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.
journal_name
Proc Natl Acad Sci U S Aauthors
Sihra TS,Wang JK,Gorelick FS,Greengard Pdoi
10.1073/pnas.86.20.8108subject
Has Abstractpub_date
1989-10-01 00:00:00pages
8108-12issue
20eissn
0027-8424issn
1091-6490journal_volume
86pub_type
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