The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Human DCTN1 (UniProt Q14203): Functional Annotation Research Report

Executive summary

The requested identity is verified: human DCTN1 encodes dynactin subunit 1, conventionally called p150Glued (also DP-150/DAP-150), the largest subunit and projecting arm of the dynactin complex. The literature’s p150Glued protein, human gene symbol DCTN1, N-terminal CAP-Gly/basic microtubule-binding module, coiled-coil architecture, and shorter p135 isoform all agree with the supplied UniProt Q14203 record. No conflicting same-symbol protein was encountered. (cianfrocco2015mechanismandregulation pages 11-12, liu2017regulationofdynein‐dynactin‐driven pages 38-41, mishima2024perrydiseasebench pages 4-5)

DCTN1 is not an enzyme or transporter. It is a non-catalytic structural and regulatory component of the cytoplasmic dynein transport machinery. Its central function is to organize dynactin, bind microtubules and plus-end proteins, engage dynein and regulators, and promote assembly and activation of processive dynein–dynactin–cargo-adaptor complexes. Dynein supplies ATP hydrolysis and force; DCTN1 supplies scaffolding, microtubule engagement, assembly control, and transport initiation. (doerksen2025sacylationofneuronal pages 23-28, cianfrocco2015mechanismandregulation pages 11-12, singh2024molecularmechanismof pages 1-3)

Table: Compact evidence-based annotation of human DCTN1/Q14203, integrating molecular structure, localization, transport pathways, 2024 mechanistic advances and clinical relevance. Caveats distinguish direct p150Glued evidence from findings attributable to the broader dynein–dynactin machinery.

1. Identity, nomenclature, and molecular class

DCTN1/p150Glued is the largest dynactin subunit and forms a homodimeric arm extending from dynactin’s shoulder. Older biochemical descriptions call it the 150-kDa dynein-associated polypeptide; literature also distinguishes a shorter p135 species. The retrieved sources independently support the DCTN1–p150Glued identity but did not independently validate every sequence-level feature or exact isoform length in UniProt Q14203. (cianfrocco2015mechanismandregulation pages 11-12, liu2017regulationofdynein‐dynactin‐driven pages 38-41, mishima2024perrydiseasebench pages 4-5)

Vertebrate dynactin has been described as an approximately 1.2-MDa complex containing 23 polypeptides, organized around an approximately 40-nm Arp1-based filament. More recent structural work describes dynactin as approximately 1.1 MDa within an active dynein–dynactin–adaptor assembly of approximately 4 MDa; the difference reflects context and measurement/description rather than a functional contradiction. (cianfrocco2015mechanismandregulation pages 11-12, singh2024molecularmechanismof pages 1-3)

2. Domain architecture and structure–function relationships

N-terminal CAP-Gly/basic microtubule-binding module

The N terminus contains the supplied-record CAP-Gly domain and an adjacent serine-rich basic region. Together they mediate microtubule binding. CAP-Gly domains recognize C-terminal aromatic EEY/F-like motifs found on tyrosinated α-tubulin and microtubule plus-end proteins such as EB1 and CLIP-170. The basic region further increases microtubule engagement and can increase the time that dynein–dynactin remains associated with the microtubule. (doerksen2025sacylationofneuronal pages 23-28, liu2017regulationofdynein‐dynactin‐driven pages 5-8, barbosa2017dynactinbindingto pages 28-29)

This module is especially important for initiating transport rather than maintaining every subsequent step of processive motion. In neurons, CAP-Gly-dependent recruitment at distal microtubule ends promotes the initiation of retrograde transport; evidence reviewed in the retrieved literature indicates that CAP-Gly can be less critical after sustained movement has begun. (liu2017regulationofdynein‐dynactin‐driven pages 5-8, doerksen2025sacylationofneuronal pages 23-28)

Coiled coils and dynactin integration

The p150 arm contains CC1A, CC1B, an inter-coiled-coil domain, CC2, and a C-terminal dynactin-association region. CC1 participates in dynein intermediate-chain binding; CC2 and distal regions contribute to adaptor interactions and organization of the dynactin shoulder/arm. The C terminus anchors p150 in the dynactin complex. (doerksen2025sacylationofneuronal pages 23-28, cianfrocco2015mechanismandregulation pages 11-12)

The supplied DUF8221 annotation is not assigned a comparably precise independent biochemical activity in the retrieved literature. Its safest annotation is therefore as part of the conserved dynactin-family structural architecture rather than as an autonomous catalytic domain.

