DYNLT1 (Tctex-1) is a small dynein light chain of the Tctex family that forms homodimers, and heterodimers with DYNLT3 or the dynein-2-specific DYNLT2B/TCTEX1D2. DYNLT dimers bind dynein intermediate chains and are non-catalytic accessory subunits of cytoplasmic dynein-1, the main minus-end-directed microtubule motor for retrograde transport of vesicles and organelles. They are also subunits of dynein-2, the retrograde intraflagellar transport motor of cilia. Depletion of Tctex-1 lengthens primary cilia, consistent with a role in dynein-2-dependent length control. Tctex-1 also has activities apart from the motor. It binds G-protein beta-gamma subunits (identical to AGS2), which compete with dynein intermediate chain for Tctex-1. It regulates neurite outgrowth and actin dynamics, and in cortical progenitors it controls G1 length and neurogenesis. When quiescent cells re-enter the cell cycle, Tctex-1 phosphorylated at Thr94 is recruited to the ciliary transition zone downstream of IGF-1 receptor and Gbetagamma signalling. There, acting apart from dynein, it activates Cdc42-dependent branched-actin polymerization and periciliary endocytosis. This promotes ciliary resorption, which is coupled to S-phase entry. Tctex-1 also binds Rab3D on osteoclast secretory vesicles and is exploited for intracellular targeting of retroviral Gag polyproteins.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000132 establishment of mitotic spindle orientation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Establishment of mitotic spindle orientation (ISS from mouse Dynlt1). Reason: Plausible through cytoplasmic dynein's role in spindle positioning, but not a defining function; cortical progenitor fate effects of Tctex-1 are reported. Supporting Evidence: PMID:21394082 Tctex-1 phosphorylated at Thr 94 is also selectively enriched at the ciliary transition zones of cortical neural progenitors, and has a key role in controlling G(1) length, cell cycle entry and fate determination of these cells during corticogenesis |
| GO:0001673 male germ cell nucleus | NAS PMID:36973253 Distinct dynein complexes defined by DYNLRB1 and DYNLRB2 reg... | UNDECIDED | Summary: Male germ cell nucleus (NAS, DYNLRB paper). Reason: The cited paper concerns DYNLRB1/2 in spermatocyte spindles. I could not find the basis for a DYNLT1 nuclear localization in the cached text, and dynein light chains are cytoplasmic. Left undecided because the curator's basis is not visible. |
| GO:0005515 protein binding | IPI PMID:10644691 Protein phosphatase 2Calpha dephosphorylates axin and activa... | REMOVE | Summary: Interaction with DVL1 (PP2C/Dishevelled paper). Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. The cached abstract concerns PP2C-Dishevelled; any Tctex-1 interaction data are in the full text. |
| GO:0005515 protein binding | IPI PMID:10644691 Protein phosphatase 2Calpha dephosphorylates axin and activa... | REMOVE | Summary: Interaction with DVL2. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. |
| GO:0005515 protein binding | IPI PMID:15503857 Testis-specific human small heat shock protein HSPB9 is a ca... | REMOVE | Summary: Interaction with HSPB9. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Testis-specific HSPB9 interaction; no functional context. |
| GO:0005515 protein binding | IPI PMID:18647839 D-retrovirus morphogenetic switch driven by the targeting si... | REMOVE | Summary: Interaction with M-PMV matrix/Gag (P07567). Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. The viral-protein targeting role is captured by the viral transport process term. Supporting Evidence: PMID:18647839 Biochemical data presented here suggest that Tctex-1, a light chain of the molecular motor dynein, is involved in the intracellular targeting of Mason-Pfizer monkey virus (M-PMV) polyproteins to the cytoplasmic assembly site |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | MODIFY | Summary: Interaction with DYNLT3 (P51808), cilia interaction landscape, a DYNLT-family light chain. