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A new member of the sorting nexin family interacts with the C-terminus of P-selectin.

Abstract：

:P-selectin is a cell adhesion molecule found in platelets and endothelial cells mediating binding of leukocytes. It is stored in secretory granules and expressed at the plasma membrane after cell activation. After rapid internalisation P-selectin recycles or is degraded. The 35 amino acid cytoplasmic domain of P-selectin contains signals for sorting into secretory granules, for endocytosis and for delivery to lysosomes. To investigate protein-protein interactions, we performed two-hybrid screening using the cytoplasmic domain of P-selectin as bait. KIAA0064 was identified as a putative intracellular P-selectin binding protein. Because the protein contains a phox homology (PX) domain in the N-terminus which is a characteristic feature of the sorting nexin (SNX) family, it was named SNX17. The PX domain is not required for binding of P-selectin in the two-hybrid system. Expression of a fusion protein between SNX17 and green fluorescent protein demonstrated localisation of SNX17 in the cytosol and to membranes.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Florian V,Schlüter T,Bohnensack R

doi

10.1006/bbrc.2001.4467

subject

Has Abstract

pub_date

2001-03-09 00:00:00

pages

1045-50

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(01)94467-5

journal_volume

281

pub_type

杂志文章

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