Identification of a human Akt3 (protein kinase Bγ) which contains the regulatory serine phosphorylation site

被引:146
|
作者
Nakatani, K
Sakaue, H
Thompson, DA
Weigel, RJ
Roth, RA [1 ]
机构
[1] Stanford Univ, Sch Med, Dept Mol Pharmacol, Stanford, CA 94305 USA
[2] Stanford Univ, Sch Med, Dept Surg, Stanford, CA 94305 USA
关键词
D O I
10.1006/bbrc.1999.0559
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
The family of protein kinases called Akt, protein kinase B (PKB), or related to A and C kinase (RAC) have been implicated in numerous biological processes including adipocyte and muscle differentiation, glycogen synthesis, glucose uptake, apoptosis and cellular proliferation. There are 3 known isoforms of this enzyme in mammalian cells (1/alpha, 2/alpha and 3/gamma), Akt1 and 2 contain a key regulatory serine phosphorylation site in the carboxy-terminal region of the protein, However, the reported sequence of the rat Akt3 protein differed significantly from this in that it lacked 25 amino acids in the C-terminal region, including this key regulatory serine phosphorylation site (Biochem. Biophys. Res. Commun. 216, 526-534). In the present studies we show that the deduced sequence of human Akt3 contains this serine and that it is phosphorylated in response to insulin. These results indicate that human Akt3 is regulated similarly to Akt1 and Akt2. (C) 1999 Academic Press.
引用
收藏
页码:906 / 910
页数:5
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