3. Primary molecular function: assembly and activation of dynein transport complexes

Cytoplasmic dynein alone is often weakly processive or autoinhibited. Dynactin plus a cargo-specific activating adaptor—examples include BICD2, Hook proteins, Spindly-family adaptors, Rab11-FIP3, and JIP3—converts dynein into a highly processive minus-end-directed motor complex. DCTN1 is the principal elongated dynactin subunit that links microtubule engagement to dynein and adaptor assembly. (cianfrocco2015mechanismandregulation pages 11-12, liu2017regulationofdynein‐dynactin‐driven pages 41-44, singh2024molecularmechanismof pages 1-3)

2024 mechanistic advance: p150–LIS1 cooperation

A March 2024 Science study used microtubule-bound cryo-EM, pull-down assays, cellular mitochondrial-relocation assays, and in-vitro motility to define how LIS1 and p150 promote active-complex assembly. DCTN1/p150 changes from a folded autoinhibited conformation to an open state. Binding of the dynein intermediate-chain N terminus, DIC-N, destabilizes the CC1A/CC1B hairpin and inter-coiled-coil-domain contacts. Exposed CC1B then binds the dynein motor and the LIS1 N-terminal region, whereas LIS1 WD40 domains bind the dynein motor. This tethers and orients dynein beneath the p150 arm for productive adaptor engagement. (singh2024molecularmechanismof pages 37-40, singh2024molecularmechanismof pages 9-11, singh2024molecularmechanismof pages 6-8)

The structure mapped DIC-N contacts to p150 residues 458–478 and dynein-motor contacts to residues 480–521, including contacts with dynein AAA2 and AAA3. The opened configuration directs the p150 CAP-Gly/basic N terminus toward the microtubule. These observations establish p150 as an actively regulated assembly scaffold, not merely a passive dynein tether. Singh et al., published March 2024, DOI. (singh2024molecularmechanismof pages 9-11, singh2024molecularmechanismof pages 4-6)

The same work showed that JIP3’s RH1/LZI-containing N-terminal region can activate dynein–dynactin. A previously unrecognized JIP3 LYHEL Spindly motif, residues 382–386, binds the dynactin pointed end; motif mutation disrupted pointed-end binding. Because this work used a reconstituted JIP3 complex, its exact structural sequence should not automatically be generalized to every cargo adaptor, although the p150-opening principle is likely broader. (singh2024molecularmechanismof pages 4-6, singh2024molecularmechanismof pages 32-37)

4. Cellular localization and site of action

DCTN1 acts principally in the cytoplasm on the microtubule cytoskeleton and in dynein–dynactin–cargo assemblies. Particularly well-supported locations are:

• Growing microtubule plus ends: EB1/EB3 and CLIP-170 recruit p150/dynactin and dynein, creating sites for cargo capture and transport initiation. Reconstitution supports sequential EB1/CLIP-170-dependent recruitment. (liu2017regulationofdynein‐dynactin‐driven pages 5-8)
• Distal axons and synaptic termini: dynactin is enriched in distal neurites, where p150’s CAP-Gly module facilitates assembly/initiation of retrograde transport toward the soma. (liu2017regulationofdynein‐dynactin‐driven pages 5-8, doerksen2025sacylationofneuronal pages 23-28)
• Cargo-associated membranes: p150-containing complexes participate in movement of endosomes, lysosomes, autophagosomes, mitochondria, signaling endosomes, Golgi/ER carriers, and other vesicles. Direct cargo attachment is often mediated by activating adaptors or other dynactin subunits, so these should be annotated as dynein–dynactin locations rather than as proof that p150 independently binds every membrane. (liu2017regulationofdynein‐dynactin‐driven pages 41-44, liu2017regulationofdynein‐dynactin‐driven pages 38-41)
• Kinetochores and spindle-associated structures: dynactin recruits dynein to kinetochores and contributes to spindle organization and chromosome-associated transport. The overall pathway is well established, but some localization evidence applies to dynactin as a complex rather than isolated human p150. (dutta2019roleofdynein pages 2-3, cianfrocco2015mechanismandregulation pages 11-12)
• Centrosome-organizing pathways: CAP-Gly binding to tyrosinated microtubules enhanced centripetal organelle transport and centrosome centration in genome-edited C. elegans embryos. This is compelling conserved mechanistic evidence, although not a direct human-cell localization experiment. Barbosa et al., published July 2017, DOI. (barbosa2017dynactinbindingto pages 28-29)