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. The partner is another Tctex-family light chain. DYNLT light chains form heterodimers (DYNLT1-DYNLT3; TCTEX-TCTEX1D2 in dynein-2), so the informative MF is protein heterodimerization activity. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:17965411 Yeast two-hybrid and co-immunoprecipitation assays demonstrate that both members of the DYNLT family are capable of forming homodimers and heterodimers PMID:31451806 to the TCTEX-TCTEX1D2 dimer identified in biochemical studies file:human/DYNLT1/DYNLT1-deep-research-falcon.md Purified human **DYNLT1βDYNLT2B/TCTEX1D2** had a SEC-MALS mass of **28.1 kDa**, supporting a heterodimer |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | MODIFY | Summary: Interaction with DYNLT2B/TCTEX1D2 (Q8WW35), cilia interaction landscape, a DYNLT-family light chain. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. The partner is another Tctex-family light chain. DYNLT light chains form heterodimers (DYNLT1-DYNLT3; TCTEX-TCTEX1D2 in dynein-2), so the informative MF is protein heterodimerization activity. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:17965411 Yeast two-hybrid and co-immunoprecipitation assays demonstrate that both members of the DYNLT family are capable of forming homodimers and heterodimers PMID:31451806 to the TCTEX-TCTEX1D2 dimer identified in biochemical studies file:human/DYNLT1/DYNLT1-deep-research-falcon.md Purified human **DYNLT1βDYNLT2B/TCTEX1D2** had a SEC-MALS mass of **28.1 kDa**, supporting a heterodimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: Interaction with DYNLT3 (P51808), HuRI, a DYNLT-family light chain. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. The partner is another Tctex-family light chain. DYNLT light chains form heterodimers (DYNLT1-DYNLT3; TCTEX-TCTEX1D2 in dynein-2), so the informative MF is protein heterodimerization activity. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:17965411 Yeast two-hybrid and co-immunoprecipitation assays demonstrate that both members of the DYNLT family are capable of forming homodimers and heterodimers PMID:31451806 to the TCTEX-TCTEX1D2 dimer identified in biochemical studies file:human/DYNLT1/DYNLT1-deep-research-falcon.md Purified human **DYNLT1βDYNLT2B/TCTEX1D2** had a SEC-MALS mass of **28.1 kDa**, supporting a heterodimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: Interaction with DYNLT2B/TCTEX1D2 (Q8WW35), HuRI, a DYNLT-family light chain. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. The partner is another Tctex-family light chain. DYNLT light chains form heterodimers (DYNLT1-DYNLT3; TCTEX-TCTEX1D2 in dynein-2), so the informative MF is protein heterodimerization activity. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:17965411 Yeast two-hybrid and co-immunoprecipitation assays demonstrate that both members of the DYNLT family are capable of forming homodimers and heterodimers PMID:31451806 to the TCTEX-TCTEX1D2 dimer identified in biochemical studies file:human/DYNLT1/DYNLT1-deep-research-falcon.md Purified human **DYNLT1βDYNLT2B/TCTEX1D2** had a SEC-MALS mass of **28.1 kDa**, supporting a heterodimer |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Interaction with a human protein from a high-throughput binary interactome screen. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. Screen hit without established functional context. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Interaction with a neurodegenerative disease protein (O76024, WFS1). Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Interaction with neurofilament light (P07196). Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: Interaction with DYNLT2B/TCTEX1D2 (Q8WW35), dual proteome-scale networks, a DYNLT-family light chain. Reason: Generic protein binding is uninformative. Removing GO:0005515 does not dispute the interaction. The partner is another Tctex-family light chain. DYNLT light chains form heterodimers (DYNLT1-DYNLT3; TCTEX-TCTEX1D2 in dynein-2), so the informative MF is protein heterodimerization activity. Proposed replacements: protein heterodimerization activity Supporting Evidence: PMID:17965411 Yeast two-hybrid and co-immunoprecipitation assays demonstrate that both members of the DYNLT family are capable of forming homodimers and heterodimers PMID:31451806 to the TCTEX-TCTEX1D2 dimer identified in biochemical studies file:human/DYNLT1/DYNLT1-deep-research-falcon.md Purified human **DYNLT1βDYNLT2B/TCTEX1D2** had a SEC-MALS mass of **28.1 kDa**, supporting a heterodimer |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-6798748 | MARK AS OVER ANNOTATED | Summary: Extracellular region (Reactome, neutrophil degranulation). Reason: Reactome places DYNLT1 in neutrophil granule/secretion compartments on the basis of granule proteomics. DYNLT1 is a cytosolic dynein light chain with no secretion signal, so these extracellular/granule-lumen locations likely reflect contamination or bystander inclusion rather than a functional location. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-6800434 | MARK AS OVER ANNOTATED | Summary: Extracellular region (Reactome, platelet/granule secretion). Reason: Reactome places DYNLT1 in neutrophil granule/secretion compartments on the basis of granule proteomics. DYNLT1 is a cytosolic dynein light chain with no secretion signal, so these extracellular/granule-lumen locations likely reflect contamination or bystander inclusion rather than a functional location. |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: Cytoplasm (IBA). Reason: Cytoplasmic dynein subunit. Supporting Evidence: PMID:17965411 The DYNLT light chains, but not DYNLL light chains, associate exclusively with the dynein complex |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: Cytoplasm (UniProt subcellular location). Reason: Correct. Supporting Evidence: PMID:17965411 The DYNLT light chains, but not DYNLL light chains, associate exclusively with the dynein complex |
| GO:0005794 Golgi apparatus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Golgi apparatus (UniProt subcellular location). Reason: Dynein and its light chains associate with Golgi membranes during trafficking; this is a plausible but non-defining location. |
| GO:0005819 spindle | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Spindle (UniProt subcellular location). Reason: Consistent with cytoplasmic dynein on the mitotic spindle; non-core. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9921297 | ACCEPT | Summary: Cytosol (Reactome). Reason: Correct; soluble light chain and dynein-associated. Supporting Evidence: PMID:17965411 The DYNLT light chains, but not DYNLL light chains, associate exclusively with the dynein complex |
| GO:0005868 cytoplasmic dynein complex | IBA GO_REF:0000033 | ACCEPT | Summary: Cytoplasmic dynein complex (IBA). Reason: DYNLT1 is a light chain of cytoplasmic dynein-1 (and dynein-2). Supporting Evidence: PMID:24986880 We co-expressed genes for all six dynein subunitsβDYNC1H1 (DHC), DYNC1I2 (DIC), DYNC1LI2 (DLIC), DYNLT1 (Tctex), DYNLRB1 (Robl) and DYNLL1 (LC8)βfrom a single baculovirus in Sf9 cells PMID:17965411 The DYNLT light chains, but not DYNLL light chains, associate exclusively with the dynein complex |
| GO:0005868 cytoplasmic dynein complex | IDA PMID:25205765 Subunit composition of the human cytoplasmic dynein-2 comple... | ACCEPT | Summary: Cytoplasmic dynein complex (IDA, dynein-2 composition). Reason: Tctex-1 co-isolates with the dynein-2 intermediate chain WDR34. GO's cytoplasmic dynein complex encompasses dynein-2. Supporting Evidence: PMID:25205765 Here, all known dynein-1 light chain isoforms (LC8-1 and LC8-2, Tctex-1 and Tctex-3, and roadblock-1 and roadblock-2) were identified in association with mGFPβWDR34 |
