Sorting nexins are a large family of evolutionarily conserved phosphoinositide-binding proteins that have roles in cargo sorting through the endosomal netwrok []. Sorting nexins contain at least a PX domain (a phospholipid-binding motif). Some nexins contain a few additional domains. Proteins in the sorting nexin 9 subfamily includes SNX9, SNX18 and SNX33 []. They are characterised by the presence of an N-terminal SH3 domain (), a PX domain that is a phosphoinositide-binding module (), and a Bin/Amphiphysin/Rvs (BAR) domain at the C terminus, which allows membrane binding and bending. They are required for progression and completion of mitosis []. This entry represents SNX18, which acts as a membrane tubulator in AP (adaptor proteins)-1-positive endosomal trafficking []. It has a similar role to SNX9 in endocytic trafficking at the plasma membrane [].
Proteins in the sorting nexin 9 subfamily includes SNX9, SNX18 and SNX33 []. They are characterised by the presence of an N-terminal SH3 domain (), a PX domain that is a phosphoinositide-binding module (), and a Bin/Amphiphysin/Rvs (BAR) domain at the C terminus, which allows membrane binding and bending. They are required for progression and completion of mitosis []. This entry also includes the sorting nexin lst-4 from Caenorhabditis elegans. It is involved in the signalling of vulval development by acting as a negative regulator of epidermal growth factor receptor (EGFR) signaling [].
Sorting nexin-18 (SNX18) is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1 []. It binds FIP5 and is required for apical lumen formation []. It may also play a role in axonal elongation []. SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system [, ]. SNX18 also contains BAR and SH3 domains.This entry represent the SH3 domain of SNX18.
Sorting nexins are a large family of evolutionarily conserved phosphoinositide-binding proteins that have roles in cargo sorting through the endosomal netwrok []. Sorting nexins contain at least a PX domain (a phospholipid-binding motif). Some nexins contain a few additional domains. Proteins in the sorting nexin 9 subfamily includes SNX9, SNX18 and SNX33 []. They are characterised by the presence of an N-terminal SH3 domain (), a PX domain that is a phosphoinositide-binding module (), and a Bin/Amphiphysin/Rvs (BAR) domain at the C terminus, which allows membrane binding and bending. They are required for progression and completion of mitosis []. This entry represents SNX33, which plays a role in maintaining cell shape and cell cycle progression through its interaction with WASp (Wiskott-Aldrich syndrome protein) []. It interferes with cellular prion protein (PrP) formation by modulation of its shedding []. It may also promote the formation of macropinosomes (large endocytic organelles) [].
Sorting nexin-18 (SNX18) is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1 []. It binds FIP5 and is required for apical lumen formation []. It may also play a role in axonal elongation []. SNXs are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system [, ]. SNX18 also contains BAR and SH3 domains.The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes [].
Sorting nexins are a large family of evolutionarily conserved phosphoinositide-binding proteins that have roles in cargo sorting through the endosomal netwrok []. Sorting nexins contain at least a PX domain (a phospholipid-binding motif). Some nexins contain a few additional domains. Proteins in the sorting nexin 9 subfamily includes SNX9, SNX18 and SNX33 []. They are characterised by the presence of an N-terminal SH3 domain (), a PX domain that is a phosphoinositide-binding module (), and a Bin/Amphiphysin/Rvs (BAR) domain at the C terminus, which allows membrane binding and bending. They are required for progression and completion of mitosis []. Sorting nexin 9 (SNX9) is a well-characterised member of this group; it is has been suggested to be involved in the endocytic process as an accessory factor []. SNX9 has binding sites for both clathrin and adaptor protein AP-2 in a low complexity region, and binds dynamin-2 (Dyn2) by its SH3 domain. SNX9 has its own membrane-binding activity, mediated by a carboxyl-terminal region containing the PX domain and the BAR domain []. Endogenous SNX9 partially co-localizes with AP-2 and Dyn2 at the plasma membrane, and over expression in K562 and HeLa cells of truncated versions of SNX9 inhibits the uptake of transferrin []. Moreover, SNX9 is required for efficient clathrin-mediated endocytosis, which suggests that it functions to regulate dynamin activity [].
Sorting nexins are a large family of evolutionarily conserved phosphoinositide-binding proteins that have roles in cargo sorting through the endosomal netwrok []. Sorting nexins contain at least a PX domain (a phospholipid-binding motif). Some nexins contain a few additional domains. Proteins in the sorting nexin 9 subfamily includes SNX9, SNX18 and SNX33 []. They are characterised by the presence of an N-terminal SH3 domain (), a PX domain that is a phosphoinositide-binding module (), and a Bin/Amphiphysin/Rvs (BAR) domain at the C terminus, which allows membrane binding and bending. They are required for progression and completion of mitosis []. SNX33 plays a role in maintaining cell shape and cell cycle progression through its interaction with WASp (Wiskott-Aldrich syndrome protein) []. It interferes with cellular prion protein (PrP) formation by modulation of its shedding []. It may also promote the formation of macropinosomes (large endocytic organelles) []. This entry represents the BAR domain of SNX33. BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions [].
