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SEC23A
Introduction
Sec23 homolog A (S. cerevisiae), also known as SEC23A, is a protein which in humans is encoded by the SEC23A gene.[1]
Function
Function
The protein encoded by this gene is a member of the SEC23 subfamily of the SEC23/SEC24 family. It contains a gelsolin domain.[2] It is part of a protein complex and found in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. This protein has similarity to yeast Sec23p component of COPII. COPII is the coat protein complex responsible for vesicle budding from the ER. The encoded protein is suggested to play a role in the ER-Golgi protein trafficking.[1]
Interactions
Interactions
SEC23A has been shown to interact with SEC24C,[3] Sec16A/p250 and iPLA1Ξ²/p125.[4]
Sec23 has also been shown to interact with TRAPPβ , Grh1p also known as GRASP65 and Dynactin. Because they are involved in anterograde vesicle transport from ER to Golgi, Sec23 is involved in vesicle transport.[5]
References
References
- β 1.0 1.1 “Entrez Gene: SEC23A Sec23 homolog A (S. cerevisiae)”.
- β Ghoshdastider, U; Popp, D; Burtnick, L. D.; Robinson, R. C. (2013). “The expanding superfamily of gelsolin homology domain proteins”. Cytoskeleton. 70 (11): 775β95. doi:10.1002/cm.21149. PMIDΒ 24155256.
- β Pagano A, Letourneur F, Garcia-Estefania D, Carpentier JL, Orci L, Paccaud JP (Mar 1999). “Sec24 proteins and sorting at the endoplasmic reticulum”. J. Biol. Chem. 274 (12): 7833β40. doi:10.1074/jbc.274.12.7833. PMIDΒ 10075675.
- β p125 is localized in endoplasmic reticulum exit sites and involved in their organization.
- β Coordination of COPII vesicle trafficking by Sec23.
Further reading
Further reading
- Paccaud JP, Reith W, Carpentier JL, Ravazzola M, Amherdt M, Schekman R, Orci L (1996). “Cloning and functional characterization of mammalian homologues of the COPII component Sec23”. Mol. Biol. Cell. 7 (10): 1535β46. doi:10.1091/mbc.7.10.1535. PMCΒ 276004. PMIDΒ 8898360.
- Pagano A, Letourneur F, Garcia-Estefania D, Carpentier JL, Orci L, Paccaud JP (1999). “Sec24 proteins and sorting at the endoplasmic reticulum”. J. Biol. Chem. 274 (12): 7833β40. doi:10.1074/jbc.274.12.7833. PMIDΒ 10075675.
- Tang BL, Kausalya J, Low DY, Lock ML, Hong W (1999). “A family of mammalian proteins homologous to yeast Sec24p”. Biochem. Biophys. Res. Commun. 258 (3): 679β84. doi:10.1006/bbrc.1999.0574. PMIDΒ 10329445.
- Boyadjiev SA, Justice CM, Eyaid W, McKusick VA, Lachman RS, Chowdry AB, Jabak M, Zwaan J, Wilson AF, Jabs EW (2003). “A novel dysmorphic syndrome with open calvarial sutures and sutural cataracts maps to chromosome 14q13-q21”. Hum. Genet. 113 (1): 1β9. doi:10.1007/s00439-003-0932-6. PMIDΒ 12677423.
- Dudognon P, Maeder-Garavaglia C, Carpentier JL, Paccaud JP (2004). “Regulation of a COPII component by cytosolic O-glycosylation during mitosis”. FEBS Lett. 561 (1β3): 44β50. doi:10.1016/S0014-5793(04)00109-7. PMIDΒ 15013749.
- Watson P, Forster R, Palmer KJ, Pepperkok R, Stephens DJ (2005). “Coupling of ER exit to microtubules through direct interaction of COPII with dynactin”. Nat. Cell Biol. 7 (1): 48β55. doi:10.1038/ncb1206. PMCΒ 1592520. PMIDΒ 15580264.
- Palmer KJ, Konkel JE, Stephens DJ (2005). “PCTAIRE protein kinases interact directly with the COPII complex and modulate secretory cargo transport”. J. Cell Sci. 118 (Pt 17): 3839β47. doi:10.1242/jcs.02496. PMIDΒ 16091426.
- Boyadjiev SA, Fromme JC, Ben J, Chong SS, Nauta C, Hur DJ, Zhang G, Hamamoto S, Schekman R, Ravazzola M, Orci L, Eyaid W (2006). “Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-Golgi trafficking”. Nat. Genet. 38 (10): 1192β7. doi:10.1038/ng1876. PMIDΒ 16980979.
- Tu LC, Yan X, Hood L, Lin B (2007). “Proteomics analysis of the interactome of N-myc downstream regulated gene 1 and its interactions with the androgen response program in prostate cancer cells”. Mol. Cell. Proteomics. 6 (4): 575β88. doi:10.1074/mcp.M600249-MCP200. PMIDΒ 17220478.