Subunit and domain requirements for adenylate-mediated protection of Snf1 kinase activation loop from dephosphorylation.

ABSTRACT: Members of the AMP-activated protein kinase (AMPK) family are activated by phosphorylation at a conserved threonine residue in the activation loop of the kinase domain. Mammalian AMPK adopts a phosphatase-resistant conformation that is stabilized by binding low energy adenylate molecules. Similarly, binding of ADP to the Snf1 complex, yeast AMPK, protects the kinase from dephosphorylation. Here, we determined the nucleotide specificity of the ligand-mediated protection from dephosphorylation and demonstrate the subunit and domain requirements for this reaction. Protection from dephosphorylation was highly specific for adenine nucleotides, with ADP being the most effective ligand for mediating protection. The full-length α subunit (Snf1) was not competent for ADP-mediated protection, confir

SUBMITTER: Chandrashekarappa DG 

PROVIDER: S-EPMC3247968 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature