Differential AMP-activated Protein Kinase (AMPK) Recognition Mechanism of Ca2+/Calmodulin-dependent Protein Kinase Kinase Isoforms

被引：31
|
作者：
Fujiwara, Yuya [1 ]
Kawaguchi, Yoshinori [1 ]
Fujimoto, Tomohito [2 ]
Kanayama, Naoki [1 ]
Magari, Masaki [1 ]
Tokumitsu, Hiroshi [1 ]
机构：
[1] Okayama Univ, Grad Sch Nat Sci & Technol, Div Med Bioengn, Okayama 7008530, Japan
[2] Carna Biosci Inc, Kobe, Hyogo 6500047, Japan
来源：
JOURNAL OF BIOLOGICAL CHEMISTRY | 2016年 / 291卷 / 26期
关键词：
AMP-activated kinase (AMPK); Ca2+; calmodulin-dependent protein kinase (CaMK); calmodulin (CaM); phosphorylation; substrate specificity; CaMKI; CaMKK; substrate recognition; MOLECULAR-CLONING; SIGNALING COMPLEX; ESCHERICHIA-COLI; CAMKK-BETA; CALMODULIN; CASCADE; EXPRESSION; TRANSCRIPTION; INHIBITOR; UPSTREAM;
D O I：
10.1074/jbc.M116.727867
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Ca2+/calmodulin-dependent protein kinase kinase (CaMKK) is a known activating kinase for AMP-activated protein kinase (AMPK). In vitro, CaMKK phosphorylates Thr(172) in the AMPK subunit more efficiently than CaMKK, with a lower K-m (approximate to 2 m) for AMPK, whereas the CaMKI 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 CaMKK/CaMKK chimera mutants. Site-directed mutagenesis analysis revealed that Leu(358) in CaMKK/Ile(322) in CaMKK confer, at least in part, a distinct recognition of AMPK but not of CaMKI.
引用
收藏
页码：13802 / 13808
页数：7
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