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

FEBS Lett. 1995 Mar 20;361(2-3):191-5. doi: 10.1016/0014-5793(95)00172-6.

Abstract

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).

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • AMP-Activated Protein Kinases
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
  • Mammals
  • Molecular Sequence Data
  • Multienzyme Complexes / metabolism*
  • Oligopeptides / chemical synthesis
  • Oligopeptides / chemistry
  • Oligopeptides / metabolism
  • Phosphorylation
  • Plants / enzymology
  • Protein Kinases / metabolism*
  • Protein-Serine-Threonine Kinases / metabolism*
  • Saccharomyces cerevisiae / metabolism
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Multienzyme Complexes
  • Oligopeptides
  • Protein Kinases
  • SNF1-related protein kinases
  • Protein-Serine-Threonine Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • AMP-Activated Protein Kinases