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LOCALIZATION OF SH‐PTP1 TO SYNAPTIC VESICLES: A POSSIBLE ROLE IN NEUROTRANSMISSION
Author(s) -
JENA BHANU P.,
WEBSTER PAUL,
GEIBEL JOHN P.,
POL ANTHONY N.,
SRITHARAN KUMUDESH C.
Publication year - 1997
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.1997.0185
Subject(s) - synaptophysin , synaptic vesicle , neurotransmission , tyrosine , neurotransmitter , microbiology and biotechnology , tyrosine kinase , tyrosine phosphorylation , phosphorylation , proto oncogene tyrosine protein kinase src , biology , vesicle , chemistry , biochemistry , neuroscience , signal transduction , central nervous system , receptor , immunology , membrane , immunohistochemistry
The tyrosine kinase pp60 src is known to phosphorylate synaptophysin and in doing so may regulate neurotransmitter release. The tyrosyl phosphorylated state of synaptophysin is dependent on pp60 src kinase and the unknown protein tyrosine phosphate phosphohydrolase (PTPase, EC 3.1.3.48). Here we report the protein tyrosine phosphate phosphohydrolase SH‐PTP1, to associate with synaptic vesicles and interact with synaptophysin. These studies identify SH‐PTP1 as a new member of the secretory machinery at the nerve terminal and suggest its involvement in neurotransmission.