Identification of different specificity requirements between SGK1 and PKBα
Identification of different specificity requirements between SGK1 and PKBα
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DOI：
10.1016/j.febslet.2004.12.069
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发表时间：
2005-02-14
期刊：
影响因子：
3.5
通讯作者：
Cohen, P
中科院分区：
文献类型：
--
作者：
Murray, JT;Cummings, LA;Cohen, P
NDRG 1在体内被SGK 1磷酸化（而不是PKB），每个残基包含在三个九肽重复序列中。在这里，我们证明了这种九肽，如NDRG 1蛋白，是由SGK 1磷酸化，但不是由PKBalpha或RSK 1在体外。PKBa和RSK 1不能磷酸化九肽，可追溯到残基n + 1、n + 2和n - 4（其中n是磷酸化位点）。将它们从Ser、Glu和Ser分别改变为Phe、Ala和Pro，将九肽转化为PKB α和RSK 1的优良底物。我们的研究结果确定了SGK 1的特定底物，并可能有助于检测这种酶的其他生理底物。(C)2005年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
NDRG1 is phosphorylated by SGK1 (but not PKB) in vivo at three residues each contained within three nonapeptide repeats. Here, we demonstrate that this nonapeptide, like the NDRG1 protein, is phosphorylated by SGK1, but not by PKBalpha or RSK1 in vitro. The inability of PKBa and RSK1 to phosphorylate the nonapeptide was traced to residues n + 1, n + 2 and n - 4 (where n is the phosphorylation site). Changing them from Ser, Glu and Ser to Phe, Ala and Pro, respectively, transformed the nonapeptide into an excellent substrate for PKBalpha and RSK1. Our results identify a specific substrate for SGK1 and may facilitate detection of additional physiological substrates for this enzyme. (C) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.