DCTN2

Dynactin 2 (p50)
Identifiers
Symbols	DCTN2; DCTN50; DYNAMITIN; RBP50
External IDs	OMIM: 607376 MGI: 107733 HomoloGene: 4667 GeneCards: DCTN2 Gene
Gene Ontology Molecular function • motor activity • protein binding Cellular component • kinetochore • cytoplasm • centrosome • cytosol • cytoskeleton • dynactin complex • microtubule • membrane • dynein complex • growth cone Biological process • G2/M transition of mitotic cell cycle • mitotic cell cycle • microtubule-based process • mitotic spindle organization • mitosis • cell proliferation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	10540	69654
Ensembl	ENSG00000175203	ENSMUSG00000025410
UniProt	Q13561	Q3TPZ5
RefSeq (mRNA)	NM_006400	NM_027151
RefSeq (protein)	NP_006391	NP_081427
Location (UCSC)	Chr 12: 57.92 – 57.94 Mb	Chr 10: 126.7 – 126.72 Mb
PubMed search	[1]	[2]

Dynactin subunit 2 is a protein that in humans is encoded by the DCTN2 gene.^[1][2]

This gene encodes a 50-kD 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 is present in 4-5 copies per dynactin molecule. It contains three short alpha-helical coiled-coil domains that may mediate association with self or other dynactin subunits. It may interact directly with the largest subunit (p150) of dynactin and may affix p150 in place.^[2]

Interactions

DCTN2 has been shown to interact with MARCKSL1.^[3]

References

1. ^ Echeverri CJ, Paschal BM, Vaughan KT, Vallee RB (Jul 1996). "Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis". J Cell Biol 132 (4): 617–33. doi:10.1083/jcb.132.4.617. PMC 2199864. PMID 8647893. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2199864. 
2. ^ ^{a b} "Entrez Gene: DCTN2 dynactin 2 (p50)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10540. 
3. ^ Yue, L; Lu S, Garces J, Jin T, Li J (Aug. 2000). "Protein kinase C-regulated dynamitin-macrophage-enriched myristoylated alanine-rice C kinase substrate interaction is involved in macrophage cell spreading". J. Biol. Chem. (UNITED STATES) 275 (31): 23948–56. doi:10.1074/jbc.M001845200. ISSN 0021-9258. PMID 10827182. 

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Starr DA, Williams BC, Hays TS, Goldberg ML (1998). "ZW10 helps recruit dynactin and dynein to the kinetochore.". J. Cell Biol. 142 (3): 763–74. doi:10.1083/jcb.142.3.763. PMC 2148168. PMID 9700164. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2148168. 
• Berrueta L, Tirnauer JS, Schuyler SC, et al. (1999). "The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain.". Curr. Biol. 9 (8): 425–8. doi:10.1016/S0960-9822(99)80190-0. PMID 10226031. 
• 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. doi:10.1083/jcb.147.2.307. PMC 2174220. PMID 10525537. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2174220. 
• 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. doi:10.1074/jbc.275.7.4834. PMID 10671518. 
• Merdes A, Heald R, Samejima K, et al. (2000). "Formation of spindle poles by dynein/dynactin-dependent transport of NuMA.". J. Cell Biol. 149 (4): 851–62. doi:10.1083/jcb.149.4.851. PMC 2174573. PMID 10811826. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2174573. 
• Yue L, Lu S, Garces J, et al. (2000). "Protein kinase C-regulated dynamitin-macrophage-enriched myristoylated alanine-rice C kinase substrate interaction is involved in macrophage cell spreading.". J. Biol. Chem. 275 (31): 23948–56. doi:10.1074/jbc.M001845200. PMID 10827182. 
• 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. doi:10.1034/j.1600-0749.2000.130607.x. PMID 11153697. 
• Hoogenraad CC, Akhmanova A, Howell SA, et al. (2001). "Mammalian Golgi-associated Bicaudal-D2 functions in the dynein-dynactin pathway by interacting with these complexes.". EMBO J. 20 (15): 4041–54. doi:10.1093/emboj/20.15.4041. PMC 149157. PMID 11483508. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=149157. 
• Short B, Preisinger C, Schaletzky J, et al. (2003). "The Rab6 GTPase regulates recruitment of the dynactin complex to Golgi membranes.". Curr. Biol. 12 (20): 1792–5. doi:10.1016/S0960-9822(02)01221-6. PMID 12401177. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Uetake Y, Terada Y, Matuliene J, Kuriyama R (2004). "Interaction of Cep135 with a p50 dynactin subunit in mammalian centrosomes.". Cell Motil. Cytoskeleton 58 (1): 53–66. doi:10.1002/cm.10175. PMID 14983524. 
• Brill LM, Salomon AR, Ficarro SB, et al. (2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.". Anal. Chem. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186. 
• Ballif BA, Villén J, Beausoleil SA, et al. (2005). "Phosphoproteomic analysis of the developing mouse brain.". Mol. Cell Proteomics 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• Ficarro SB, Salomon AR, Brill LM, et al. (2005). "Automated immobilized metal affinity chromatography/nano-liquid chromatography/electrospray ionization mass spectrometry platform for profiling protein phosphorylation sites.". Rapid Commun. Mass Spectrom. 19 (1): 57–71. doi:10.1002/rcm.1746. PMID 15570572.