5. Biological processes and pathways

Retrograde axonal transport

The best-defined specialized role is initiation and support of fast retrograde axonal transport. In mouse dorsal-root-ganglion neurons and fly motor neurons, EB proteins recruit CLIP-170, which recruits p150/dynactin at distal microtubules. This facilitates soma-directed movement of early and late endosomes, mitochondria, and neurotrophin-signaling endosomes. (liu2017regulationofdynein‐dynactin‐driven pages 5-8)

Fast axonal transport is commonly reported at approximately 1 μm/s, potentially reaching approximately 400 mm/day, but these values characterize the broader motor-transport system and are not intrinsic catalytic rates for DCTN1. (doerksen2025sacylationofneuronal pages 19-23)

Endolysosomal and autophagy pathways

DCTN1-containing dynactin complexes participate in Rab7–RILP/HPS6-dependent late-endosome and lysosome movement, JIP3-associated lysosomal transport, LC3–JIP1-linked autophagosome transport, and transport-dependent autophagosome maturation. Minus-end-directed movement brings distal autophagosomes and endolysosomal cargo toward perinuclear or somatic degradative compartments. (liu2017regulationofdynein‐dynactin‐driven pages 41-44, liu2017regulationofdynein‐dynactin‐driven pages 38-41)

This is a transport/positioning role rather than lysosomal enzymatic activity. DCTN1 has no known transported molecular “substrate” analogous to a membrane transporter; its cargo repertoire is determined by adaptors and organelle-specific small-GTPase pathways.

Secretory and endosomal sorting pathways

Reported p150-containing pathways include Rab6–Bicaudal-D-dependent Golgi/secretory traffic, SNX5/SNX6-dependent endosome-to-trans-Golgi transport, Sec23-associated COPII/ER export, and signaling-receptor endosomal transport involving EGFR, TrkA/TrkB, and APP-associated carriers. Attribution should generally be to the dynein–dynactin machinery unless a direct p150 interaction was experimentally demonstrated. (liu2017regulationofdynein‐dynactin‐driven pages 41-44, liu2017regulationofdynein‐dynactin‐driven pages 38-41)

Mitosis and cellular organization

Dynactin supports dynein recruitment to kinetochores, spindle-pole-directed movement, centrosome positioning, and organelle-generated cytoplasmic pulling forces. CAP-Gly/tubulin-tyrosination mutants reduce the frequency of centripetal organelle movement and impair centrosome centration in dividing embryos, linking microtubule recognition directly to force-generating cellular organization. (dutta2019roleofdynein pages 2-3, barbosa2017dynactinbindingto pages 28-29, cianfrocco2015mechanismandregulation pages 11-12)

6. Disease mechanisms and genotype–phenotype relationships

Established Mendelian disorders

Dominant DCTN1 variants cause Perry disease/syndrome and distal hereditary motor neuropathy type 7B (HMN7B). Perry disease typically combines parkinsonism, depression or apathy, weight loss, and central hypoventilation or sleep-related respiratory dysfunction. It is neuropathologically classified as a TDP-43 proteinopathy. Most Perry-associated substitutions cluster in the N-terminal microtubule-binding region, emphasizing the functional importance of CAP-Gly/basic-domain interactions. Mishima et al., published January 2024, DOI. (mishima2024perrydiseasebench pages 4-5, mishima2024perrydiseasebench pages 2-4)

