microtubule polymerization | IDA PMID:23874158 Dynactin subunit p150(Glued) is a neuron-specific anti-catas... | ACCEPT | Summary: Positive regulation of microtubule polymerization IDA; p150 N-terminus promotes microtubule polymerization and suppresses catastrophe in neurons. Reason: Direct in vitro and neuronal evidence; a neuron-specific function of the full-length CAP-Gly-containing isoform. Supporting Evidence: PMID:23874158 Here, we demonstrate in vitro using assembly assays and TIRF microscopy, and in primary neurons using live-cell imaging, that p150(Glued) is a potent anti-catastrophe factor for microtubules. PMID:23874158 Polymerization rates and catastrophe frequencies from seeded assembly shows that 200 nM p150 Nt-GCN4 promotes polymerization and inhibits catastrophe independently of 25 nM EB1 |
| GO:0031116 positive regulation of microtubule polymerization | IMP PMID:16505168 A motor neuron disease-associated mutation in p150Glued pert... | ACCEPT | Summary: Positive regulation of microtubule polymerization IMP from the G59S study. Reason: Consistent with the IDA; the CAP-Gly domain is required for the microtubule-stabilizing activity. Supporting Evidence: PMID:16505168 we observed the binding of only half of the mutant p150Glued polypeptide to microtubules, suggesting that some portion of the mutant protein population is unavailable for binding to microtubules. |
| GO:0031252 cell leading edge | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cell leading edge (IEA ortholog transfer). Reason: Plausible peripheral localization; not a core site of DCTN1 function. |
| GO:0032935 sterol sensor activity | IDA PMID:19564404 Cholesterol sensor ORP1L contacts the ER protein VAP to cont... | REMOVE | Summary: Contributes_to sterol sensor activity (IDA, ORP1L study). Reason: In this study the cholesterol sensor is ORP1L; p150Glued is the downstream effector whose recruitment to Rab7-RILP is controlled by ORP1L/VAP. DCTN1 has no sterol-binding domain and does not contribute to sensing sterol; the effect on p150Glued is a readout of the sensor, so this MF assignment is incorrect. The companion cholesterol-transport process rows from the same paper are marked over-annotated rather than removed, because p150Glued does take part in the late-endosome positioning that the process depends on, whereas sensing sterol is an activity it lacks. Supporting Evidence: PMID:19564404 Cholesterol sensor ORP1L contacts the ER protein VAP to control Rab7-RILP-p150 Glued and late endosome positioning. PMID:19564404 VAP-A removes p150Glued from Rab7βRILP. |
| GO:0032991 protein-containing complex | IDA PMID:19564404 Cholesterol sensor ORP1L contacts the ER protein VAP to cont... | MODIFY | Summary: Protein-containing complex IDA; p150Glued recruited (as part of dynactin) to the Rab7-RILP-ORP1L complex on late endosomes. Reason: Correct but generic. The stable complex p150Glued belongs to is dynactin; the RILP-mediated association is a transient cargo-adaptor interaction without a dedicated GO complex term. Replace with dynactin complex. Proposed replacements: dynactin complex Supporting Evidence: PMID:19564404 VAP-A removes p150Glued from Rab7βRILP. file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0032991 protein-containing complex | IEA GO_REF:0000107 | MODIFY | Summary: Protein-containing complex (IEA ortholog transfer); the relevant complex is dynactin. Reason: Replace the generic root-level complex term by dynactin complex. Proposed replacements: dynactin complex Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules |
| GO:0034454 microtubule anchoring at centrosome | IMP PMID:23386061 Kif3a interacts with Dynactin subunit p150 Glued to organize... | ACCEPT | Summary: Microtubule anchoring at centrosome IMP; p150Glued at subdistal appendages is required for microtubule anchoring at the mother centriole. Reason: Direct experimental evidence; well established role of centrosomal dynactin. Supporting Evidence: PMID:23386061 Depletion of p150(Glued) phenocopies the effects of loss of Kif3a, indicating that Kif3a recruitment of p150(Glued) is critical for subdistal appendage formation. file:human/DCTN1/DCTN1-uniprot.txt Also required for microtubule anchoring at the mother centriole |
