SNX1

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.[5] SNX1 is a component of the retromer complex.[6][7]

SNX1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2I4K, 4FZS
Identifiers
Aliases	SNX1, HsT17379, VPS5, sorting nexin 1
External IDs	OMIM: 601272 MGI: 1928395 HomoloGene: 99716 GeneCards: SNX1
Gene location (Human) Chr. Chromosome 15 (human)[1] Band 15q22.31 Start 64,094,123 bp[1] End 64,146,090 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9|9 C Start 66,088,133 bp[2] End 66,126,587 bp[2]
Gene ontology Molecular function • protein homodimerization activity • insulin receptor binding • leptin receptor binding • epidermal growth factor receptor binding • GO:0001948 protein binding • phosphatidylinositol binding • identical protein binding • protein heterodimerization activity • transferrin receptor binding • lipid binding • cadherin binding Cellular component • cytoplasm • cytosol • Golgi apparatus • cell projection • early endosome membrane • membrane • retromer, tubulation complex • intracellular membrane-bounded organelle • Retromer • early endosome • endosome membrane • lamellipodium • extrinsic component of membrane • vesicle • lysosome • endosome • macromolecular complex Biological process • positive regulation of protein catabolic process • vesicle organization • early endosome to Golgi transport • receptor internalization • endosomal transport • retrograde transport, endosome to Golgi • protein transport • intracellular protein transport • lamellipodium morphogenesis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6642	56440
Ensembl	ENSG00000028528	ENSMUSG00000032382
UniProt	Q13596	Q9WV80
RefSeq (mRNA)	NM_001242933 NM_003099 NM_148955 NM_152826	NM_019727
RefSeq (protein)	NP_001229862 NP_003090 NP_683758	NP_062701
Location (UCSC)	Chr 15: 64.09 – 64.15 Mb	Chr 9: 66.09 – 66.13 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000028528 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000032382 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. Vergés M (2008). Retromer: multipurpose sorting and specialization in polarized transport. Int Rev Cell Mol Biol. International Review of Cell and Molecular Biology. 271. pp. 153–98. doi:10.1016/S1937-6448(08)01204-5. ISBN 9780123747280. PMID 19081543.
7. 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.
8. "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. hdl:11336/31768. 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.