| GO:0005868 cytoplasmic dynein complex | IPI PMID:24986880 In vitro reconstitution of a highly processive recombinant h... | ACCEPT | Summary: Cytoplasmic dynein complex (IPI, recombinant human dynein-1). Reason: DYNLT1 is one of the six subunits used to reconstitute processive human dynein-1. Supporting Evidence: PMID:24986880 We co-expressed genes for all six dynein subunitsβDYNC1H1 (DHC), DYNC1I2 (DIC), DYNC1LI2 (DLIC), DYNLT1 (Tctex), DYNLRB1 (Robl) and DYNLL1 (LC8)βfrom a single baculovirus in Sf9 cells |
| GO:0005868 cytoplasmic dynein complex | ISS GO_REF:0000024 | ACCEPT | Summary: Cytoplasmic dynein complex (ISS). Reason: Correct. Supporting Evidence: PMID:17965411 The DYNLT light chains, but not DYNLL light chains, associate exclusively with the dynein complex |
| GO:0005868 cytoplasmic dynein complex | ISS GO_REF:0000024 | ACCEPT | Summary: Cytoplasmic dynein complex (ISS, rat). Reason: Correct. Supporting Evidence: PMID:17965411 The DYNLT light chains, but not DYNLL light chains, associate exclusively with the dynein complex |
| GO:0005881 cytoplasmic microtubule | IDA PMID:21262767 Tctex-1, a novel interaction partner of Rab3D, is required f... | KEEP AS NON CORE | Summary: Cytoplasmic microtubule (IDA, osteoclasts). Reason: Tctex-1 associates with microtubules via dynein in osteoclasts; correct but secondary. Supporting Evidence: PMID:21262767 we provide evidence that Tctex-1 and Rab3D intimately associate with the dynein motor complex and microtubules in osteoclasts |
| GO:0005929 cilium | NAS PMID:30065109 Emerging mechanisms of dynein transport in the cytoplasm ver... | ACCEPT | Summary: Cilium (NAS, dynein transport review). Reason: DYNLT1 is a dynein-2 light chain, and phospho-Tctex-1 localizes to the ciliary transition zone. Supporting Evidence: PMID:31451806 light chains (DYNLRB1/2, DYNLL1/2, DYNLT1/3, and TCTEX1D2) PMID:21394082 We show that Tctex-1 phosphorylated at Thr 94 is recruited to ciliary transition zones before S-phase entry and has a pivotal role in both ciliary disassembly and cell cycle progression |
| GO:0005929 cilium | NAS PMID:32229580 Cytoplasmic dynein-2 at a glance. | ACCEPT | Summary: Cilium (NAS, dynein-2 at a glance). Reason: As above. Supporting Evidence: PMID:25205765 Here, all known dynein-1 light chain isoforms (LC8-1 and LC8-2, Tctex-1 and Tctex-3, and roadblock-1 and roadblock-2) were identified in association with mGFPβWDR34 |
| GO:0007018 microtubule-based movement | IBA GO_REF:0000033 | ACCEPT | Summary: Microtubule-based movement (IBA). Reason: As a dynein light chain, DYNLT1 is part of the motor complex that drives microtubule-based movement. It is non-catalytic and contributes through IC binding and cargo/adaptor interactions. Supporting Evidence: PMID:24986880 We co-expressed genes for all six dynein subunitsβDYNC1H1 (DHC), DYNC1I2 (DIC), DYNC1LI2 (DLIC), DYNLT1 (Tctex), DYNLRB1 (Robl) and DYNLL1 (LC8)βfrom a single baculovirus in Sf9 cells PMID:17965411 In addition, both homodimers of the DYNLT family bind all six intermediate chain isoforms |
| GO:0008277 regulation of G protein-coupled receptor signaling pathway | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Regulation of G protein-coupled receptor signaling pathway (ISS). Reason: Tctex-1 is AGS2, a Gbetagamma-binding receptor-independent activator of G protein signalling. Real, but a dynein-independent auxiliary function. Supporting Evidence: PMID:17491591 Tctex-1 was recently identified as a Gbetagamma-binding protein and shown to be identical to the receptor-independent activator of G protein signaling AGS2 PMID:17491591 Furthermore, Gbeta competes with the dynein intermediate chain for binding to Tctex-1, regulating assembly of Tctex-1 into the dynein motor complex |