| GO:0035371 microtubule plus-end | IDA PMID:26972003 Ξ±-Tubulin Tyrosination and CLIP-170 Phosphorylation Regulate... | ACCEPT | Summary: Microtubule plus-end IDA; p150Glued is a +TIP recruited by EB1/CLIP-170 to growing ends. Reason: Core localization for initiating dynein transport. Supporting Evidence: PMID:24997520 a hierarchical recruitment mode targets the large dynactin subunit p150Glued to growing microtubule ends via EB1 and CLIP-170 |
| GO:0035371 microtubule plus-end | IEA GO_REF:0000107 | ACCEPT | Summary: Microtubule plus-end IEA; consistent with experimental data. Reason: Correct. Supporting Evidence: file:human/DCTN1/DCTN1-uniprot.txt Localizes to microtubule plus ends |
| GO:0036064 ciliary basal body | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ciliary basal body (IEA); p150Glued appears at the base of the primary cilium in G0. Reason: Consistent with human data; non-core. Supporting Evidence: PMID:25774020 During serum starvation (G0 stage), p150(glued) appeared at the base of primary cilium and its depletion attenuated starvation-induced primary cilium formation. |
| GO:0042147 retrograde transport, endosome to Golgi | IMP PMID:19619496 The retromer coat complex coordinates endosomal sorting and ... | ACCEPT | Summary: Retrograde transport, endosome to Golgi IMP; SNX5/SNX6-p150Glued coupling of retromer carriers to dynein-dynactin is required for efficient endosome-to-TGN sorting. Reason: Dynein-dynactin drives the movement of retromer tubular carriers; DCTN1 is the direct adaptor-binding subunit, so it does part of the work of this transport. Supporting Evidence: PMID:19619496 which is regulated through association of SNX5/SNX6 with the p150(glued) component of dynactin, an activator of the minus-end directed microtubule motor dynein PMID:19935774 recruitment of the motor complex to the membrane-associated retromer requires the SNX6-p150(Glued) interaction |
| GO:0042632 cholesterol homeostasis | IDA PMID:19564404 Cholesterol sensor ORP1L contacts the ER protein VAP to cont... | MARK AS OVER ANNOTATED | Summary: Cholesterol homeostasis IDA from the ORP1L study. Reason: p150Glued positioning of late endosomes is regulated by cholesterol levels via ORP1L, but DCTN1 is a downstream effector of that sensing, not a component of cholesterol homeostasis machinery. Supporting Evidence: PMID:19564404 VAP-A removes p150Glued from Rab7βRILP. |
| GO:0043005 neuron projection | IDA PMID:18364389 Lysosomal proliferation and distal degeneration in motor neu... | ACCEPT | Summary: Neuron projection localization in motor neurons. Reason: Correct; dynactin is present throughout axons and dendrites. Supporting Evidence: PMID:18364389 In addition, we observe deficits in axonal caliber and neuromuscular junction (NMJ) integrity, indicating distal degeneration of motor neurons. |
| GO:0043025 neuronal cell body | IDA PMID:18364389 Lysosomal proliferation and distal degeneration in motor neu... | ACCEPT | Summary: Neuronal cell body localization in motor neurons. Reason: Correct. Supporting Evidence: PMID:18364389 mutant p150(Glued) causes neurodegeneration in the absence of significant changes in axonal transport |
| GO:0045171 intercellular bridge | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Intercellular bridge (HPA immunofluorescence). Reason: Plausible midbody-associated pool during cytokinesis; non-core. |
| GO:0048156 tau protein binding | NAS PMID:28386764 Roles of tau protein in health and disease. | KEEP AS NON CORE | Summary: Tau protein binding (NAS, tau review). Reason: The tau N-terminus binds the p150 C-terminus (PMID:17932487); a real but non-core interaction. Supporting Evidence: PMID:28386764 The N-terminal region of tau also binds to the C terminus of the p150 subunit of the dynactin complex |
