Differential AMP-activated protein kinase (AMPK) recognition mechanism of Ca2+/calmodulin-dependent protein kinase kinase isoforms

Yuya Fujiwara, Yoshinori Kawaguchi, Tomohito Fujimoto, Naoki Kanayama, Masaki Magari, Hiroshi Tokumitsu

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Ca2+/calmodulin-dependent protein kinase kinase β (CaMKKβ) is a known activating kinase for AMP-activated protein kinase (AMPK). In vitro, CaMKKβ phosphorylates Thr172 in the AMPKα subunit more efficiently than CaMKKα, with a lower Km (∼2 μM) for AMPK, whereas the CaMKIα phosphorylation efficiencies by both CaMKKs are indistinguishable. Here we found that subdomain VIII of CaMKK is involved in the discrimination of AMPK as a native substrate by measuring the activities of various CaMKKα/CaMKKβ chimera mutants. Site-directed mutagenesis analysis revealed that Leu358 in CaMKKβ/Ile322 in CaMKKα confer, at least in part, a distinct recognition of AMPK but not of CaMKIα.

Original languageEnglish
Pages (from-to)13802-13808
Number of pages7
JournalJournal of Biological Chemistry
Volume291
Issue number26
DOIs
Publication statusPublished - Jun 24 2016

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Calcium-Calmodulin-Dependent Protein Kinases
AMP-Activated Protein Kinases
Protein Isoforms
Phosphotransferases
Calcium-Calmodulin-Dependent Protein Kinase Kinase
Mutagenesis
Phosphorylation
Protein Subunits
Site-Directed Mutagenesis
Substrates

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Differential AMP-activated protein kinase (AMPK) recognition mechanism of Ca2+/calmodulin-dependent protein kinase kinase isoforms. / Fujiwara, Yuya; Kawaguchi, Yoshinori; Fujimoto, Tomohito; Kanayama, Naoki; Magari, Masaki; Tokumitsu, Hiroshi.

In: Journal of Biological Chemistry, Vol. 291, No. 26, 24.06.2016, p. 13802-13808.

Research output: Contribution to journalArticle

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