| GO:0019060 intracellular transport of viral protein in host cell | IMP PMID:18647839 D-retrovirus morphogenetic switch driven by the targeting si... | KEEP AS NON CORE | Summary: Intracellular transport of viral protein in host cell (IMP). Reason: Tctex-1 is used for targeting M-PMV Gag to the cytoplasmic assembly site; host-pathogen context. Supporting Evidence: PMID:18647839 Biochemical data presented here suggest that Tctex-1, a light chain of the molecular motor dynein, is involved in the intracellular targeting of Mason-Pfizer monkey virus (M-PMV) polyproteins to the cytoplasmic assembly site |
| GO:0030286 dynein complex | NAS PMID:30065109 Emerging mechanisms of dynein transport in the cytoplasm ver... | ACCEPT | Summary: Dynein complex (NAS). Reason: Correct (parent of cytoplasmic dynein complex). Supporting Evidence: PMID:24986880 We co-expressed genes for all six dynein subunitsβDYNC1H1 (DHC), DYNC1I2 (DIC), DYNC1LI2 (DLIC), DYNLT1 (Tctex), DYNLRB1 (Robl) and DYNLL1 (LC8)βfrom a single baculovirus in Sf9 cells |
| GO:0030286 dynein complex | NAS PMID:32229580 Cytoplasmic dynein-2 at a glance. | ACCEPT | Summary: Dynein complex (NAS). Reason: Correct. Supporting Evidence: PMID:25205765 Here, all known dynein-1 light chain isoforms (LC8-1 and LC8-2, Tctex-1 and Tctex-3, and roadblock-1 and roadblock-2) were identified in association with mGFPβWDR34 |
| GO:0032388 positive regulation of intracellular transport | NAS PMID:33957056 Structure and Mechanics of Dynein Motors. | KEEP AS NON CORE | Summary: Positive regulation of intracellular transport (NAS, dynein mechanics review). Reason: Light chains link dynein to cargo/adaptors, but DYNLT1 is a structural component of the transport machinery rather than a regulator of it. The term is acceptable only loosely. Supporting Evidence: PMID:17965411 The DYNLT light chains, but not DYNLL light chains, associate exclusively with the dynein complex |
| GO:0034774 secretory granule lumen | TAS Reactome:R-HSA-6798748 | MARK AS OVER ANNOTATED | Summary: Secretory granule lumen (Reactome). Reason: Reactome places DYNLT1 in neutrophil granule/secretion compartments on the basis of granule proteomics. DYNLT1 is a cytosolic dynein light chain with no secretion signal, so these extracellular/granule-lumen locations likely reflect contamination or bystander inclusion rather than a functional location. |
| GO:0035721 intraciliary retrograde transport | NAS PMID:31451806 Structure of the dynein-2 complex and its assembly with intr... | ACCEPT | Summary: Intraciliary retrograde transport (NAS, dynein-2 structure). Reason: DYNLT1/3 are light chains of dynein-2, the retrograde IFT motor, and were included in the recombinant human dynein-2 used for structure. Supporting Evidence: PMID:31451806 light chains (DYNLRB1/2, DYNLL1/2, DYNLT1/3, and TCTEX1D2) PMID:31451806 to the TCTEX-TCTEX1D2 dimer identified in biochemical studies |
| GO:0035721 intraciliary retrograde transport | NAS PMID:32229580 Cytoplasmic dynein-2 at a glance. | ACCEPT | Summary: Intraciliary retrograde transport (NAS). Reason: As above. Supporting Evidence: PMID:25205765 Here, all known dynein-1 light chain isoforms (LC8-1 and LC8-2, Tctex-1 and Tctex-3, and roadblock-1 and roadblock-2) were identified in association with mGFPβWDR34 PMID:21700358 Our data show that Tctex-1 is a key regulator of cilia length and most likely functions as part of dynein-2 |
| GO:0042802 identical protein binding | IPI PMID:17965411 Interaction of the DYNLT (TCTEX1/RP3) light chains and the i... | MODIFY | Summary: Identical protein binding (IPI): DYNLT1 homodimerizes. Reason: DYNLT light chains function as dimers (homodimers bind all IC isoforms). The more informative term is protein homodimerization activity. Proposed replacements: protein homodimerization activity Supporting Evidence: PMID:17965411 Yeast two-hybrid and co-immunoprecipitation assays demonstrate that both members of the DYNLT family are capable of forming homodimers and heterodimers PMID:17965411 In addition, both homodimers of the DYNLT family bind all six intermediate chain isoforms |
