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.
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 calmodulin-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; Snf1: 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).
Dale
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Department of Biochemistry, The University, Dundee, Scotland, UK.
Wilson
W A
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Edelman
A M
AM
Hardie
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DG
D055372:AMP-Activated Protein Kinases; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000378:metabolism*; D008322:Mammals; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000378:metabolism*; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D010944:Plants / Q000201:enzymology; D011494:Protein Kinases / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D009097:Multienzyme Complexes; D009842:Oligopeptides; D011494:Protein Kinases; C071570:SNF1-related protein kinases; D017346:Protein Serine-Threonine Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D055372:AMP-Activated Protein Kinases