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 language | English |
|---|---|
| Pages (from-to) | 13802-13808 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 291 |
| Issue number | 26 |
| DOIs | |
| Publication status | Published - Jun 24 2016 |
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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 journal › Article
}
TY - JOUR
T1 - Differential AMP-activated protein kinase (AMPK) recognition mechanism of Ca2+/calmodulin-dependent protein kinase kinase isoforms
AU - Fujiwara, Yuya
AU - Kawaguchi, Yoshinori
AU - Fujimoto, Tomohito
AU - Kanayama, Naoki
AU - Magari, Masaki
AU - Tokumitsu, Hiroshi
PY - 2016/6/24
Y1 - 2016/6/24
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84976339944&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84976339944&partnerID=8YFLogxK
U2 - 10.1074/jbc.M116.727867
DO - 10.1074/jbc.M116.727867
M3 - Article
C2 - 27151216
AN - SCOPUS:84976339944
VL - 291
SP - 13802
EP - 13808
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 26
ER -