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Proc Natl Acad Sci U S A. 1989 Oct;86(20):8108-12.

Translocation of synapsin I in response to depolarization of isolated nerve terminals.

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1
Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, NY 10021.

Abstract

Depolarization of isolated nerve terminals (synaptosomes) has been shown to stimulate neurotransmitter release and to increase the phosphorylation state of a number of proteins, including synapsin I, in a Ca2+-dependent manner. Synapsin I, a prominent nerve terminal phosphoprotein, interacts with the cytoplasmic surface of small synaptic vesicles and with cytoskeletal elements in a phosphorylation-dependent manner. In the present study we have found that depolarization of synaptosomes resulted in a rapid (2-5 sec) translocation of synapsin I from the particulate to the cytosolic (soluble) fraction. This translocation of synapsin I correlated with its phosphorylation state and was dependent on the presence of Ca2+ in the incubation medium. The stoichiometry of phosphorylation of soluble synapsin I was considerably higher than that of synapsin I in the particulate fraction, under both basal and depolarizing conditions. These data are consistent with the hypothesis that, in situ, the phosphorylation of synapsin I promotes its translocation from synaptic vesicles/cytoskeleton to the cytosol. This phosphorylation/translocation may be instrumental in regulating the release of neurotransmitter.

PMID:
2510160
PMCID:
PMC298224
[Indexed for MEDLINE]
Free PMC Article
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