期刊
CELL METABOLISM
卷 27, 期 2, 页码 299-313出版社
CELL PRESS
DOI: 10.1016/j.cmet.2017.10.009
关键词
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资金
- Cancer Research UK [C37030/A15101]
- Wellcome Trust [097726/Z/11/Z]
- National Foundation of Sciences
- Ministry of Science and Technology of China
- National Key R&D Program of China [2016YFA0502001]
- National Natural Science Foundation of China [31430094, 31601152]
- Wellcome Trust [204766/Z/16/Z] Funding Source: Wellcome Trust
- Cancer Research UK [15101] Funding Source: researchfish
- Wellcome Trust [204766/Z/16/Z] Funding Source: researchfish
Mammalian AMPK is known to be activated by falling cellular energy status, signaled by rising AMP/ATP and ADP/ATP ratios. We review recent information about how this occurs but also discuss new studies suggesting that AMPK is able to sense glucose availability independently of changes in adenine nucleotides. The glycolytic intermediate fructose-1,6-bisphosphate (FBP) is sensed by aldolase, which binds to the v-ATPase on the lysosomal surface. In the absence of FBP, interactions between aldolase and the v-ATPase are altered, allowing formation of an AXIN-based AMPK-activation complex containing the v-ATPase, Ragulator, AXIN, LKB1, and AMPK, causing increased Thr172 phosphorylation and AMPK activation. This nutrient-sensing mechanism activates AMPK but also primes it for further activation if cellular energy status subsequently falls. Glucose sensing at the lysosome, in which AMPK and other components of the activation complex act antagonistically with another key nutrient sensor, mTORC1, may have been one of the ancestral roles of AMPK.
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