Synapsin I phosphorylated by Ca2+, calmodulin‐dependent protein kinase II is able to self‐degrade

FEBS Letters

Severin, S.E.¹  Gubin, A.N.¹ 

[1] Research Center of Molecular Diagnostics, USSR Ministry of Health, Sympheropolsky blvd. 8, Moscow 113149, USSR

关键词: Synapsin I;    Calmodulin-dependent protein kinase II;    Phosphorylation;    Self-degradation;    SI;    synapsin I;    PK C;    protein kinase C;    PK A;    cAMP-dependent protein kinase;    PK II;    calmodulin-dependent protein kinase;   

DOI  :  10.1016/0014-5793(91)80897-C

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phosphorylation of the neurospecific protein synapsin I (SI) by various cellular protein kinases was studied. The analysis of functional properties of phosphosynapsins showed that in the case of PK II-mediated modification of the protein, it becomes capable of self-degradation. The latter process was found to be specific and did not appear to be characteristic of the phosphoforms emerging after the protein modification by PK C or PK A. A possible involvement of the process in the regulation of neurotransmitter secretion is discussed.

【 授权许可】

Unknown