AUTOPHOSPHORYLATION - A SALIENT FEATURE OF PROTEIN-KINASES

被引：76

作者：

SMITH, JA ^{[1
]}

FRANCIS, SH ^{[1
]}

CORBIN, JD ^{[1
]}

机构：

[1] VANDERBILT UNIV, DEPT MOLEC PHYSIOL & BIOPHYS, NASHVILLE, TN 37232 USA

来源：

MOLECULAR AND CELLULAR BIOCHEMISTRY | 1993年 / 128卷

关键词：

PROTEIN KINASES; AUTOPHOSPHORYLATION; PROTEIN PHOSPHORYLATION; POSTTRANSLATIONAL MODIFICATION; REGULATION; SH2; DOMAINS;

D O I：

10.1007/BF01076757

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Most protein kinases catalyze autophosphorylation, a process which is generally intramolecular and is modulated by regulatory ligands. Either serine/threonine or tyrosine serves as the phosphoacceptor, and several sites on the same kinase subunit are usually autophosphorylated. Autophosphorylation affects the functional properties of most protein kinases. Members of the protein kinase family exhibit diversity in the characteristics and functions of autophosphorylation, but certain common themes are emerging.

引用

页码：51 / 70

页数：20

共 239 条

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