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-dependen...
Saved in:
Published in | FEBS letters Vol. 361; no. 2; pp. 191 - 195 |
---|---|
Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier B.V
20.03.1995
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | 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: Φ(X,β)XXS/TXXXΦ; HRK-A: Φ(X,β)XXSXXXΦ; Snf1: ΦXRXXSXXXΦ; CaMKI: ΦXRXXS/TXXXΦ; where Φ is a hydrophobic residue (M, V, L, I or F) and β is a basic residue (R, K or H). |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(95)00172-6 |