Reported genotype examples include p.G59S in HMN7B; p.G59R in distal motor neuropathy/ALS phenotypes; p.Q93H in motor-neuron and Perry phenotypes; and Perry-associated p.F52L, p.G67D, and p.G71E. Distinct variants can therefore perturb the same molecular module yet produce different neuronal vulnerabilities. HMN7B pathology may feature dynactin/p50-positive aggregates without the characteristic TDP-43 pathology of Perry disease. (mishima2024perrydiseasebench pages 4-5, mishima2024perrydiseasebench pages 2-4, flores‑lagunes2024firstfamilywith pages 6-7)

A June 2024 report described the first recorded Mexican Perry family and identified NM_004082:c.212G>A, p.Gly71Glu by exome sequencing. The variant had previously been reported in at least four Perry cases of differing backgrounds. Structural modeling suggested that the larger, charged glutamate side chain could alter CAP-Gly conformation and partner interactions, but this remains a modeled mechanism rather than direct biochemical proof. Flores-Lagunes et al., published June 2024, DOI. (flores‑lagunes2024firstfamilywith pages 6-7)

TDP-43 and stress-granule biology

A February 2024 study found that DCTN1 deficiency delayed stress-granule disassembly and increased ubiquitin-positive cytoplasmic TDP-43 inclusions in cultured cells and human-TDP-43 Drosophila models, exacerbating neurodegeneration. Dynein or kinesin perturbation produced related effects, indicating that disrupted bidirectional microtubule transport—not necessarily a DCTN1-only pathway—can destabilize stress-granule dynamics. Ueda et al., published February 2024, DOI. (ueda2024dysregulationofstress pages 1-2)

The study is mechanistically important because TDP-43 pathology is estimated to occur in almost all ALS cases and approximately half of FTD cases; TDP-43-positive inclusions also occur in Perry disease, especially in the substantia nigra, globus pallidus, and brainstem. Nevertheless, knockdown in flies is not equivalent to a heterozygous human CAP-Gly missense variant, and validation in patient-derived neurons and longitudinal human tissue is still needed. (ueda2024dysregulationofstress pages 1-2)

Strength of broader disease associations

Open Targets identifies literature-supported associations with ALS, neurodegenerative disease, Perry syndrome, HMN7B, and cancer. The retrieved association scores include approximately 0.87 for neurodegenerative disease, 0.80 for ALS, 0.80 for Perry syndrome, and 0.74 for HMN7B. These are database evidence-integration scores—not prevalence, penetrance, effect sizes, or proof that DCTN1 is a therapeutic target in every listed disease. (OpenTargets Search: -DCTN1)

7. Current applications and real-world implementation

The clearest current applications are:

1. Genetic diagnosis and counseling. Exome or panel sequencing can identify pathogenic DCTN1 variants and distinguish Perry disease or HMN7B from overlapping parkinsonian, respiratory, motor-neuron, and frontotemporal syndromes. The 2024 Mexican-family report illustrates direct diagnostic implementation. (mishima2024perrydiseasebench pages 2-4, flores‑lagunes2024firstfamilywith pages 6-7)
2. Neuropathological classification. DCTN1 genotype, dynactin aggregation, regional neuronal loss, and the pattern of TDP-43 inclusions help separate Perry disease from HMN7B and other TDP-43 proteinopathies. (mishima2024perrydiseasebench pages 4-5, mishima2024perrydiseasebench pages 2-4)
3. Patient-derived and animal models. p.F52L patient-derived iPSC dopaminergic neurons develop cytoplasmic dynactin aggregates, while fly and mouse models are used to connect transport failure to TDP-43, stress granules, ER abnormalities, and selective neuronal degeneration. The iPSC phenotype only partially recapitulates the human disease. (mishima2024perrydiseasebench pages 4-5, ueda2024dysregulationofstress pages 13-14, ueda2024dysregulationofstress pages 14-15)
4. Mechanistic reconstitution. Purified dynein–dynactin–adaptor complexes and cryo-EM are used to define motor activation, adaptor recognition, and LIS1-dependent assembly at residue-level resolution. (singh2024molecularmechanismof pages 1-3, singh2024molecularmechanismof pages 4-6)

No DCTN1-specific approved drug or established variant-directed therapy was identified in the gathered evidence. Current Perry-disease care remains diagnostic and supportive, while therapeutic concepts aimed at restoring transport, improving proteostasis, or modulating TDP-43/stress-granule clearance remain experimental.

