Ubiquitin carboxyl-terminal hydrolase 10 (USP10) isa hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, BECN1, SNX3 and CFTR []. It regulates the localisation and stability of p53 by de-ubiquitinatiing p53 []. It is also implicated in vesicular transport and trafficking of membrane proteins [].
This entry represents the PX domain found in Sorting nexin-3 (SNX3) from vertebrates. In budding yeasts, Snx3 homologue has been shown to associate with early endosomes through a PX domain-mediated interaction with phosphatidylinositol-3-phosphate (PI3P) []. It associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer. SNX3 is required for the formation of multivesicular bodies, which function as transport intermediates to late endosomes [, ]. It also promotes cell surface expression of the amiloride-sensitive epithelial Na+ channel (ENaC), which is critical in sodium homeostasis and maintenance of extracellular fluid volume [].The Phox Homology (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 phosphoinositides (PIs) and targets the protein to PI-enriched membranes [, ]. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway [, , ].
This entry represents the PX domain found in SNX3 (also known as Grd19) from fungi. Grd19 has been shown to associate with early endosomes through a PX domain-mediated interaction with phosphatidylinositol-3-phosphate (PI3P) []. Grd19 is involved in the localization of late Golgi membrane proteins in yeast. It associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer [].The Phox Homology (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 phosphoinositides (PIs) and targets the protein to PI-enriched membranes [, ]. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway [, , ].
