NDLI: Phosphorylation-induced conformational changes in Rap1b: allosteric effects on switch domains and effector loop.

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Phosphorylation-induced conformational changes in Rap1b: allosteric effects on switch domains and effector loop.

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Phosphorylation-induced conformational changes in Rap1b: allosteric effects on switch domains and effector loop.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ribeiro-neto, Fernando Hochbaum, Daniel Wong, Sergio Li, Sheng Edreira, Martin M. Altschuler, Daniel L. Gorfe, Alemayehu A. Woods, Virgil L.
Description	Author Affiliation: Edreira MM ( Department of Pharmacology and Chemical Biology, School of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, USA.)
Abstract	Rap1b has been implicated in the transduction of the cAMP mitogenic response. Agonists that increase intracellular cAMP rapidly activate (i.e. GTP binding) and phosphorylate Rap1b on Ser(179) at its C terminus. cAMP-dependent protein kinase (PKA)-mediated phosphorylation of Rap1b is required for cAMP-dependent mitogenesis, tumorigenesis, and inhibition of AKT activity. However, the role of phosphorylation still remains unknown. In this study, we utilized amide hydrogen/deuterium exchange mass spectroscopy (DXMS) to assess potential conformational changes and/or mobility induced by phosphorylation. We report here DXMS data comparing exchange rates for PKA-phosphorylated (Rap1-P) and S179D phosphomimetic (Rap1-D) Rap1b proteins. Rap1-P and Rap1-D behaved exactly the same, revealing an increased exchange rate in discrete regions along the protein; these regions include a domain around the phosphorylation site and unexpectedly the two switch loops. Thus, local effects induced by Ser(179) phosphorylation communicate allosterically with distal domains involved in effector interaction. These results provide a mechanistic explanation for the differential effects of Rap1 phosphorylation by PKA on effector protein interaction.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	40
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-10-02
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Rap GTP-Binding Proteins Chemistry Metabolism Allosteric Regulation Amino Acid Sequence Cell Line Deuterium Exchange Measurement Mass Spectrometry Models, Molecular Phosphorylation Protein Conformation Protein Structure, Tertiary Research Support, N.I.H., Extramural 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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