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• W2148489566 abstract "Rab27a and Rab27b have recently been recognized to play versatile roles in regulating the exocytosis of secretory granules and lysosome-related organelles by using multiple effector proteins. However, the precise roles of these effector proteins in particular cell types largely remain uncharacterized, except for those in pancreatic β cells and in melanocytes. Here, we showed that one of the Rab27a/b effectors, exophilin4/Slp2-a, is specifically expressed in pancreatic α cells, in contrast to another effector, granuphilin, in β cells. Like granuphilin toward insulin granules, exophilin4 promotes the targeting of glucagon granules to the plasma membrane. Although the interaction of granuphilin with syntaxin-1a is critical for the targeting activity, exophilin4 does this primarily through the affinity of its C2A domain toward the plasma membrane phospholipids phosphatidylserine and phosphatidylinositol-4,5-bisphosphate. Notably, the binding activity to phosphatidylserine is inhibited by a physiological range of the Ca 2+ concentration attained after secretagogue stimulation, which presents a striking contrast to the Ca 2+ -stimulatory activity of the C2A domain of synaptotagmin I. Analyses of the mutant suggested that this novel Ca 2+ -inhibitory phospholipid-binding activity not only mediates docking but also modulates the subsequent fusion of the secretory granules." @default.
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• W2148489566 date "2007-02-01" @default.
• W2148489566 modified "2023-09-26" @default.
• W2148489566 title "Exophilin4/Slp2-a Targets Glucagon Granules to the Plasma Membrane through Unique Ca²⁺-inhibitory Phospholipid-binding Activity of the C2A Domain" @default.
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• W2148489566 doi "https://doi.org/10.1091/mbc.e06-10-0914" @default.
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