NDLI: Phosphorylation-dependent changes in nucleotide binding, conformation, and dynamics of the first nucleotide binding domain (NBD1) of the sulfonylurea receptor 2B (SUR2B).

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Phosphorylation-dependent changes in nucleotide binding, conformation, and dynamics of the first nucleotide binding domain (NBD1) of the sulfonylurea receptor 2B (SUR2B).

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	De Araujo, Elvin D. Alvarez, Claudia P. Kanelis, Voula López-alonso, Jorge P. Sooklal, Clarissa R. Stagljar, Marijana
Description	Author Affiliation: de Araujo ED ( From the Department of Chemical and Physical Sciences, University of Toronto Mississauga, Mississauga, Ontario L5L 1C6, the Department of Chemistry, University of Toronto, Toronto, Ontario M5S 3H6, and.); Alvarez CP ( From the Department of Chemical and Physical Sciences, University of Toronto Mississauga, Mississauga, Ontario L5L 1C6, the Department of Chemistry, University of Toronto, Toronto, Ontario M5S 3H6, and.); López-Alonso JP ( From the Department of Chemical and Physical Sciences, University of Toronto Mississauga, Mississauga, Ontario L5L 1C6, the Department of Chemistry, University of Toronto, Toronto, Ontario M5S 3H6, and the Department of Cell and Systems Biology, University of Toronto, Toronto, Ontario M5S 3G5, Canad); Sooklal CR ( From the Department of Chemical and Physical Sciences, University of Toronto Mississauga, Mississauga, Ontario L5L 1C6, the Department of Chemistry, University of Toronto, Toronto, Ontario M5S 3H6, and.); Stagljar M ( From the Department of Chemical and Physical Sciences, University of Toronto Mississauga, Mississauga, Ontario L5L 1C6, the Department of Chemistry, University of Toronto, Toronto, Ontario M5S 3H6, and the Department of Cell and Systems Biology, University of Toronto, Toronto, Ontario M5S 3G5, Canad); Kanelis V ( From the Department of Chemical and Physical Sciences, University of Toronto Mississauga, Mississauga, Ontario L5L 1C6, the Department of Chemistry, University of Toronto, Toronto, Ontario M5S 3H6, and the Department of Cell and Systems Biology, University of Toronto, Toronto, Ontario M5S 3G5, Canad)
Abstract	The sulfonylurea receptor 2B (SUR2B) forms the regulatory subunit of ATP-sensitive potassium (KATP) channels in vascular smooth muscle. Phosphorylation of the SUR2B nucleotide binding domains (NBD1 and NBD2) by protein kinase A results in increased channel open probability. Here, we investigate the effects of phosphorylation on the structure and nucleotide binding properties of NBD1. Phosphorylation sites in SUR2B NBD1 are located in an N-terminal tail that is disordered. Nuclear magnetic resonance (NMR) data indicate that phosphorylation of the N-terminal tail affects multiple residues in NBD1, including residues in the NBD2-binding site, and results in altered conformation and dynamics of NBD1. NMR spectra of NBD1 lacking the N-terminal tail, NBD1-ΔN, suggest that phosphorylation disrupts interactions of the N-terminal tail with the core of NBD1, a model supported by dynamic light scattering. Increased nucleotide binding of phosphorylated NBD1 and NBD1-ΔN, compared with non-phosphorylated NBD1, suggests that by disrupting the interaction of the NBD core with the N-terminal tail, phosphorylation also exposes the MgATP-binding site on NBD1. These data provide insights into the molecular basis by which phosphorylation of SUR2B NBD1 activates KATP channels.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	37
Volume Number	290
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2015-09-11
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenosine Triphosphate Chemistry Sulfonylurea Receptors Genetics Metabolism Animals Cyclic AMP-Dependent Protein Kinases Ion Channel Gating Physiology Nuclear Magnetic Resonance, Biomolecular Phosphorylation Protein Structure, Tertiary Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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