AMPK signaling pathway

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'''AMP-activated protein kinase''' (AMPK) is a [[nuclear receptor]] which regulates cellular uptake of glucose, β-oxidation of fatty acids and biogenesis of glucose transporter thus playing a role in cellular energy homeostasis by phosphorylating key proteins. In response to low levels of ATP, AMPK activates energy-producing pathways and inhibits energy-consuming pathways.
'''AMP-activated protein kinase''' (AMPK) is a [[nuclear receptor]] which regulates cellular uptake of glucose, β-oxidation of fatty acids and biogenesis of glucose transporter thus playing a role in cellular energy homeostasis by phosphorylating key proteins. In response to low levels of ATP, AMPK activates energy-producing pathways and inhibits energy-consuming pathways.
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AMPK is an important drug target for obesity, type 2 diabetes and cancer. AMPK activity is enhanced during exercise resulting in increased glucose uptake and blood supply in muscles. Stresses like hypoglycemia, anoxia and ischemia produce increase in AMPK levels.<br />
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== Structural highlights ==
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AMPK is a heterotrimer: <br /> <scene name='49/493732/Cv/10'>AMPK α subunit</scene> is the catalytic subunit and contains <scene name='49/493732/Cv/11'>Thr174 (TPO) which undergoes phosphorylation</scene>. <br /> <scene name='49/493732/Cv/5'>AMPK β subunit</scene> is a scaffold on which the heterotrimer assembles. There are 2 β subunits. β subunit contains <scene name='49/493732/Cv/12'>phosphorylated Ser108 (SEP)</scene>. <br /> <scene name='49/493732/Cv/8'>AMPK γ subunit</scene> detects shifts in AMP:ATP ratio via its 4 cystathionine β synthase (CBS) domains. <scene name='49/493732/Cv/13'>The active site binds 3 AMPs</scene>.<ref>PMID:25412657</ref>
</StructureSection>
</StructureSection>
== References ==
== References ==
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Revision as of 12:51, 23 February 2022

Human AMP-activated protein kinase α1 subunit (deeppink) +β2 subunit (green) +γ1 subunit (cyan) complex with AMP, staurosporine, cyclodextrin and HEPES (PDB code 4rer)

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References

  1. Li X, Wang L, Zhou XE, Ke J, de Waal PW, Gu X, Tan MH, Wang D, Wu D, Xu HE, Melcher K. Structural basis of AMPK regulation by adenine nucleotides and glycogen. Cell Res. 2014 Nov 21. doi: 10.1038/cr.2014.150. PMID:25412657 doi:http://dx.doi.org/10.1038/cr.2014.150

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