A New Member of the Sorting Nexin Family Interacts with the C-Terminus of P-Selectin
| Autor: | Volker Florian, Ralf Bohnensack, Thomas Schlüter |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
DNA
Complementary Recombinant Fusion Proteins Biophysics CHO Cells Plasma protein binding Biology Biochemistry Cytosol Cricetinae Animals Humans Protein Isoforms Luciferases Transport Vesicles Molecular Biology C-terminus Binding protein Sequence Analysis DNA Cell Biology PX domain Fusion protein Peptide Fragments Cell biology P-Selectin Sorting nexin Microscopy Fluorescence Cytoplasm Carrier Proteins Cell activation Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 281:1045-1050 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.2001.4467 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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