SIMILAR SUBSTRATE RECOGNITION MOTIFS FOR MAMMALIAN AMP-ACTIVATED PROTEIN-KINASE, HIGHER-PLANT HMG-COA REDUCTASE KINASE-A, YEAST SNF1, AND MAMMALIAN CALMODULIN-DEPENDENT PROTEIN-KINASE-I

被引:270
作者
DALE, S
WILSON, WA
EDELMAN, AM
HARDIE, DG
机构
[1] UNIV DUNDEE,DEPT BIOCHEM,DUNDEE DD1 4HN,SCOTLAND
[2] SUNY BUFFALO,DEPT PHARMACOL & TOXICOL,BUFFALO,NY
基金
英国惠康基金;
关键词
AMP-ACTIVATED PROTEIN KINASE; HMG-COA REDUCTASE KINASE; SNF1; CALMODULIN-DEPENDENT PROTEIN KINASE I; SPECIFICITY DETERMINANT; CONSENSUS SEQUENCE;
D O I
10.1016/0014-5793(95)00172-6
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
We have analysed phosphorylation of the synthetic peptide AMARAASAAALARRR, and 23 variants, by mammalian, higher plant and yeast members of the SNF1 protein kinase subfamily (AMP-activated protein kinase (AMPK), HMG-CoA reductase kinase (HRK-A), and SNF1 itself), and by mammalian calnodulin-dependent protein kinase I (CaMKI). These four kinases recognize motifs which are very similar, although distinguishable, Our studies define the following recognition motifs: AMPK: Phi(X,beta)XXS/TXXX Phi; HRK-A: Phi(X,beta)XXSXXX Phi; Suf1: Phi XRXXSXXX Phi; CaMKI: Phi XRXXS/TXXX Phi; where Phi is a hydrophobic residue (M, V, L, I or F) and beta is a basic residue (R, K or H).
引用
收藏
页码:191 / 195
页数:5
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