AMP-Activated Protein Kinase Induces a p53-Dependent Metabolic Checkpoint
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چکیده
منابع مشابه
AMP-activated protein kinase induces a p53-dependent metabolic checkpoint.
Replicative cell division is an energetically demanding process that can be executed only if cells have sufficient metabolic resources to support a doubling of cell mass. Here we show that proliferating mammalian cells have a cell-cycle checkpoint that responds to glucose availability. The glucose-dependent checkpoint occurs at the G(1)/S boundary and is regulated by AMP-activated protein kinas...
متن کاملAMP-activated protein kinase and metabolic control.
AMP-activated protein kinase AMP-activated protein kinase (AMPK AMPK ), a phylogenetically conserved serine/threonine protein kinase, is a major regulator of cellular and whole-body energy homeostasis that coordinates metabolic pathways in order to balance nutrient supply with energy demand. It is now recognized that pharmacological activation of AMPK improves blood glucose homeostasis, lipid p...
متن کاملAMP-activated protein kinase, super metabolic regulator.
The AMP-activated protein kinase (AMPK) is a metabolic-stress-sensing protein kinase that regulates metabolism in response to energy demand and supply by directly phosphorylating rate-limiting enzymes in metabolic pathways as well as controlling gene expression.
متن کاملSIRT1 phosphorylation by AMP-activated protein kinase regulates p53 acetylation.
The deacetylase SIRT1 regulates multiple biological processes including cellular metabolism and aging. Importantly, SIRT1 can also inactivate the p53 tumor suppressor via deacetylation, suggesting a role in oncogenesis. Recently, SIRT1 was shown to be released from its endogenous inhibitor DBC1 by a process requiring AMPK and the phosphorylation of SIRT1 by yet undefined kinase(s). Here we prov...
متن کاملAMP-activated protein kinase induces p53 by phosphorylating MDMX and inhibiting its activity.
AMP-activated protein kinase (AMPK) has been shown to activate p53 in response to metabolic stress. However, the underlying mechanisms remain unclear. Here we show that metabolic stresses induce AMPK-mediated phosphorylation of human MDMX on Ser342 in vitro and in cells, leading to enhanced association between MDMX and 14-3-3. This markedly inhibits p53 ubiquitylation and significantly stabiliz...
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ژورنال
عنوان ژورنال: Molecular Cell
سال: 2005
ISSN: 1097-2765
DOI: 10.1016/j.molcel.2005.03.027