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Phosphorylation of proteins in neuron terminals: Specificity depends on coincidental signaling
Author(s) -
Zhang Lixing,
Tinette Sylvette,
Robichon Alain
Publication year - 2002
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.10363
Subject(s) - phosphorylation , phosphatase , kinase , microbiology and biotechnology , signal transduction , biology , function (biology) , vesicle , second messenger system , protein phosphorylation , biochemistry , glutamate receptor , chemistry , protein kinase a , receptor , membrane
We investigate the role of neuronal coincidental signaling mediated by the second messengers, on phosphorylation of three major proteins of neurosecretory vesicles. Our data show that different combinations of coincidental signaling generate specific pattern of phosphoproteins and not strictly additional effects. This suggests that an added phosphate on a site might ‘mask’ or ‘unmask’ the next sites for specific kinases and phosphatases action by inducing conformation change or protein association. We show that a function of vesicles such as the uptake of glutamate is highly regulated by coincidental signaling. © 2002 Wiley‐Liss, Inc.