Sorting nexin-2 (SNX2) belongs to the sorting nexin family, which contains a conserved PX (phox homology) domain that is responsible for binding to specific phosphoinositides []. SNX1 and SNX2 are orthologues of yeast Vps5, which is a component of retromercomplex that is essential in endosome-to-Golgi retrograde transport []. The mammalian retromer complex is composed of the SNX1/2 alternative heterodimer or homodimer and the a Vps26-Vps29-Vps35 obligate heterotrimer []. Like SNX1, SNX2 also has an additional C-terminal BAR domain. SNX1 and SNX2 play interchangeable but essential roles in retromer structure and function [].
Sorting nexin-2 (SNX2) belongs to the sorting nexin family, which contains a conserved PX (phox homology) domain that is responsible for binding to specific phosphoinositides []. SNX1 and SNX2 are orthologues of yeast Vps5, which is a component of retromer complex that is essential in endosome-to-Golgi retrograde transport []. The mammalian retromer complex is composed of the SNX1/2 alternative heterodimer or homodimer and the a Vps26-Vps29-Vps35 obligate heterotrimer []. Like SNX1, SNX2 also has an additional C-terminal BAR domain. SNX1 and SNX2 play interchangeable but essential roles in retromer structure and function [].This entry represents the PX domain of SNX2.
Sorting nexin-1 (SNX1) belongs to the sorting nexin family, which contains a conserved PX (phox homology) domain that is responsible for binding to specific phosphoinositides []. SNX1 and SNX2 are orthologues of yeast Vps5, which is a component of retromer complex that is essential in endosome-to-Golgi retrograde transport []. The mammalian retromer complex is composed of the SNX1/SNX2 alternative heterodimer or homodimer and the Vps26-Vps29-Vps35 obligate heterotrimer []. Like SNX2, SNX1 also has an additional C-terminal BAR domain. SNX1 and SNX2 play interchangeable but essential roles in retromer structure and function [].SNX1 may have a role in sensing membrane curvature and inducing the formation of tubules [, ].
Sorting nexins (SNXs) are hydrophilic molecules that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domains () or through protein-protein interactions with membrane-associated protein complexes []. Indeed, several of the SNXs require several targeting motifs for their appropriate cellular localization. In almost every case studied, mammalian SNXs can be shown to have a role in protein sorting, with the most commonly used experimental model being plasma-membrane receptor endocytosis and sorting through the endosomal pathway. However, it is equally probable that SNXs sort vesicles that are not derived from the plasma membrane, and have a function in the accurate targeting of these vesicles and their cargo. The N-terminal domain appears to be specific to sorting nexins 1 and 2. SNX1 and SNX2 are members of the retromer complex involved in protein sorting within the endocytic pathway []. SNX1 is both membrane-associated and cytosolic, where it probably exists as a tetramer in large protein complexes and may hetero-oligomerize with SNX2.
