Autor: |
STEEL, Gregor J., BUCHHEIM, Georg, EDWARDSON, J. Michael, WOODMAN, Philip G. |
Zdroj: |
Biochemical Journal; July 1997, Vol. 325 Issue: 2 p511-518, 8p |
Abstrakt: |
α-SNAP [soluble N-ethylmaleimide-sensitive fusion protein (NSF)-attachment protein] is required for fusion of transport vesicles with their target membrane. In this study, we have examined the membrane-binding properties of α-SNAP. We have found that in several tissues a much larger amount of α-SNAP per unit weight of protein is bound to membranes than is free in the cytosol. Biochemical analysis shows that a fraction of α-SNAP behaves in ways characteristic of hydrophobic, lipid-associated proteins. These findings suggest that membrane binding may be accounted for, at least in part, by interaction with membrane lipid. Consistent with this idea, binding of newly synthesized α-SNAP to brain membranes was found to be independent of functional SNAP receptors and could be accounted for by direct binding of α-SNAP to membrane lipid. Furthermore, membrane lipid enhanced the ability of α-SNAP to stimulate NSF-dependent ATPase activity. |
Databáze: |
Supplemental Index |
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