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- W2006874662 abstract "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 Ca(2+)-dependent F-actin-severing protein) potentiated Ca(2+)-evoked F-actin disassembly and exocytosis in permeabilized chromaffin cells, an effect blocked by peptides Sc-ABP1 and Sc-ABP2 (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 scinderin254-715 (lacking actin-severing domains) did not potentiate exocytosis. Sc-ABP1, Sc-ABP2, 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." @default.
- W2006874662 created "2016-06-24" @default.
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- W2006874662 date "1996-08-01" @default.
- W2006874662 modified "2023-10-13" @default.
- W2006874662 title "Recombinant Scinderin Enhances Exocytosis, an Effect Blocked by Two Scinderin-Derived Actin-Binding Peptides and PIP2" @default.
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- W2006874662 doi "https://doi.org/10.1016/s0896-6273(00)80160-9" @default.
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