AMPK signaling pathway
From Proteopedia
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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> | 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> | ||
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| + | [[HMGR]] is phosphorylated and inactivated by an AMP-activated protein kinase, when the energy charge of the cell is low and AMP concentrations are high. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 13:26, 29 March 2022
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References
- ↑ Brose MS, Volpe P, Feldman M, Kumar M, Rishi I, Gerrero R, Einhorn E, Herlyn M, Minna J, Nicholson A, Roth JA, Albelda SM, Davies H, Cox C, Brignell G, Stephens P, Futreal PA, Wooster R, Stratton MR, Weber BL. BRAF and RAS mutations in human lung cancer and melanoma. Cancer Res. 2002 Dec 1;62(23):6997-7000. PMID:12460918
- ↑ 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
