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.
^ abcHoward 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 Chem274 (44): 31693–9. doi:10.1074/jbc.274.44.31693. PMID10531379.
^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 Cell13 (1): 43–56. doi:10.1016/j.devcel.2007.04.014. PMID17609109.
^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. ISSN0021-9258. PMID12952949.
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. PMID11799118.
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. PMID12952949.