Sorting nexin-5/6/32 (IPR014637)

Short name: SNX5/SNX6/SNX32

Overlapping homologous superfamilies

Family relationships


Sorting nexins (SNXs) are a diverse group of cellular trafficking proteins that are unified by the presence of a phospholipid-binding motif, the PX domain. The ability of these proteins to bind specific phospholipids, as well as their propensity to form protein-protein complexes, points to a role for these proteins in membrane trafficking and protein sorting [PMID: 12461558]. Members of this group also contain coiled-coil regions within their large C-terminal domains and a BAR domain, whose function has been defined as a dimerisation motif, as sensing and inducing membrane curvature, and/or likely to bind to small GTPases [PMID: 14993925].

This entry includes SNX5, SNX6 and SNX32 (also known as SNX6B).

SNX5 contains a BAR domain that is C teminus to the PX domain. SNX5 plays a role in macropinocytosis [PMID: 18854019] and in the internalisation of EGFR after EGF stimulation [PMID: 21048941].

SNX6 was found to interact with members of the transforming growth factor-beta family of receptor serine/threonine kinases. Strong heteromeric interactions were also seen among SNX1, -2, -4, and -6, suggesting the formation in vivo of oligomeric complexes. SNX6 is localized in the cytoplasm where it is thought to target proteins to the trans-Golgi network [PMID: 11279102]. In addition, SNX6 was found to be translocated from the cytoplasm to nucleus by Pim-1, an oncogene product of serine/threonine kinase. This translocation is not affected by Pim-1-dependent phosphorylation, but the functional significance is unknown [PMID: 11591366].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.