8. Expert interpretation and annotation confidence

The strongest defensible primary annotation is:

DCTN1 encodes the p150Glued structural/regulatory arm of dynactin, which binds microtubules and plus-end proteins, engages dynein and LIS1, and promotes adaptor-dependent assembly, transport initiation, and processive minus-end-directed movement of diverse cellular cargoes.

Three distinctions are important:

• Motor versus activator: DCTN1 does not hydrolyze ATP to move cargo; cytoplasmic dynein is the ATPase motor.
• Direct p150 function versus complex-level function: microtubule binding, p150 conformational opening, DIC/LIS1 engagement, and distal transport initiation are directly assignable to DCTN1. Many organelle and mitotic functions are established for dynactin as a whole and should not be over-annotated as independent p150–cargo interactions.
• Transport initiation versus sustained motion: the CAP-Gly/basic region strongly influences plus-end targeting and initiation, whereas processive motion after assembly also depends on dynein, the dynactin Arp1 scaffold, and cargo adaptors. (singh2024molecularmechanismof pages 9-11, liu2017regulationofdynein‐dynactin‐driven pages 5-8, doerksen2025sacylationofneuronal pages 23-28)

9. Evidence limitations and research priorities

The 2024 structural work is highly authoritative but examines selected reconstituted adaptor states; live-cell studies are needed to determine how frequently the same p150-opening sequence occurs across endogenous cargoes. Disease models frequently use knockdown, overexpression, or non-human systems and may not reproduce dominant, variant-specific human biology. Finally, the field needs quantitative comparisons of how individual CAP-Gly variants alter tyrosinated-tubulin affinity, plus-end residence, DIC/LIS1 assembly, cargo-specific motility, and neuronal survival in isogenic human neurons. (singh2024molecularmechanismof pages 37-40, singh2024molecularmechanismof pages 4-6, ueda2024dysregulationofstress pages 1-2)

Key recent sources

• Singh K. et al. “Molecular mechanism of dynein-dynactin complex assembly by LIS1.” Science. March 2024. https://doi.org/10.1126/science.adk8544. (singh2024molecularmechanismof pages 1-3)
• Ueda T. et al. “Dysregulation of stress granule dynamics by DCTN1 deficiency exacerbates TDP-43 pathology in Drosophila models of ALS/FTD.” Acta Neuropathologica Communications. February 2024. https://doi.org/10.1186/s40478-024-01729-8. (ueda2024dysregulationofstress pages 1-2)
• Mishima T. et al. “Perry Disease: Bench to Bedside Circulation and a Team Approach.” Biomedicines 12:113. January 2024. https://doi.org/10.3390/biomedicines12010113. (mishima2024perrydiseasebench pages 4-5)
• Flores-Lagunes L. et al. “First family with Perry syndrome from Mexico.” Biomedical Reports. June 2024. https://doi.org/10.3892/br.2024.1808. (flores‑lagunes2024firstfamilywith pages 6-7)
• Cianfrocco M.A. et al. “Mechanism and regulation of cytoplasmic dynein.” Annual Review of Cell and Developmental Biology 31:83–108. November 2015. https://doi.org/10.1146/annurev-cellbio-100814-125438. (cianfrocco2015mechanismandregulation pages 11-12)
• Liu J.-J. “Regulation of dynein-dynactin-driven vesicular transport.” Traffic 18:336–347. June 2017. https://doi.org/10.1111/tra.12475. (liu2017regulationofdynein‐dynactin‐driven pages 41-44)

References

1. (cianfrocco2015mechanismandregulation pages 11-12): Michael A. Cianfrocco, Morgan E. DeSantis, Andres E. Leschziner, and Samara L. Reck-Peterson. Mechanism and regulation of cytoplasmic dynein. Annual review of cell and developmental biology, 31:83-108, Nov 2015. URL: https://doi.org/10.1146/annurev-cellbio-100814-125438, doi:10.1146/annurev-cellbio-100814-125438. This article has 315 citations and is from a domain leading peer-reviewed journal.

