AMP-activated protein kinase

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== Function ==
== Function ==
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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.
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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.
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See also [[AMPK signaling pathway]].
== Relevance ==
== Relevance ==
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== Structural highlights ==
== Structural highlights ==
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AMPK is a heterotrimer: <br /> <scene name='49/493732/Cv/4'>AMPK α subunit</scene> is the catalytic subunit and contains <scene name='49/493732/Cv/3'>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/7'>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/9'>The active site binds 3 AMPs</scene>.<ref>PMID:25412657</ref>
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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>
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</StructureSection>
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==3D structures of AMP-activated protein kinase==
==3D structures of AMP-activated protein kinase==
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[[AMP-activated protein kinase 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*AMPK α-1 subunit
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**[[4red]] - hAMPK α1 subunit (mutant) - human<br />
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**[[4f2l]] - rAMPK α1 subunit – rat<br />
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*AMPK α-2 subunit
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**[[2h6d]] - hAMPK α2 subunit<br />
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**[[2ltu]] - hAMPK α2 subunit – NMR<br />
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**[[2yza]] - hAMPK α2 subunit (mutant) <br />
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**[[3aqv]] - hAMPK α2 subunit (mutant) + inhibitor<br />
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*AMPK β-1 carbohydrate-binding domain
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**[[1z0m]], [[4yef]] – rAMPK + β-cyclodextrin - rat<br />
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**[[1z0n]] – rAMPK (mutant) + β-cyclodextrin <br />
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**[[4yef]] – rAMPK + glucosyl-cyclodextrin <br />
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*AMPK β-2 carbohydrate-binding domain
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**[[2f15]] – hAMPK <br />
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**[[2lu3]] – rAMPK - NMR<br />
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**[[2lu4]] – rAMPK + glycosyl-cyclodextrin - NMR<br />
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**[[4y0g]] – rAMPK <br />
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**[[4yee]] – rAMPK + glycosyl-cyclodextrin <br />
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*AMPK γ-1 subunit
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**[[2uv4]], [[2uv5]] - hAMPK CBS 3+4 domains + AMP<br />
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**[[2uv6]], [[2uv7]] - hAMPK CBS 3+4 domains (mutant) + AMP<br />
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*AMPK α-1+β-2+γ-1
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**[[2v8q]], [[4eai]] – rAMPK + AMP<br />
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**[[2v92]], [[2v9j]], [[4eaj]] – rAMPK + AMP + ATP<br />
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**[[2y8l]], [[2y8q]] – rAMPK + ADP <br />
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**[[2ya3]] – rAMPK + coumarin-ADP + AMP<br />
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**[[4rew]] – hAMPK (mutant) + AMP <br />
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*AMPK α-1+β-1+γ-1
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**[[4eal]] – rAMPK + AMP<br />
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**[[4eak]] – rAMPK + ATP <br />
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**[[4eag]] – SNF1A/rAMPK β-1 γ-1 + ATP <br />
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*Phosphorylated AMPK α-1+β-2+γ-1
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**[[4cfh]] – rAMPK + AMP + staurosporine <br />
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**[[4rer]] – hAMPK (mutant) + AMP + staurosporine + cyclodextrin<br />
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*Phosphorylated AMPK α-1+β-1+γ-1
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**[[4qfg]] – rAMPK (mutant) + AMP + staurosporine <br />
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**[[5ufu]] – rAMPK + AMP + ADP + staurosporine + activator<br />
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**[[4qfr]], [[4qfs]], [[5t5t]] – rAMPK (mutant) + AMP + ADP + staurosporine + activator<br />
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**[[5kq5]] – rAMPK + AMP + ADP + staurosporine + activator<br />
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*Phosphorylated AMPK α-2+β-1+γ-1
 
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**[[4cfe]], [[5iso]] – hAMPK + AMP + staurosporine + benzimidazole derivative<br />
 
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**[[4cff]] – hAMPK + AMP + staurosporine + pyridone derivative<br />
 
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**[[4zhx]], [[5ezv]] – hAMPK + AMP + staurosporine + furan-2-posphonic derivative<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

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

Drag the structure with the mouse to rotate


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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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