AUTOPHOSPHORYLATION OF PROTEIN KINASE-C AT 3-SEPARATED REGIONS OF ITS PRIMARY SEQUENCE

被引：137

作者：

FLINT, AJ ^{[1
]}

PALADINI, RD ^{[1
]}

KOSHLAND, DE ^{[1
]}

机构：

[1] UNIV CALIF BERKELEY,DEPT MOLEC & CELLULAR BIOL,DIV BIOCHEM & MOLEC BIOL,BERKELEY,CA 94720

来源：

SCIENCE | 1990年 / 249卷 / 4967期

关键词：

D O I：

10.1126/science.2377895

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The major autophosphorylation sites of the rat βII isozyme of protein kinase C were identified. The modified threonine and serine residues were found in the amino-terminal peptide, the carboxyl-terminal tail, and the hinge region between the regulatory lipid-binding domain and the catalytic kinase domain. Because this auto-phosphorylation follows an intrapeptide mechanism, extraordinary flexibility of the protein is necessary to phosphorylate the three regions. Comparison of the sequences surrounding the modified residues showed no obvious recognition motif nor any similarity to substrate phosphorylation sites, suggesting that proximity to the active site may be the primary criterion for their phosphorylation.

引用

页码：408 / 411

页数：4