2. (liu2017regulationofdynein‐dynactin‐driven pages 38-41): Jia‐Jia Liu. Regulation of dynein‐dynactin‐driven vesicular transport. Traffic, 18:336-347, Jun 2017. URL: https://doi.org/10.1111/tra.12475, doi:10.1111/tra.12475. This article has 72 citations and is from a peer-reviewed journal.

3. (mishima2024perrydiseasebench pages 4-5): Takayasu Mishima, Junichi Yuasa-Kawada, Shinsuke Fujioka, and Yoshio Tsuboi. Perry disease: bench to bedside circulation and a team approach. Biomedicines, 12:113, Jan 2024. URL: https://doi.org/10.3390/biomedicines12010113, doi:10.3390/biomedicines12010113. This article has 7 citations.

4. (doerksen2025sacylationofneuronal pages 23-28): A Doerksen. S-acylation of neuronal transport machinery: a focused exploration of p150glued s-acylation in neurons. Unknown journal, 2025.

5. (singh2024molecularmechanismof pages 1-3): Kashish Singh, Clinton K. Lau, Giulia Manigrasso, José B. Gama, Reto Gassmann, and Andrew P. Carter. Molecular mechanism of dynein-dynactin complex assembly by lis1. Mar 2024. URL: https://doi.org/10.1126/science.adk8544, doi:10.1126/science.adk8544. This article has 93 citations and is from a highest quality peer-reviewed journal.

6. (liu2017regulationofdynein‐dynactin‐driven pages 5-8): Jia‐Jia Liu. Regulation of dynein‐dynactin‐driven vesicular transport. Traffic, 18:336-347, Jun 2017. URL: https://doi.org/10.1111/tra.12475, doi:10.1111/tra.12475. This article has 72 citations and is from a peer-reviewed journal.

7. (barbosa2017dynactinbindingto pages 28-29): Daniel J. Barbosa, Joana Duro, Bram Prevo, Dhanya K. Cheerambathur, Ana X. Carvalho, and Reto Gassmann. Dynactin binding to tyrosinated microtubules promotes centrosome centration in c. elegans by enhancing dynein-mediated organelle transport. PLOS Genetics, 13:e1006941, Jul 2017. URL: https://doi.org/10.1371/journal.pgen.1006941, doi:10.1371/journal.pgen.1006941. This article has 53 citations and is from a domain leading peer-reviewed journal.

8. (singh2024molecularmechanismof pages 37-40): Kashish Singh, Clinton K. Lau, Giulia Manigrasso, José B. Gama, Reto Gassmann, and Andrew P. Carter. Molecular mechanism of dynein-dynactin complex assembly by lis1. Mar 2024. URL: https://doi.org/10.1126/science.adk8544, doi:10.1126/science.adk8544. This article has 93 citations and is from a highest quality peer-reviewed journal.

9. (singh2024molecularmechanismof pages 9-11): Kashish Singh, Clinton K. Lau, Giulia Manigrasso, José B. Gama, Reto Gassmann, and Andrew P. Carter. Molecular mechanism of dynein-dynactin complex assembly by lis1. Mar 2024. URL: https://doi.org/10.1126/science.adk8544, doi:10.1126/science.adk8544. This article has 93 citations and is from a highest quality peer-reviewed journal.

10. (singh2024molecularmechanismof pages 6-8): Kashish Singh, Clinton K. Lau, Giulia Manigrasso, José B. Gama, Reto Gassmann, and Andrew P. Carter. Molecular mechanism of dynein-dynactin complex assembly by lis1. Mar 2024. URL: https://doi.org/10.1126/science.adk8544, doi:10.1126/science.adk8544. This article has 93 citations and is from a highest quality peer-reviewed journal.

