BRSK2 is activated by cyclic AMP-dependent protein kinase A through phosphorylation at Thr260

Biochem Biophys Res Commun. 2006 Sep 8;347(4):867-71. doi: 10.1016/j.bbrc.2006.06.178. Epub 2006 Jul 25.

Abstract

Brain selective kinase 2 (BRSK2) has been identified as a member of AMPK related kinases. LKB1 can phosphorylate the Thr174 of BRSK2, increasing its activity >50-fold. In this study, we identified cAMP-dependent protein kinase A (PKA) as another upstream kinase of BRSK2, which can phosphorylate BRSK2 at Thr260. The association between these two proteins was confirmed by GST pull-down. Furthermore, our study indicated that the kinase activity of BRSK2 can be increased through phosphorylation by PKA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cyclic AMP-Dependent Protein Kinases / metabolism*
  • Enzyme Activation
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Serine-Threonine Kinases / metabolism*
  • Sequence Alignment
  • Threonine / metabolism*

Substances

  • Threonine
  • Brsk2 protein, human
  • Protein Serine-Threonine Kinases
  • Cyclic AMP-Dependent Protein Kinases