Literature DB >> 228175

The time course of the phosphorylation of proteins in the synaptic plasma membrane and the effect of certain cations.

M Weller.   

Abstract

The phosphorylation of proteins in the synaptic plasma membrane is a rather slow reaction taking several minutes to saturate all the phosphate acceptor sites. (The time for half the protein bound phosphate groups to turnover is about 1 min). A divalent cation is needed as a cofactor for the reaction. At high (0.5 mM) ATP concentrations Mg2+ is more effective than Mn2+ but at low (10 microM) ATP concentrations the reverse is the case. Zn2+ and Ca2+ support very little phosphorylation.

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Year:  1979        PMID： 228175     DOI： 10.1007/bf00218350

Source DB:  PubMed          Journal:  Mol Cell Biochem        ISSN： 0300-8177            Impact factor:   3.396


  20 in total

1.  Localization in the synaptic junction of the cyclic AMP stimulated intrinsic protein kinase activity of synaptosomal plasma membranes.

Authors:  M Weller; I G Morgan
Journal:  Biochim Biophys Acta       Date:  1976-04-16

2.  Distribution of protein kinase activities in subcellular fractions of rat brain.

Authors:  M Weller; I Morgan
Journal:  Biochim Biophys Acta       Date:  1976-07-01

3.  A theoretical treatment of the turnover of protein-bound phosphate in the presence of both protein kinase and phosphatase activities.

Authors:  M Weller
Journal:  Biochim Biophys Acta       Date:  1974-05-24

4.  Regulation of endogenous phosphorylation of specific proteins in synaptic membrane fractions from rat brain by adenosine 3':5'-monophosphate.

Authors:  T Ueda; H Maeno; P Greengard
Journal:  J Biol Chem       Date:  1973-12-10       Impact factor: 5.157

5.  A simple method for the preparation of 32-P-labelled adenosine triphosphate of high specific activity.

Authors:  I M Glynn; J B Chappell
Journal:  Biochem J       Date:  1964-01       Impact factor: 3.857

Review 6.  Possible role for cyclic nucleotides and phosphorylated membrane proteins in postsynaptic actions of neurotransmitters.

Authors:  P Greengard
Journal:  Nature       Date:  1976-03-11       Impact factor: 49.962

7.  Protein kinase activity in membrane preparations from ox brain. Stimulation of intrinsic activity by adenosine 3':5'-cyclic monophosphate.

Authors:  M Weller; R Rodnight
Journal:  Biochem J       Date:  1973-03       Impact factor: 3.857

8.  Protein kinase activity stimulated by adenosine 3' :5'-cyclic monophosphate in synaptic-membrane fragments from ox brain. Inhibition of intrinsic activity by free and membrane-bound calcium ions.

Authors:  M Weller; R Rodnight
Journal:  Biochem J       Date:  1974-09       Impact factor: 3.857

9.  Turnover of protein-bound phosphorylserine in membrane preparations from ox brain catalysed by intrinsic kinase and phosphatase activity.

Authors:  M Weller; R Rodnight
Journal:  Biochem J       Date:  1971-09       Impact factor: 3.857

10.  Phosphate binding by cerebral microsomes in relation to adenosine-triphosphatase activity.

Authors:  R Rodnight; D A Hems; B E Lavin
Journal:  Biochem J       Date:  1966-11       Impact factor: 3.857
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  1 in total

1.  Cyclic AMP independent protein kinase activity in rat cerebral cortex synaptic vesicles--partial characterization.

Authors:  J Glaser; M G Weller; A C Neethling; J J Taljaard
Journal:  Neurochem Res       Date:  1982-10       Impact factor: 3.996
  1 in total

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