| GO:0050905 neuromuscular process | IMP PMID:18305234 Motor neuron disease occurring in a mutant dynactin mouse mo... | MARK AS OVER ANNOTATED | Summary: Neuromuscular process IMP from transgenic mutant p150Glued mice. Reason: This annotation derives from phenotypes of mice overexpressing disease-mutant human p150Glued (a gain-of-function/dominant model). The phenotype reflects neurodegeneration caused by the mutant protein, not a process in which normal DCTN1 performs a step. It is an indirect, organism-level consequence. Supporting Evidence: PMID:18305234 Neuronal expression of mutant, but not wild type, dynactin p150(Glued) causes motor neuron disease in these animals that are characterized by defects in vesicular transport in cell bodies of motor neurons, axonal swelling and axo-terminal degeneration. |
| GO:0060236 regulation of mitotic spindle organization | IMP PMID:23027904 Cortical dynein is critical for proper spindle positioning i... | MODIFY | Summary: Regulation of mitotic spindle organization IMP; p150Glued siRNA shows that cortical dynein-dynactin is needed for spindle positioning. Reason: The phenotype assayed is spindle positioning (oscillation/centering) driven by cortical dynein-dynactin pulling, which is better captured by establishment of mitotic spindle localization than by spindle organization. Proposed replacements: establishment of mitotic spindle localization Supporting Evidence: PMID:23027904 Cortical dynein is critical for proper spindle positioning in human cells. |
| GO:0061744 motor behavior | IMP PMID:18305234 Motor neuron disease occurring in a mutant dynactin mouse mo... | MARK AS OVER ANNOTATED | Summary: Motor behavior IMP from mice expressing mutant human p150Glued. Reason: This annotation derives from phenotypes of mice overexpressing disease-mutant human p150Glued (a gain-of-function/dominant model). The phenotype reflects neurodegeneration caused by the mutant protein, not a process in which normal DCTN1 performs a step. It is an indirect, organism-level consequence. Supporting Evidence: PMID:18305234 Neuronal expression of mutant, but not wild type, dynactin p150(Glued) causes motor neuron disease in these animals that are characterized by defects in vesicular transport in cell bodies of motor neurons, axonal swelling and axo-terminal degeneration. |
| GO:0061744 motor behavior | IMP PMID:18364389 Lysosomal proliferation and distal degeneration in motor neu... | MARK AS OVER ANNOTATED | Summary: Motor behavior IMP from G59S p150Glued transgenic mice (dSBMA model). Reason: This annotation derives from phenotypes of mice overexpressing disease-mutant human p150Glued (a gain-of-function/dominant model). The phenotype reflects neurodegeneration caused by the mutant protein, not a process in which normal DCTN1 performs a step. It is an indirect, organism-level consequence. Supporting Evidence: PMID:18364389 these mice exhibit late-onset, slowly progressive muscle weakness but do not have a shortened lifespan |
| GO:0070050 neuron cellular homeostasis | IMP PMID:18305234 Motor neuron disease occurring in a mutant dynactin mouse mo... | MARK AS OVER ANNOTATED | Summary: Neuron cellular homeostasis IMP from mutant p150Glued mice. Reason: This annotation derives from phenotypes of mice overexpressing disease-mutant human p150Glued (a gain-of-function/dominant model). The phenotype reflects neurodegeneration caused by the mutant protein, not a process in which normal DCTN1 performs a step. It is an indirect, organism-level consequence. Supporting Evidence: PMID:18305234 Neuronal expression of mutant, but not wild type, dynactin p150(Glued) causes motor neuron disease in these animals that are characterized by defects in vesicular transport in cell bodies of motor neurons, axonal swelling and axo-terminal degeneration. |
| GO:0090063 positive regulation of microtubule nucleation | IDA PMID:23874158 Dynactin subunit p150(Glued) is a neuron-specific anti-catas... | ACCEPT | Summary: Positive regulation of microtubule nucleation IDA; dimeric p150 N-terminus promotes microtubule nucleation in vitro. Reason: Direct evidence; neuron-isoform-specific microtubule regulatory function. Supporting Evidence: PMID:23874158 dimeric p150 Nt-GCN4 catalyzes microtubule nucleation in contrast to monomeric p150 Nt. |
| GO:0090120 lysosome to ER cholesterol transport | IDA PMID:19564404 Cholesterol sensor ORP1L contacts the ER protein VAP to cont... | MARK AS OVER ANNOTATED | Summary: Lysosome to ER cholesterol transport IDA from the ORP1L study. Reason: The study shows cholesterol-regulated removal of p150Glued from Rab7-RILP; DCTN1 does not carry out cholesterol transfer between lysosomes and ER. Supporting Evidence: PMID:19564404 VAP-A removes p150Glued from Rab7βRILP. |
