SNX1
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Sorting nexin-1 is a protein that in humans is encoded by the SNX1 gene. The protein encoded by this gene is a sorting nexin.[3] SNX1 is a component of the retromer complex.[4][5]
Function
This gene encodes a member of the sorting nexin family. Members of this family contain a phox (PX) domain, which is a phosphoinositide binding domain, and are involved in intracellular trafficking. This endosomal protein regulates the cell-surface expression of epidermal growth factor receptor. This protein also has a role in sorting protease-activated receptor-1 from early endosomes to lysosomes. This protein may form oligomeric complexes with other family members.[6]
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ Kurten RC, Cadena DL, Gill GN (May 1996). "Enhanced degradation of EGF receptors by a sorting nexin, SNX1". Science. 272 (5264): 1008–10. doi:10.1126/science.272.5264.1008. PMID 8638121.
- ↑ Vergés M (2008). "Retromer: multipurpose sorting and specialization in polarized transport". Int Rev Cell Mol Biol. 271: 153–98. doi:10.1016/S1937-6448(08)01204-5. PMID 19081543.
- ↑ Bonifacino JS, Hurley JH (August 2008). "Retromer". Curr. Opin. Cell Biol. 20 (4): 427–36. doi:10.1016/j.ceb.2008.03.009. PMC 2833274. PMID 18472259.
- ↑ "Entrez Gene: sorting nexin 1".
Further reading
- Parks WT, Frank DB, Huff C, et al. (2001). "Sorting nexin 6, a novel SNX, interacts with the transforming growth factor-beta family of receptor serine-threonine kinases.". J. Biol. Chem. 276 (22): 19332–9. doi:10.1074/jbc.M100606200. PMID 11279102.
- Cozier GE, Carlton J, McGregor AH, et al. (2002). "The phox homology (PX) domain-dependent, 3-phosphoinositide-mediated association of sorting nexin-1 with an early sorting endosomal compartment is required for its ability to regulate epidermal growth factor receptor degradation.". J. Biol. Chem. 277 (50): 48730–6. doi:10.1074/jbc.M206986200. PMID 12198132.
- Shank BB, Wiley HS, Kurten RC (2001). "Structural and functional characterization of the human gene for sorting nexin 1 (SNX1).". DNA Cell Biol. 20 (5): 287–96. doi:10.1089/104454901750232481. PMID 11410165.
- Liu H, Liu ZQ, Chen CX, et al. (2006). "Inhibitory regulation of EGF receptor degradation by sorting nexin 5.". Biochem. Biophys. Res. Commun. 342 (2): 537–46. doi:10.1016/j.bbrc.2006.01.179. PMID 16487940.
- Bryant DM, Kerr MC, Hammond LA, et al. (2007). "EGF induces macropinocytosis and SNX1-modulated recycling of E-cadherin.". J. Cell. Sci. 120 (Pt 10): 1818–28. doi:10.1242/jcs.000653. PMID 17502486.
- Simpson F, Martin S, Evans TM, et al. (2005). "A novel hook-related protein family and the characterization of hook-related protein 1.". Traffic. 6 (6): 442–58. doi:10.1111/j.1600-0854.2005.00289.x. PMID 15882442.
- Imabayashi H, Mori T, Gojo S, et al. (2003). "Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis.". Exp. Cell Res. 288 (1): 35–50. doi:10.1016/S0014-4827(03)00130-7. PMID 12878157.
- Zhong Q, Watson MJ, Lazar CS, et al. (2005). "Determinants of the endosomal localization of sorting nexin 1.". Mol. Biol. Cell. 16 (4): 2049–57. doi:10.1091/mbc.E04-06-0504. PMC 1073682. PMID 15673616.
- Mari M, Bujny MV, Zeuschner D, et al. (2008). "SNX1 defines an early endosomal recycling exit for sortilin and mannose 6-phosphate receptors.". Traffic. 9 (3): 380–93. doi:10.1111/j.1600-0854.2007.00686.x. PMID 18088323.
- Nguyen LN, Holdren MS, Nguyen AP, et al. (2006). "Sorting nexin 1 down-regulation promotes colon tumorigenesis.". Clin. Cancer Res. 12 (23): 6952–9. doi:10.1158/1078-0432.CCR-06-0317. PMID 17145813.
- Pons V, Hullin-Matsuda F, Nauze M, et al. (2003). "Enterophilin-1, a new partner of sorting nexin 1, decreases cell surface epidermal growth factor receptor.". J. Biol. Chem. 278 (23): 21155–61. doi:10.1074/jbc.M211008200. PMID 12657642.
- Rojas R, Kametaka S, Haft CR, Bonifacino JS (2007). "Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors.". Mol. Cell. Biol. 27 (3): 1112–24. doi:10.1128/MCB.00156-06. PMC 1800681. PMID 17101778.
- Gullapalli A, Wolfe BL, Griffin CT, et al. (2006). "An essential role for SNX1 in lysosomal sorting of protease-activated receptor-1: evidence for retromer-, Hrs-, and Tsg101-independent functions of sorting nexins.". Mol. Biol. Cell. 17 (3): 1228–38. doi:10.1091/mbc.E05-09-0899. PMC 1382312. PMID 16407403.
- 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.
- Zhong Q, Lazar CS, Tronchère H, et al. (2002). "Endosomal localization and function of sorting nexin 1.". Proc. Natl. Acad. Sci. U.S.A. 99 (10): 6767–72. doi:10.1073/pnas.092142699. PMC 124477. PMID 11997453.
- Wang Y, Zhou Y, Szabo K, et al. (2002). "Down-regulation of protease-activated receptor-1 is regulated by sorting nexin 1.". Mol. Biol. Cell. 13 (6): 1965–76. doi:10.1091/mbc.E01-11-0131. PMC 117618. PMID 12058063.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "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.
- Carlton J, Bujny M, Peter BJ, et al. (2004). "Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides.". Curr. Biol. 14 (20): 1791–800. doi:10.1016/j.cub.2004.09.077. PMID 15498486.
- Kurten RC, Eddington AD, Chowdhury P, et al. (2001). "Self-assembly and binding of a sorting nexin to sorting endosomes.". J. Cell. Sci. 114 (Pt 9): 1743–56. PMID 11309204.
External links
- sorting nexins at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.