DCTN1

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Dynactin 1 (p150, glued homolog, Drosophila)
PDB rendering based on 1txq.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols DCTN1 ; DAP-150; DP-150; P135
External IDs Template:OMIM5 Template:MGI HomoloGene3011
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Dynactin 1 (p150, glued homolog, Drosophila), also known as DCTN1, is a human gene.

This gene encodes the largest subunit of dynactin, a macromolecular complex consisting of 10-11 subunits ranging in size from 22 to 150 kD. Dynactin binds to both microtubules and cytoplasmic dynein. It is involved in a diverse array of cellular functions, including ER-to-Golgi transport, the centripetal movement of lysosomes and endosomes, spindle formation, chromosome movement, nuclear positioning, and axonogenesis. This subunit interacts with dynein intermediate chain by its domains directly binding to dynein. Alternative splicing of this gene results in at least 2 functionally distinct isoforms: a ubiquitously expressed one and a brain-specific one. Based on its cytogenetic location, this gene is considered as a candidate gene for limb-girdle muscular dystrophy.[1]

References

  1. "Entrez Gene: DCTN1 dynactin 1 (p150, glued homolog, Drosophila)".

Further reading

  • Holzbaur EL, Hammarback JA, Paschal BM; et al. (1991). "Homology of a 150K cytoplasmic dynein-associated polypeptide with the Drosophila gene Glued". Nature. 351 (6327): 579–83. doi:10.1038/351579a0. PMID 1828535.
  • Waterman-Storer CM, Karki S, Holzbaur EL (1995). "The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1)". Proc. Natl. Acad. Sci. U.S.A. 92 (5): 1634–8. PMID 7878030.
  • Paschal BM, Holzbaur EL, Pfister KK; et al. (1993). "Characterization of a 50-kDa polypeptide in cytoplasmic dynein preparations reveals a complex with p150GLUED and a novel actin". J. Biol. Chem. 268 (20): 15318–23. PMID 8325901.
  • Vaughan KT, Vallee RB (1996). "Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued". J. Cell Biol. 131 (6 Pt 1): 1507–16. PMID 8522607.
  • Holzbaur EL, Tokito MK (1997). "Localization of the DCTN1 gene encoding p150Glued to human chromosome 2p13 by fluorescence in situ hybridization". Genomics. 31 (3): 398–9. doi:10.1006/geno.1996.0068. PMID 8838327.
  • Tokito MK, Howland DS, Lee VM, Holzbaur EL (1997). "Functionally distinct isoforms of dynactin are expressed in human neurons". Mol. Biol. Cell. 7 (8): 1167–80. PMID 8856662.
  • Sahni M, Zhou XM, Bakiri L; et al. (1997). "Identification of a novel 135-kDa Grb2-binding protein in osteoclasts". J. Biol. Chem. 271 (51): 33141–7. PMID 8955163.
  • Blangy A, Arnaud L, Nigg EA (1997). "Phosphorylation by p34cdc2 protein kinase regulates binding of the kinesin-related motor HsEg5 to the dynactin subunit p150". J. Biol. Chem. 272 (31): 19418–24. PMID 9235942.
  • Korthaus D, Wedemeyer N, Lengeling A; et al. (1997). "Integrated radiation hybrid map of human chromosome 2p13: possible involvement of dynactin in neuromuscular diseases". Genomics. 43 (2): 242–4. doi:10.1006/geno.1997.4789. PMID 9244444.
  • Waterman-Storer CM, Karki SB, Kuznetsov SA; et al. (1997). "The interaction between cytoplasmic dynein and dynactin is required for fast axonal transport". Proc. Natl. Acad. Sci. U.S.A. 94 (22): 12180–5. PMID 9342383.
  • Engelender S, Sharp AH, Colomer V; et al. (1998). "Huntingtin-associated protein 1 (HAP1) interacts with the p150Glued subunit of dynactin". Hum. Mol. Genet. 6 (13): 2205–12. PMID 9361024.
  • Li SH, Gutekunst CA, Hersch SM, Li XJ (1998). "Interaction of huntingtin-associated protein with dynactin P150Glued". J. Neurosci. 18 (4): 1261–9. PMID 9454836.
  • Karki S, LaMonte B, Holzbaur EL (1998). "Characterization of the p22 subunit of dynactin reveals the localization of cytoplasmic dynein and dynactin to the midbody of dividing cells". J. Cell Biol. 142 (4): 1023–34. PMID 9722614.
  • Collin GB, Nishina PM, Marshall JD, Naggert JK (1998). "Human DCTN1: genomic structure and evaluation as a candidate for Alström syndrome". Genomics. 53 (3): 359–64. doi:10.1006/geno.1998.5542. PMID 9799602.
  • Tokito MK, Holzbaur EL (1998). "The genomic structure of DCTN1, a candidate gene for limb-girdle muscular dystrophy (LGMD2B)". Biochim. Biophys. Acta. 1442 (2–3): 432–6. PMID 9805007.
  • Bingham JB, Schroer TA (1999). "Self-regulated polymerization of the actin-related protein Arp1". Curr. Biol. 9 (4): 223–6. PMID 10074429.
  • Heimann K, Percival JM, Weinberger R; et al. (1999). "Specific isoforms of actin-binding proteins on distinct populations of Golgi-derived vesicles". J. Biol. Chem. 274 (16): 10743–50. PMID 10196146.
  • Eckley DM, Gill SR, Melkonian KA; et al. (1999). "Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the arp1 minifilament pointed end". J. Cell Biol. 147 (2): 307–20. PMID 10525537.
  • Karki S, Tokito MK, Holzbaur EL (2000). "A dynactin subunit with a highly conserved cysteine-rich motif interacts directly with Arp1". J. Biol. Chem. 275 (7): 4834–9. PMID 10671518.
  • Vancoillie G, Lambert J, Haeghen YV; et al. (2001). "Colocalization of dynactin subunits P150Glued and P50 with melanosomes in normal human melanocytes". Pigment Cell Res. 13 (6): 449–57. PMID 11153697.

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