| GO:0098930 axonal transport | IMP NOT PMID:18364389 Lysosomal proliferation and distal degeneration in motor neu... | REMOVE | Summary: NOT axonal transport, based on the absence of detectable transport inhibition in G59S p150Glued transgenic mice. Reason: The experiment shows that one disease allele does not measurably impair bulk axonal transport in this model; it does not show that DCTN1 is not involved in axonal transport. Dynactin is widely documented as essential for dynein-driven (retrograde) axonal transport, and even the G59S study authors interpret a subtle loss of function as affecting retrograde axonal transport. The negative assertion is contradicted by the broader evidence. Supporting Evidence: PMID:18364389 mutant p150(Glued) causes neurodegeneration in the absence of significant changes in axonal transport PMID:17932487 The dynein-activator complex dynactin has an essential role in axonal transport file:human/DCTN1/DCTN1-deep-research-falcon.md The best-defined specialized role is initiation and support of fast retrograde axonal transport. PMID:16505168 This subtle loss of function does not significantly perturb nonneuronal cells but may be sufficient to affect the overall efficiency of retrograde axonal transport in neurons. |
| GO:0099558 maintenance of synapse structure | TAS PMID:18305234 Motor neuron disease occurring in a mutant dynactin mouse mo... | KEEP AS NON CORE | Summary: Maintenance of synapse structure (TAS) from mutant p150Glued mouse work. Reason: Dynein/dynactin is proposed to stabilize the neuromuscular junction, but the evidence is indirect (mutant models); non-core. Supporting Evidence: PMID:18364389 such as trafficking in the degradative pathway and stabilization of the NMJ are likely to be critical in maintaining the health of motor neurons |
| GO:0099738 cell cortex region | IDA PMID:22327364 Chromosome- and spindle-pole-derived signals generate an int... | ACCEPT | Summary: Cell cortex region IDA; asymmetric cortical p150 localization during metaphase. Reason: Direct observation. Supporting Evidence: PMID:22327364 showing the symmetric cortical localization of GFP-LGN and the asymmetric localization of the dynactin subunit p150 |
| GO:0120103 centriolar subdistal appendage | IDA PMID:23213374 3D-structured illumination microscopy provides novel insight... | ACCEPT | Summary: Centriolar subdistal appendage IDA. Reason: p150Glued is a recognized subdistal appendage component; corroborated by PMID:23386061. Supporting Evidence: PMID:23386061 Kif3a recruits p150(Glued) to the subdistal appendages of mother centrioles, critical for centrosomes to function as microtubule-organizing centres. |
| GO:1904398 positive regulation of neuromuscular junction development | IMP PMID:18364389 Lysosomal proliferation and distal degeneration in motor neu... | MARK AS OVER ANNOTATED | Summary: Positive regulation of NMJ development IMP from G59S transgenic mice. Reason: This annotation derives from phenotypes of mice overexpressing disease-mutant human p150Glued (a gain-of-function/dominant model). The phenotype reflects neurodegeneration caused by the mutant protein, not a process in which normal DCTN1 performs a step. It is an indirect, organism-level consequence. Supporting Evidence: PMID:18364389 In addition, we observe deficits in axonal caliber and neuromuscular junction (NMJ) integrity, indicating distal degeneration of motor neurons. |
| GO:1905515 non-motile cilium assembly | IMP PMID:25774020 Cell Cycle-Dependent Localization of Dynactin Subunit p150 g... | KEEP AS NON CORE | Summary: Non-motile cilium assembly IMP; p150Glued depletion attenuates starvation-induced primary cilium formation. Reason: Supported by knockdown data, likely via centrosomal/satellite transport; non-core. Supporting Evidence: PMID:25774020 During serum starvation (G0 stage), p150(glued) appeared at the base of primary cilium and its depletion attenuated starvation-induced primary cilium formation. file:human/DCTN1/DCTN1-uniprot.txt Plays a role in primary cilia formation |
