SNX9

Sorting nexin 9

Rendering based on PDB 2RAI.

Available structures
PDB	2RAI, 2RAJ, 2RAK, 3DYT, 3DYU, 3LGE

Identifiers

Symbols

SNX9; MST155; MSTP155; SDP1; SH3PX1; SH3PXD3A; WISP

External IDs

OMIM: 605952 MGI: 1913866 HomoloGene: 49454 GeneCards: SNX9 Gene

Gene Ontology
Molecular function	• protein binding • 1-phosphatidylinositol binding • lipid binding • ubiquitin protein ligase binding • protein homodimerization activity
Cellular component	• ruffle • intracellular • cytoplasm • Golgi apparatus • trans-Golgi network • plasma membrane • cytoplasmic membrane-bounded vesicle • clathrin-coated vesicle • cytoplasmic vesicle membrane • extrinsic to internal side of plasma membrane
Biological process	• intracellular protein transport • receptor-mediated endocytosis • cell communication • positive regulation of protein oligomerization • positive regulation of GTPase activity • lipid tube assembly
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 6:
158.24 – 158.37 Mb

Chr 17:
5.84 – 5.93 Mb

PubMed search

[1]

[2]

Sorting nexin-9 is a protein that in humans is encoded by the SNX9 gene.^[1]^[2]^[3]

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 protein does not contain a coiled coil region, like some family members, but does contain an SH3 domain near its N-terminus. This protein interacts with the cytoplasmic domains of the precursor but not the processed forms of a disintegrin and metalloprotease domain 9 and 15. This protein binds the beta-appendage domain of adaptor protein 2 and may function to assist adaptor protein 2 in its role at the plasma membrane. This protein interacts with activated Cdc42-associated kinase-2 to regulate the degradation of epidermal growth factor receptor protein.^[3]

Interactions

SNX9 has been shown to interact with ADAM9,^[1] DNM2^[4] and ADAM15.^[1]

References

^ ^a ^b ^c Howard L, Nelson KK, Maciewicz RA, Blobel CP (Dec 1999). "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1". J Biol Chem 274 (44): 31693–9. doi:10.1074/jbc.274.44.31693. PMID 10531379.
^ Yarar D, Waterman-Storer CM, Schmid SL (Jul 2007). "SNX9 couples actin assembly to phosphoinositide signals and is required for membrane remodeling during endocytosis". Dev Cell 13 (1): 43–56. doi:10.1016/j.devcel.2007.04.014. PMID 17609109.
^ ^a ^b "Entrez Gene: SNX9 sorting nexin 9". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51429.
^ Lundmark, Richard; Carlsson Sven R (Nov. 2003). "Sorting nexin 9 participates in clathrin-mediated endocytosis through interactions with the core components". J. Biol. Chem. (United States) 278 (47): 46772–81. doi:10.1074/jbc.M307334200. ISSN 0021-9258. PMID 12952949.

Teasdale RD, Loci D, Houghton F, et al. (2001). "A large family of endosome-localized proteins related to sorting nexin 1.". Biochem. J. 358 (Pt 1): 7–16. doi:10.1042/0264-6021:3580007. PMC 1222026. PMID 11485546. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222026.
Lin Q, Lo CG, Cerione RA, Yang W (2002). "The Cdc42 target ACK2 interacts with sorting nexin 9 (SH3PX1) to regulate epidermal growth factor receptor degradation.". J. Biol. Chem. 277 (12): 10134–8. doi:10.1074/jbc.M110329200. PMID 11799118.
Lundmark R, Carlsson SR (2002). "The beta-appendages of the four adaptor-protein (AP) complexes: structure and binding properties, and identification of sorting nexin 9 as an accessory protein to AP-2.". Biochem. J. 362 (Pt 3): 597–607. doi:10.1042/0264-6021:3620597. PMC 1222423. PMID 11879186. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222423.
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.
Lundmark R, Carlsson SR (2004). "Sorting nexin 9 participates in clathrin-mediated endocytosis through interactions with the core components.". J. Biol. Chem. 278 (47): 46772–81. doi:10.1074/jbc.M307334200. PMID 12952949.
Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6.". Nature 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
Schulze WX, Mann M (2004). "A novel proteomic screen for peptide-protein interactions.". J. Biol. Chem. 279 (11): 10756–64. doi:10.1074/jbc.M309909200. PMID 14679214.
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.
Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation.". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=442147.
Lundmark R, Carlsson SR (2004). "Regulated membrane recruitment of dynamin-2 mediated by sorting nexin 9.". J. Biol. Chem. 279 (41): 42694–702. doi:10.1074/jbc.M407430200. PMID 15299020.
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.
Soulet F, Yarar D, Leonard M, Schmid SL (2005). "SNX9 regulates dynamin assembly and is required for efficient clathrin-mediated endocytosis.". Mol. Biol. Cell 16 (4): 2058–67. doi:10.1091/mbc.E04-11-1016. PMC 1073683. PMID 15703209. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1073683.
Yeow-Fong L, Lim L, Manser E (2005). "SNX9 as an adaptor for linking synaptojanin-1 to the Cdc42 effector ACK1.". FEBS Lett. 579 (22): 5040–8. doi:10.1016/j.febslet.2005.07.093. PMID 16137687.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Childress C, Lin Q, Yang W (2006). "Dimerization is required for SH3PX1 tyrosine phosphorylation in response to epidermal growth factor signalling and interaction with ACK2.". Biochem. J. 394 (Pt 3): 693–8. doi:10.1042/BJ20050576. PMC 1383719. PMID 16316319. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1383719.
Marchès O, Batchelor M, Shaw RK, et al. (2006). "EspF of enteropathogenic Escherichia coli binds sorting nexin 9.". J. Bacteriol. 188 (8): 3110–5. doi:10.1128/JB.188.8.3110-3115.2006. PMC 1447016. PMID 16585770. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1447016.
Schmid EM, Ford MG, Burtey A, et al. (2007). "Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly.". PLoS Biol. 4 (9): e262. doi:10.1371/journal.pbio.0040262. PMC 1540706. PMID 16903783. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1540706.
Badour K, McGavin MK, Zhang J, et al. (2007). "Interaction of the Wiskott-Aldrich syndrome protein with sorting nexin 9 is required for CD28 endocytosis and cosignaling in T cells.". Proc. Natl. Acad. Sci. U.S.A. 104 (5): 1593–8. doi:10.1073/pnas.0610543104. PMC 1785243. PMID 17242350. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1785243.

Sorting nexins

SNX-BAR	SNX1 · SNX2 · SNX4 · SNX5 · SNX6 · SNX7 · SNX8 · SNX9 · SNX18 · SNX30 · SNX32 · SNX33

SNX-PX	SNX3 · SNX10 · SNX11 · SNX12 · SNX16 · SNX20 · SNX21 · SNX22 · SNX24 · SNX29

SNX-Other	SNX13 · SNX14 · SNX15 · SNX17 · SNX19 · SNX23 · SNX25 · SNX26 · SNX27 · SNX28 · SNX31

Related articles	PX domain · BAR domain · Retromer

B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

SNX9

Interactions

References

Further reading