| GO:0043657 host cell | IEA GO_REF:0000108 | REMOVE | Summary: Host cell (IEA, inferred from viral transport term). Reason: GO:0043657 'host cell' describes the location of a symbiont gene product within its host. It is inappropriate for a host (human) protein and arose mechanically from the viral protein transport process annotation. |
| GO:0045505 dynein intermediate chain binding | IBA GO_REF:0000033 | ACCEPT | Summary: Dynein intermediate chain binding (IBA). Reason: DYNLT homodimers bind all six cytoplasmic dynein intermediate chain isoforms; core molecular function. Supporting Evidence: PMID:17965411 In addition, both homodimers of the DYNLT family bind all six intermediate chain isoforms |
| GO:0050768 negative regulation of neurogenesis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Negative regulation of neurogenesis (ISS from mouse). Reason: Phospho-Tctex-1 at the transition zone of cortical progenitors controls G1 length and fate. Loss of the pathway causes premature differentiation, so this sits downstream of its ciliary resorption role. Supporting Evidence: PMID:21394082 Tctex-1 phosphorylated at Thr 94 is also selectively enriched at the ciliary transition zones of cortical neural progenitors, and has a key role in controlling G(1) length, cell cycle entry and fate determination of these cells during corticogenesis |
| GO:0090267 positive regulation of mitotic cell cycle spindle assembly checkpoint | NAS PMID:19229290 Dynein light intermediate chain 1 is required for progress t... | UNDECIDED | Summary: Positive regulation of mitotic cell cycle spindle assembly checkpoint (NAS, LIC1 paper). Reason: The cited paper concerns dynein LIC1, which is required for spindle assembly checkpoint silencing (i.e. removal of checkpoint proteins), the opposite sign to the annotation. DYNLT1 is not mentioned in the cached abstract. Without the curator's basis I cannot evaluate it. Supporting Evidence: PMID:19229290 We conclude that a Cdk1 phosphorylated form of LIC1 is required to remove Mad1/2 and Zw10 but not BubR1 from kinetochores during spindle assembly checkpoint silencing |
| GO:0099503 secretory vesicle | IDA PMID:21262767 Tctex-1, a novel interaction partner of Rab3D, is required f... | KEEP AS NON CORE | Summary: Secretory vesicle (IDA, osteoclast Rab3D vesicles). Reason: Tctex-1 co-occupies Rab3D-bearing vesicles in osteoclasts; cell-type-specific cargo association. Supporting Evidence: PMID:21262767 We demonstrate that Tctex-1 binds specifically to Rab3D in a GTP-dependent manner and co-occupies Rab3D-bearing vesicles in bone-resorbing osteoclasts |
| GO:1904813 ficolin-1-rich granule lumen | TAS Reactome:R-HSA-6800434 | MARK AS OVER ANNOTATED | Summary: Ficolin-1-rich granule lumen (Reactome). Reason: Reactome places DYNLT1 in neutrophil granule/secretion compartments on the basis of granule proteomics. DYNLT1 is a cytosolic dynein light chain with no secretion signal, so these extracellular/granule-lumen locations likely reflect contamination or bystander inclusion rather than a functional location. |
