NDLI: Ligand binding to the AMP-activated protein kinase active site mediates protection of the activation loop from dephosphorylation.

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Ligand binding to the AMP-activated protein kinase active site mediates protection of the activation loop from dephosphorylation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Chandrashekarappa, Dakshayini G. Mccartney, Rhonda R. Schmidt, Martin C.
Description	Author Affiliation: Chandrashekarappa DG ( Department of Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, USA.)
Abstract	The AMP-activated protein kinase (AMPK) is a conserved signaling molecule in a pathway that maintains adenosine triphosphate homeostasis. Recent studies have suggested that low energy adenylate ligands bound to one or more sites in the Î³ subunit of AMPK promote the formation of an active, phosphatase-resistant conformation. We propose an alternative model in which the kinase domain association with the heterotrimer core results in activation of the kinase catalytic activity, whereas low energy adenylate ligands bound in the kinase active site promote phosphatase resistance. Purified Snf1 subunit with a conservative, single amino acid substitution in the kinase domain is protected from dephosphorylation by adenosine diphosphate in the complete absence of the ß and Î³ subunits. Staurosporine, a compound known to bind to the active site of many protein kinases, mediates strong protection from dephosphorylation to yeast and mammalian AMPK enzymes. The analog-sensitive Snf1-I132G protein but not wild type Snf1 exhibits protection from dephosphorylation when bound by the adenosine analog 2NM-PP1 in vitro and in vivo. These data demonstrate that ligand binding to the Snf1 active site can mediate phosphatase resistance. Finally, Snf1 kinase with an amino acid substitution at the interface of the kinase domain and the heterotrimer core exhibits normal regulation of phosphorylation in vivo but greatly reduced Snf1 kinase activity, supporting a model in which kinase domain association with the heterotrimer core is needed for kinase activation.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	1
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-01-04
Publisher Place	United States
Access Restriction	Open
Subject Keyword	AMP-Activated Protein Kinases Chemistry Gene Expression Regulation, Enzymologic Schizosaccharomyces Metabolism Adenosine Diphosphate Animals Catalytic Domain Enzyme Inhibitors Pharmacology Fungal Proteins Kinetics Ligands Models, Molecular Molecular Conformation Mutation Phosphorylation Protein Binding Protein Structure, Tertiary Protein-Serine-Threonine Kinases Signal Transduction Staurosporine Substrate Specificity Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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