11. (singh2024molecularmechanismof pages 4-6): Kashish Singh, Clinton K. Lau, Giulia Manigrasso, José B. Gama, Reto Gassmann, and Andrew P. Carter. Molecular mechanism of dynein-dynactin complex assembly by lis1. Mar 2024. URL: https://doi.org/10.1126/science.adk8544, doi:10.1126/science.adk8544. This article has 93 citations and is from a highest quality peer-reviewed journal.

12. (liu2017regulationofdynein‐dynactin‐driven pages 41-44): Jia‐Jia Liu. Regulation of dynein‐dynactin‐driven vesicular transport. Traffic, 18:336-347, Jun 2017. URL: https://doi.org/10.1111/tra.12475, doi:10.1111/tra.12475. This article has 72 citations and is from a peer-reviewed journal.

13. (doerksen2025sacylationofneuronal pages 19-23): A Doerksen. S-acylation of neuronal transport machinery: a focused exploration of p150glued s-acylation in neurons. Unknown journal, 2025.

14. (dutta2019roleofdynein pages 2-3): Rajib Dutta and Swatilekha Roy Sarkar. Role of dynein and dynactin (dctn-1) in neurodegenerative diseases. ArXiv, pages 53-58, Dec 2641. URL: https://doi.org/10.33805/2641-8991.123, doi:10.33805/2641-8991.123. This article has 1 citations.

15. (singh2024molecularmechanismof pages 32-37): Kashish Singh, Clinton K. Lau, Giulia Manigrasso, José B. Gama, Reto Gassmann, and Andrew P. Carter. Molecular mechanism of dynein-dynactin complex assembly by lis1. Mar 2024. URL: https://doi.org/10.1126/science.adk8544, doi:10.1126/science.adk8544. This article has 93 citations and is from a highest quality peer-reviewed journal.

16. (mishima2024perrydiseasebench pages 2-4): Takayasu Mishima, Junichi Yuasa-Kawada, Shinsuke Fujioka, and Yoshio Tsuboi. Perry disease: bench to bedside circulation and a team approach. Biomedicines, 12:113, Jan 2024. URL: https://doi.org/10.3390/biomedicines12010113, doi:10.3390/biomedicines12010113. This article has 7 citations.

17. (flores‑lagunes2024firstfamilywith pages 6-7): Leonardo Flores‑Lagunes, Luis Del Pozo‑Yauner, Karol Carrillo‑Sánchez, Carolina Molina‑Garay, Marco Jiménez‑Olivares, Joaquin Garcia‑Solorio, Ulises Rodríguez Corona, Guillermo Herrera, Edgar Ricardez‑Marcial, and Carmen Alaez‑verson. First family with perry syndrome from mexico. Biomedical Reports, Jun 2024. URL: https://doi.org/10.3892/br.2024.1808, doi:10.3892/br.2024.1808. This article has 2 citations and is from a peer-reviewed journal.

18. (OpenTargets Search: -DCTN1): Open Targets Query (-DCTN1, 5 results). Buniello, A. et al. (2025). Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery. Nucleic Acids Research.

19. (ueda2024dysregulationofstress pages 1-2): Tetsuhiro Ueda, Toshihide Takeuchi, Nobuhiro Fujikake, Mari Suzuki, Eiko N. Minakawa, Morio Ueyama, Yuzo Fujino, Nobuyuki Kimura, Seiichi Nagano, Akio Yokoseki, Osamu Onodera, Hideki Mochizuki, Toshiki Mizuno, Keiji Wada, and Yoshitaka Nagai. Dysregulation of stress granule dynamics by dctn1 deficiency exacerbates tdp-43 pathology in drosophila models of als/ftd. Acta Neuropathologica Communications, Feb 2024. URL: https://doi.org/10.1186/s40478-024-01729-8, doi:10.1186/s40478-024-01729-8. This article has 22 citations and is from a peer-reviewed journal.