| GO:0061523 cilium disassembly | IMP PMID:21394082 Ciliary transition zone activation of phosphorylated Tctex-1... | NEW | Summary: Thr94-phosphorylated Tctex-1 is recruited to the ciliary transition zone before S-phase entry and promotes ciliary resorption. Reason: Loss-of-function and phospho-mimic gain-of-function both affect cilium disassembly. T94E accelerates disassembly, and the mechanism involves actin dynamics. Recruitment is driven by IGF-1R-AGS3-Gbetagamma signalling at the ciliary base (PMID:23954591). Participation/comparator: DYNLT1 is a signalling effector acting at the transition zone, analogous to the AURKA activator NEDD9, which carries GO:0061523 in human GOA together with AURKA and HDAC6. Saito et al. 2017 (full text) show that phospho-T94 Tctex-1 is required for Cdc42 activation and drives branched-actin-dependent periciliary endocytosis at the onset of resorption. Tctex-1 therefore does part of the work of disassembly rather than only being required for it. The cached 2011 paper is abstract-only. Supporting Evidence: PMID:21394082 We show that Tctex-1 phosphorylated at Thr 94 is recruited to ciliary transition zones before S-phase entry and has a pivotal role in both ciliary disassembly and cell cycle progression PMID:21394082 Exogenously adding a phospho-mimic Tctex-1(T94E) mutant accelerates cilium disassembly and S-phase entry PMID:21394082 Mechanistic studies show the involvement of actin dynamics in Tctex-1-regulated cilium resorption PMID:23954591 At the base of the cilium, phosphorylated IGF-1R activates an AGS3-regulated GΞ²Ξ³ signaling pathway that subsequently recruits phospho(T94)Tctex-1 to the transition zone PMID:28607034 Mechanistically, Tctex-1 physically and functionally interacts with the actin dynamics regulators annexin A2, Arp2/3 complex, and Cdc42. Phospho(T94)Tctex-1 is required for Cdc42 activation before the onset of ciliary resorption PMID:28607034 our results support a model in which phospho(T94)Tctex-1-regulated actin polymerization and periciliary endocytosis play an active role in orchestrating the initial phase of ciliary resorption |
| GO:0035869 ciliary transition zone | IDA PMID:21394082 Ciliary transition zone activation of phosphorylated Tctex-1... | NEW | Summary: Thr94-phosphorylated Tctex-1 is recruited to the ciliary transition zone before S phase. Reason: Direct localization of the phospho-T94 pool (phospho-specific antibody) at transition zones of cultured cells and cortical neural progenitors. Recruitment there depends on IGF-1R/Gbetagamma signalling. This is the site of its ciliary resorption activity. Supporting Evidence: PMID:21394082 We show that Tctex-1 phosphorylated at Thr 94 is recruited to ciliary transition zones before S-phase entry and has a pivotal role in both ciliary disassembly and cell cycle progression PMID:21394082 Tctex-1 phosphorylated at Thr 94 is also selectively enriched at the ciliary transition zones of cortical neural progenitors, and has a key role in controlling G(1) length, cell cycle entry and fate determination of these cells during corticogenesis PMID:23954591 At the base of the cilium, phosphorylated IGF-1R activates an AGS3-regulated GΞ²Ξ³ signaling pathway that subsequently recruits phospho(T94)Tctex-1 to the transition zone file:human/DYNLT1/DYNLT1-deep-research-falcon.md Following Thr94 phosphorylation, DYNLT1 is not associated with the dynein complex. The phosphorylated protein accumulates at the **ciliary transition zone** before S-phase entry. |
Loading supporting contentβ¦
Download this section (compressed HTML)Q: Does phospho-T94 Tctex-1 promote resorption as a free light chain (dynein-independent, Gbetagamma-associated) or within dynein-1/dynein-2 complexes at the transition zone?
Q: How can Tctex-1 depletion both lengthen steady-state cilia and impair serum-induced resorption? Are these the same or separable activities?
Q: Which kinase phosphorylates Tctex-1 at T94 in response to mitogens?
Q: Is DYNLT3 redundant with DYNLT1 in dynein-2 and in ciliary resorption?
Experiment: Knock out DYNLT1 in RPE1 cells and rescue with WT, T94A, T94E and IC-binding-deficient mutants. Measure steady-state cilium length, retrograde IFT and serum-induced resorption separately.
Experiment: Proximity labelling of transition-zone phospho-T94 Tctex-1 to identify partners (Gbetagamma, actin regulators, dynein subunits) during resorption.
Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)