The regulation of AMP-activated protein kinase by phosphorylation
نویسندگان
چکیده
منابع مشابه
Regulation of autophagy by AMP-activated protein kinase/ sirtuin 1 pathway reduces spinal cord neurons damage
Objective(s): AMP-activated protein kinase/sirtuin 1 (AMPK/SIRT1) signaling pathway has been proved to be involved in the regulation of autophagy in various models. The aim of this study was to evaluate the effect of AMPK/SIRT1 pathway on autophagy after spinal cord injury (SCI). Materials and Methods:The SCI model was established in rats in vivo and the primary spinal cord neurons were subject...
متن کاملThe regulation of AMP-activated protein kinase by phosphorylation.
The AMP-activated protein kinase (AMPK) cascade is activated by an increase in the AMP/ATP ratio within the cell. AMPK is regulated allosterically by AMP and by reversible phosphorylation. Threonine-172 within the catalytic subunit (alpha) of AMPK (Thr(172)) was identified as the major site phosphorylated by the AMP-activated protein kinase kinase (AMPKK) in vitro. We have used site-directed mu...
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The AMP-activated protein kinase (AMPK) is the central component of a protein kinase cascade which plays an important role in the regulation of many different aspects of lipid metabolism [1,2]. AMPK is activated 50to 100-fold by phosphorylation by an upstream protein kinase, AMPK kinase (AMPKK) [3]. The key regulators of the AMPK cascade currently appear to be S’-AMP and ATP. AMP activates the ...
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The AMP-activated protein kinase (AMPK) is an energy-sensing enzyme that is activated during exercise and muscle contraction as a result of acute decreases in ATP:AMP and phosphocreatine:creatine. Physical exercise increases muscle glucose uptake, enhances insulin sensitivity and leads to fatty acid oxidation in muscle. An important issue in muscle biology is to understand whether AMPK plays a ...
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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...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2000
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3450437