20. (ueda2024dysregulationofstress pages 13-14): Tetsuhiro Ueda, Toshihide Takeuchi, Nobuhiro Fujikake, Mari Suzuki, Eiko N. Minakawa, Morio Ueyama, Yuzo Fujino, Nobuyuki Kimura, Seiichi Nagano, Akio Yokoseki, Osamu Onodera, Hideki Mochizuki, Toshiki Mizuno, Keiji Wada, and Yoshitaka Nagai. Dysregulation of stress granule dynamics by dctn1 deficiency exacerbates tdp-43 pathology in drosophila models of als/ftd. Acta Neuropathologica Communications, Feb 2024. URL: https://doi.org/10.1186/s40478-024-01729-8, doi:10.1186/s40478-024-01729-8. This article has 22 citations and is from a peer-reviewed journal.

21. (ueda2024dysregulationofstress pages 14-15): Tetsuhiro Ueda, Toshihide Takeuchi, Nobuhiro Fujikake, Mari Suzuki, Eiko N. Minakawa, Morio Ueyama, Yuzo Fujino, Nobuyuki Kimura, Seiichi Nagano, Akio Yokoseki, Osamu Onodera, Hideki Mochizuki, Toshiki Mizuno, Keiji Wada, and Yoshitaka Nagai. Dysregulation of stress granule dynamics by dctn1 deficiency exacerbates tdp-43 pathology in drosophila models of als/ftd. Acta Neuropathologica Communications, Feb 2024. URL: https://doi.org/10.1186/s40478-024-01729-8, doi:10.1186/s40478-024-01729-8. This article has 22 citations and is from a peer-reviewed journal.

Artifacts

• Edison artifact artifact-00

Citations

1. cianfrocco2015mechanismandregulation pages 11-12
2. barbosa2017dynactinbindingto pages 28-29
3. doerksen2025sacylationofneuronal pages 19-23
4. ueda2024dysregulationofstress pages 1-2
5. singh2024molecularmechanismof pages 1-3
6. mishima2024perrydiseasebench pages 4-5
7. doerksen2025sacylationofneuronal pages 23-28
8. singh2024molecularmechanismof pages 37-40
9. singh2024molecularmechanismof pages 9-11
10. singh2024molecularmechanismof pages 6-8
11. singh2024molecularmechanismof pages 4-6
12. dutta2019roleofdynein pages 2-3
13. singh2024molecularmechanismof pages 32-37
14. mishima2024perrydiseasebench pages 2-4
15. ueda2024dysregulationofstress pages 13-14
16. ueda2024dysregulationofstress pages 14-15
17. 2015 DOI
18. 2024 DOI
19. Science, March 2024
20. 2017 DOI
21. Traffic review, June 2017
22. June 2024 DOI
23. February 2024 DOI
24. January 2024 review
25. June 2024 report
26. Singh et al., published March 2024, DOI
27. Barbosa et al., published July 2017, DOI
28. Mishima et al., published January 2024, DOI
29. Flores-Lagunes et al., published June 2024, DOI
30. Ueda et al., published February 2024, DOI
31. https://doi.org/10.1146/annurev-cellbio-100814-125438
32. https://doi.org/10.3390/biomedicines12010113
33. https://doi.org/10.1126/science.adk8544
34. https://doi.org/10.1371/journal.pgen.1006941
35. https://doi.org/10.1111/tra.12475
36. https://doi.org/10.3892/br.2024.1808
37. https://doi.org/10.1186/s40478-024-01729-8
38. https://doi.org/10.1126/science.adk8544.
39. https://doi.org/10.1186/s40478-024-01729-8.
40. https://doi.org/10.3390/biomedicines12010113.
41. https://doi.org/10.3892/br.2024.1808.
42. https://doi.org/10.1146/annurev-cellbio-100814-125438.
43. https://doi.org/10.1111/tra.12475.
44. https://doi.org/10.1146/annurev-cellbio-100814-125438,
45. https://doi.org/10.1111/tra.12475,
46. https://doi.org/10.3390/biomedicines12010113,
47. https://doi.org/10.1126/science.adk8544,
48. https://doi.org/10.1371/journal.pgen.1006941,
49. https://doi.org/10.33805/2641-8991.123,
50. https://doi.org/10.3892/br.2024.1808,
51. https://doi.org/10.1186/s40478-024-01729-8,