High impact information on SNX17

• Sorting nexin 17 facilitates LRP recycling in the early endosome [1].
• Functional studies on the LDLR pathway showed that SNX17 enhances the endocytosis rate of this receptor [2].
• Sorting nexin 17 (SNX17) has recently been implicated in LDLR intracellular trafficking [3].
• A potential player in this complex endocytic itinerary is SNX17, a member of the sorting nexin family, which has been shown in a yeast two-hybrid assay to bind P-selectin [4].
• The functional part of SNX17 that binds P-selectin or Patched (PTCH) consists of a truncated FERM domain and a unique C terminus together (FC-unit) [5].

Biological context of SNX17

• Using rhodamine-labeled LDL, it was possible to demonstrate that during endocytosis, LDL passes through SNX17-positive compartments [2].
• Our finding suggests a SNX17 involvement in the indicated KRIT1 function in cell adhesion processes by integrin signaling [6].
• KIAA0064 was identified as a putative intracellular P-selectin binding protein [7].

Anatomical context of SNX17

• We show here that endogenous SNX17 is highly expressed in several cell types and is localized partially in early endosomes [3].
• Here, we report that the PX domain of SNX17 specifically binds to phosphatidylinositol 3-phosphate-containing membranes [5].
• Expression of a fusion protein between SNX17 and green fluorescent protein demonstrated localisation of SNX17 in the cytosol and to membranes [7].

Associations of SNX17 with chemical compounds

• By gel filtration and lipid overlay assays we show that SNX17 is a non-self-assembling and a PtdIns(3)P high class affinity protein [6].

Physical interactions of SNX17

• KRIT1 binds SNX17 by its N-terminal region like the known interaction partner ICAP1alpha (integrin cytoplasmic domain-associated protein-1) [6].

Other interactions of SNX17

• The interaction was also detected in HEK 293 cells transiently expressing GFP-tagged KRIT1 and Xpress-tagged SNX17 [6].

References