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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Sorting nexin 17 accelerates internalization yet retards degradation of P-selectin.

The transient appearance of P-selectin on the surface of endothelial cells helps recruit leukocytes into sites of inflammation. The tight control of cell surface P-selectin on these cells depends on regulated exocytosis of Weibel-Palade bodies where the protein is stored and on its rapid endocytosis. After endocytosis, P-selectin is either sorted via endosomes and the Golgi apparatus for storage in Weibel-Palade bodies or targeted to lysosomes for degradation. 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. Here, we show that overexpression of SNX17 in mammalian cells can influence two key steps in the endocytic trafficking of P-selectin. First, it promotes the endocytosis of P-selectin from the plasma membrane. Second, it inhibits the movement of P-selectin into lysosomes, thereby reducing its degradation.[1]

References

  1. Sorting nexin 17 accelerates internalization yet retards degradation of P-selectin. Williams, R., Schlüter, T., Roberts, M.S., Knauth, P., Bohnensack, R., Cutler, D.F. Mol. Biol. Cell (2004) [Pubmed]
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