Recombinant scinderin enhances exocytosis, an effect blocked by two scinderin-derived actin-binding peptides and PIP2

被引:67
作者
Zhang, L
Marcu, MG
NauStaudt, K
Trifaro, JM
机构
[1] Secretory Process Research Program, Department of Pharmacology, University of Ottawa, Ottawa
基金
英国医学研究理事会;
关键词
D O I
10.1016/S0896-6273(00)80160-9
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
The cortical F-actin cytoskeleton represents a negative control for secretion, and it must be locally disassembled to allow chromaffin vesicle exocytosis. Recombinant scinderin (a Ca2+-dependent F-actin-severing protein) potentiated Ca2+-evoked F-actin disassembly and exocytosis in permeabilized chromaffin cells, an effect blocked by peptides Sc-ABP(1) and Sc-ABP(2) (with sequences corresponding to two actin-binding sites of scinderin), exogenous gamma-actin, or phosphatidylinositol 4,5-bisphosphate (PIP2) PIP2 effect was blocked by peptide Sc-PIP2BP (with sequence corresponding to a PIP2-binding site of scinderin). Truncated scinderin(254-715) (lacking actin-severing domains) did not potentiate exocytosis. Sc-ABP(1), Sc-ABP(2), and gamma-actin also inhibited exocytosis in the absence of recombinant scinderin, suggesting an inhibition of endogenous scinderin. Results suggest that scinderin-evoked cortical F-actin disassembly is required for secretion and that scinderin is an important component of the exocytotic machinery.
引用
收藏
页码:287 / 296
页数:10
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