| GO:1990535 neuron projection maintenance | IMP PMID:18305234 Motor neuron disease occurring in a mutant dynactin mouse mo... | KEEP AS NON CORE | Summary: Neuron projection maintenance IMP (mutant p150Glued mice; axo-terminal degeneration). Reason: Consistent with dynactin roles in axonal microtubule stability and transport, but inferred from dominant-mutant models; non-core. Supporting Evidence: PMID:18305234 Neuronal expression of mutant, but not wild type, dynactin p150(Glued) causes motor neuron disease in these animals that are characterized by defects in vesicular transport in cell bodies of motor neurons, axonal swelling and axo-terminal degeneration. |
| GO:1990535 neuron projection maintenance | IMP PMID:18364389 Lysosomal proliferation and distal degeneration in motor neu... | KEEP AS NON CORE | Summary: Neuron projection maintenance IMP (G59S mice; distal degeneration). Reason: As above; non-core. Supporting Evidence: PMID:18364389 In addition, we observe deficits in axonal caliber and neuromuscular junction (NMJ) integrity, indicating distal degeneration of motor neurons. |
| GO:0140660 cytoskeletal motor activator activity | IDA PMID:25035494 Activation of cytoplasmic dynein motility by dynactin-cargo ... | NEW | Summary: Dynactin (with p150Glued as its dynein- and microtubule-binding projection) activates processive motility of mammalian cytoplasmic dynein together with cargo adaptors such as BICD2. Reason: Purified mammalian dynein alone is poorly processive; dynein-dynactin-BICD2 complexes move robustly and processively, and BICD2 alone does not stimulate motility without dynactin. This dynein-activating function is the central molecular role of dynactin and is not represented in the existing annotation set. Because activation is a property of the whole dynactin complex, this is best asserted as contributes_to for DCTN1. Supporting Evidence: PMID:25035494 The addition of BicD2 to purified brain dynein did not stimulate processive motility, indicating a requirement for dynactin PMID:25035494 In contrast to brain dynein, the DDB complexes moved robustly and processively along MTs PMID:38547289 DIC-N opens dynactinβs p150 arm for LIS1 and dynein binding file:human/DCTN1/DCTN1-uniprot.txt Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules file:human/DCTN1/DCTN1-deep-research-falcon.md Many organelle and mitotic functions are established for dynactin as a whole and should not be over-annotated as independent p150βcargo interactions. |
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Download this section (compressed HTML)Q: Should DCTN1 carry an explicit contributes_to cytoskeletal motor activator activity (GO:0140660) annotation, given that dynein activation is a property of the assembled dynactin complex with a cargo adaptor?
Suggested experts: GO molecular function editors, dynein/dynactin biochemists
Q: Is the NOT axonal transport annotation (PMID:18364389) intended to capture only that the G59S allele does not impair bulk transport, and should it be withdrawn given that dynactin is required for retrograde axonal transport initiation?
Suggested experts: GO annotation QC, neuronal transport experts
Q: Which nucleokinesis contexts (radial migration, interkinetic nuclear migration, neural crest) have direct DCTN1-specific evidence, as opposed to evidence from dynactin disruption by dynamitin overexpression?
Suggested experts: neuronal migration biologists
Experiment: Acute degron-mediated depletion of DCTN1 in migrating cortical neurons with live imaging of nucleus-centrosome coupling, rescued by p150 or p135 isoforms and by a CAP-Gly mutant.
Hypothesis: Nuclear translocation in neuronal nucleokinesis requires the dynein-activating function of dynactin but not the CAP-Gly microtubule-binding domain.
Type: live imaging with isoform rescue
Experiment: Single-molecule reconstitution of dynein-dynactin-BICD2 on nesprin-2-decorated membranes with p150 variants lacking CAP-Gly or CC1.
Hypothesis: p150 CC1 and the dynein-binding region are required for nuclear-envelope-anchored dynein force generation.
Type: in vitro reconstitution
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