NDLI: Regulation of AMP-activated protein kinase by a pseudosubstrate sequence on the γ subunit

Content Provider	PubMed Central
Author	Scott, John W. Ross, Fiona A. Liu, J. K. David Hardie, D. Grahame
Copyright Year	2007
Abstract	The AMP-activated protein kinase (AMPK) system monitors cellular energy status by sensing AMP and ATP, and is a key regulator of energy balance at the cellular and whole-body levels. AMPK exists as heterotrimeric αβγ complexes, and the γ subunits contain two tandem domains that bind the regulatory nucleotides. There is a sequence in the first of these domains that is conserved in γ subunit homologues in all eukaryotes, and which resembles the sequence around sites phosphorylated on target proteins of AMPK, except that it has a non-phosphorylatable residue in place of serine. We propose that in the absence of AMP this pseudosubstrate sequence binds to the active site groove on the α subunit, preventing phosphorylation by the upstream kinase, LKB1, and access to downstream targets. Binding of AMP causes a conformational change that prevents this interaction and relieves the inhibition. We present several lines of evidence supporting this hypothesis.
Related Links	http://dx.doi.org/10.1038/sj.emboj.7601542
Ending Page	815
Page Count	10
Starting Page	806
File Format	PDF
ISSN	02614189
e-ISSN	14602075
Journal	The EMBO Journal
Issue Number	3
Volume Number	26
Language	English
Publisher	Nature Publishing Group
Publisher Date	2007-02-07
Access Restriction	Open
Rights Holder	Nature Publishing Group
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Immunology and Microbiology(all) Neuroscience(all) Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Immunology and Microbiology Medicine Molecular Biology

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