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Title: Phosphorylation of a synaptic vesicle-associated protein by an inositol hexakisphosphate-regulated protein kinase.
Authors: Hilton, JM
Plomann, M
Ritter, B
Modregger, J
Freeman, HN
Falck, JR
Krishna, UM
Tobin, AB
First Published: 11-May-2001
Citation: J BIOL CHEM, 2001, 276 (19), pp. 16341-16347
Abstract: Despite the fact that inositol hexakisphosphate (InsP(6)) is the most abundant inositol metabolite in cells, its cellular function has remained an enigma. In the present study, we present the first evidence of a protein kinase identified in rat cerebral cortex/hippocampus that is activated by InsP(6). The substrate for the InsP(6)-regulated protein kinase was found to be the synaptic vesicle-associated protein, pacsin/syndapin I. This brain-specific protein, which is highly enriched at nerve terminals, is proposed to act as a molecular link coupling components of the synaptic vesicle endocytic machinery to the cytoskeleton. We show here that the association between pacsin/syndapin I and dynamin I can be increased by InsP(6)-dependent phosphorylation of pacsin/syndapin I. These data provide a model by which InsP(6)-dependent phosphorylation regulates synaptic vesicle recycling by increasing the interaction between endocytic proteins at the synapse.
DOI Link: 10.1074/jbc.M011122200
ISSN: 0021-9258
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Cell Physiology and Pharmacology

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