REGULATION OF BRAIN TYPE-II CA-2+ CALMODULIN-DEPENDENT PROTEIN-KINASE BY AUTOPHOSPHORYLATION - A CA-2+-TRIGGERED MOLECULAR SWITCH

被引：786

作者：

MILLER, SG ^{[1
]}

KENNEDY, MB ^{[1
]}

机构：

[1] CALTECH, DIV BIOL, PASADENA, CA 91125 USA

来源：

CELL | 1986年 / 44卷 / 06期

关键词：

D O I：

10.1016/0092-8674(86)90008-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Calcium/calmodulin-stimulated autophosphorylation of a prominent brain calmodulin-dependent protein kinase (Type II CaM kinase) produces dramatic changes in its enzymatic activity. These changes suggest a mechanism by which the kinase could act as a calcium-triggered molecular switch. Incorporation of 3-12 of a possible total of 30 phosphate groups per holoenzyme causes kinase activity toward exogenous substrates as well as autophosphorylation itself to become independent of calcium. Thus, kinase activity could be prolonged beyond the duration of an initial activating calcium signal. The calcium-independent autophosphorylation could further prolong the active state by opposing dephosphorylation by cellular phosphatases.

引用

页码：861 / 870

页数：10

共 51 条

[1]

AHMAD Z, 1982, J BIOL CHEM, V257, P8348

[2]

BENNETT MK, 1983, J BIOL CHEM, V258, P2735

[3] LONG-LASTING POTENTIATION OF SYNAPTIC TRANSMISSION IN DENTATE AREA OF ANESTHETIZED RABBIT FOLLOWING STIMULATION OF PERFORANT PATH [J].