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Activity‐dependent control of bulk endocytosis by protein dephosphorylation in central nerve terminals
Author(s) -
Clayton Emma L.,
Evans Gareth J. O.,
Cousin Michael A.
Publication year - 2007
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2007.137539
Subject(s) - endocytosis , bulk endocytosis , dephosphorylation , exocytosis , dynamin , microbiology and biotechnology , synaptic vesicle , chemistry , phosphatase , synaptic vesicle recycling , phosphorylation , endocytic cycle , gtpase , biophysics , biology , vesicle , biochemistry , membrane , receptor
Bulk endocytosis is the process by which nerve terminals retrieve large amounts of synaptic vesicle membrane during periods of strong stimulation intensity. The process is rapidly activated and is most probably calcium dependent in a similar manner to synaptic vesicle exocytosis. This article briefly summarizes the current knowledge of bulk endocytosis with respect to its activation, kinetics and molecular mechanism. It also presents recent data from our laboratory showing that the dephosphorylation of a group of endocytosis proteins called the dephosphins by the Ca 2+ ‐dependent protein phosphatase calcineurin is key to the activity‐dependent stimulation of the process. Possible downstream effectors of calcineurin are discussed such as the large GTPase dynamin I and its phosphorylation‐dependent interaction partner syndapin I.