DCTN2
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Template:Short description Template:Cs1 config An Error has occurred retrieving Wikidata item for infobox Dynactin subunit 2 is a protein that in humans is encoded by the DCTN2 gene.[1][2]
Function
This gene encodes a 50-kD subunit of dynactin, a macromolecular complex consisting of 23 subunits (11 individual proteins ranging in size from 22 to 150 kD).[3] The subunit is commonly referred to as p50 or dynamitin.[1] 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 four copies per dynactin molecule. It contains three short alpha-helical coiled-coil domains that bind to two copies of p150-glued (DCTN1) and two copies of p24 (DCTN3) to form the dynactin shoulder domain.[3]
Interactions
DCTN2 has been shown to interact with MARCKSL1.[4]
References
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- ^ a b Page Module:Citation/CS1/styles.css has no content.Echeverri CJ, Paschal BM, Vaughan KT, Vallee RB (February 1996). "Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis". The Journal of Cell Biology. 132 (4): 617–33. doi:10.1083/jcb.132.4.617. PMC 2199864. PMID 8647893.
- ^ Page Module:Citation/CS1/styles.css has no content."Entrez Gene: DCTN2 dynactin 2 (p50)".
- ^ a b Page Module:Citation/CS1/styles.css has no content.Urnavicius L, Zhang K, Diamant AG, Motz C, Schlager MA, Yu M, Patel NA, Robinson CV, Carter AP (March 2015). "The structure of the dynactin complex and its interaction with dynein". Science. 347 (6229): 1441–1446. Bibcode:2015Sci...347.1441U. doi:10.1126/science.aaa4080. PMC 4413427. PMID 25814576.
- ^ Page Module:Citation/CS1/styles.css has no content.Yue L, Lu S, Garces J, Jin T, Li J (August 2000). "Protein kinase C-regulated dynamitin-macrophage-enriched myristoylated alanine-rice C kinase substrate interaction is involved in macrophage cell spreading". The Journal of Biological Chemistry. 275 (31): 23948–56. doi:10.1074/jbc.M001845200. PMID 10827182.
Further reading
Page Template:Refbegin/styles.css has no content.
- Page Module:Citation/CS1/styles.css has no content.Maruyama K, Sugano S (January 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.
- Page Module:Citation/CS1/styles.css has no content.Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 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.
- Page Module:Citation/CS1/styles.css has no content.Starr DA, Williams BC, Hays TS, Goldberg ML (August 1998). "ZW10 helps recruit dynactin and dynein to the kinetochore". The Journal of Cell Biology. 142 (3): 763–74. doi:10.1083/jcb.142.3.763. PMC 2148168. PMID 9700164.
- Page Module:Citation/CS1/styles.css has no content.Berrueta L, Tirnauer JS, Schuyler SC, Pellman D, Bierer BE (April 1999). "The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain". Current Biology. 9 (8): 425–8. Bibcode:1999CBio....9..425B. doi:10.1016/S0960-9822(99)80190-0. PMID 10226031. S2CID 14191776.
- Page Module:Citation/CS1/styles.css has no content.Eckley DM, Gill SR, Melkonian KA, Bingham JB, Goodson HV, Heuser JE, Schroer TA (October 1999). "Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the arp1 minifilament pointed end". The Journal of Cell Biology. 147 (2): 307–20. doi:10.1083/jcb.147.2.307. PMC 2174220. PMID 10525537.
- Page Module:Citation/CS1/styles.css has no content.Karki S, Tokito MK, Holzbaur EL (February 2000). "A dynactin subunit with a highly conserved cysteine-rich motif interacts directly with Arp1". The Journal of Biological Chemistry. 275 (7): 4834–9. doi:10.1074/jbc.275.7.4834. PMID 10671518.
- Page Module:Citation/CS1/styles.css has no content.Merdes A, Heald R, Samejima K, Earnshaw WC, Cleveland DW (May 2000). "Formation of spindle poles by dynein/dynactin-dependent transport of NuMA". The Journal of Cell Biology. 149 (4): 851–62. doi:10.1083/jcb.149.4.851. PMC 2174573. PMID 10811826.
- Page Module:Citation/CS1/styles.css has no content.Yue L, Lu S, Garces J, Jin T, Li J (August 2000). "Protein kinase C-regulated dynamitin-macrophage-enriched myristoylated alanine-rice C kinase substrate interaction is involved in macrophage cell spreading". The Journal of Biological Chemistry. 275 (31): 23948–56. doi:10.1074/jbc.M001845200. PMID 10827182.
- Page Module:Citation/CS1/styles.css has no content.Vancoillie G, Lambert J, Haeghen YV, Westbroek W, Mulder A, Koerten HK, Mommaas AM, Van Oostveldt P, Naeyaert JM (December 2000). "Colocalization of dynactin subunits P150Glued and P50 with melanosomes in normal human melanocytes". Pigment Cell Research. 13 (6): 449–57. doi:10.1034/j.1600-0749.2000.130607.x. PMID 11153697.
- Page Module:Citation/CS1/styles.css has no content.Hoogenraad CC, Akhmanova A, Howell SA, Dortland BR, De Zeeuw CI, Willemsen R, Visser P, Grosveld F, Galjart N (August 2001). "Mammalian Golgi-associated Bicaudal-D2 functions in the dynein-dynactin pathway by interacting with these complexes". The EMBO Journal. 20 (15): 4041–54. doi:10.1093/emboj/20.15.4041. PMC 149157. PMID 11483508.
- Page Module:Citation/CS1/styles.css has no content.Short B, Preisinger C, Schaletzky J, Kopajtich R, Barr FA (October 2002). "The Rab6 GTPase regulates recruitment of the dynactin complex to Golgi membranes". Current Biology. 12 (20): 1792–5. Bibcode:2002CBio...12.1792S. doi:10.1016/S0960-9822(02)01221-6. PMID 12401177. S2CID 14031165.
- Page Module:Citation/CS1/styles.css has no content.Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
- Page Module:Citation/CS1/styles.css has no content.Uetake Y, Terada Y, Matuliene J, Kuriyama R (May 2004). "Interaction of Cep135 with a p50 dynactin subunit in mammalian centrosomes". Cell Motility and the Cytoskeleton. 58 (1): 53–66. doi:10.1002/cm.10175. PMID 14983524.
- Page Module:Citation/CS1/styles.css has no content.Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC (May 2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Analytical Chemistry. 76 (10): 2763–72. doi:10.1021/ac035352d. PMID 15144186.
- Page Module:Citation/CS1/styles.css has no content.Ballif BA, Villén J, Beausoleil SA, Schwartz D, Gygi SP (November 2004). "Phosphoproteomic analysis of the developing mouse brain". Molecular & Cellular Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
- Page Module:Citation/CS1/styles.css has no content.Ficarro SB, Salomon AR, Brill LM, Mason DE, Stettler-Gill M, Brock A, Peters EC (2005). "Automated immobilized metal affinity chromatography/nano-liquid chromatography/electrospray ionization mass spectrometry platform for profiling protein phosphorylation sites". Rapid Communications in Mass Spectrometry. 19 (1): 57–71. Bibcode:2005RCMS...19...57F. doi:10.1002/rcm.1746. PMID 15570572.
