Is TAK1 a Direct Upstream Kinase of AMPK?

被引：76
作者：
Neumann, Dietbert [1 ]
机构：
[1] Maastricht Univ, CARIM Sch Cardiovasc Dis, Fac Hlth Med & Life Sci, Dept Pathol, NL-6200 MD Maastricht, Netherlands
来源：
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | 2018年 / 19卷 / 08期
关键词：
TAK1; AMPK; phosphorylation; AMPK kinase; ACTIVATED PROTEIN-KINASE; ENERGY-SENSOR; SIGNALING PATHWAYS; INDUCED APOPTOSIS; EPITHELIAL-CELLS; BETA; AUTOPHAGY; CANCER; BALANCE; SNF1;
D O I：
10.3390/ijms19082412
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：
Alongside Liver kinase B1 (LKB1) and Ca2+/Calmodulin-dependent protein kinase kinase 2 (CaMKK2), Transforming growth factor-beta (TGF-beta)-activated kinase 1 (TAK1) has been suggested as a direct upstream kinase of AMP-activated protein kinase (AMPK). Several subsequent studies have reported on the TAK1-AMPK relationship, but the interpretation of the respective data has led to conflicting views. Therefore, to date the acceptance of TAK1 as a genuine AMPK kinase is lagging behind. This review provides with argumentation, whether or not TAK1 functions as a direct upstream kinase of AMPK. Several specific open questions that may have precluded the consensus are discussed based on available data. In brief, TAK1 can function as direct AMPK upstream kinase in specific contexts and in response to a subset of TAK1 activating stimuli. Further research is needed to define the intricate signals that are conditional for TAK1 to phosphorylate and activate AMPK at T172.
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页数：8
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