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Polyphosphoinositides as activators of PKC‐dependent synapsin I phosphorylation
Author(s) -
Severin S.E.,
Moskvitina E.L.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80480-q
Subject(s) - synapsin i , phosphorylation , protein kinase c , synapsin , chemistry , microbiology and biotechnology , biology , biochemistry , vesicle , membrane , synaptic vesicle
The effect of PIP 2 and diacylglycerol (products of polyphosphoinositide turnover) on the activation level of phosphorylation of the human brain neurospecific protein SI by PKC from the same source was studied. The apparent activation constant of the phosphorylation process was shown to decrease in the presence of PIP 2 from 1.1 μg/ml to 0.2 μg/ml for PI and from 0.8 μg/ml to 0.6 μg/ml for PS; the value of 0.4 μg/ml in the latter case was detected merely after the addition of DOG into the reaction mixture. Polyphosphoinositides are suggested to play a role in activating PKC‐mediated phosphorylation of SI in nerve terminals.