NDLI: Sensing Domain Dynamics in Protein Kinase A-Iα Complexes by Solution X-ray $Scattering^{*}$

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Sensing Domain Dynamics in Protein Kinase A-Iα Complexes by Solution X-ray $Scattering^{*}$

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Yang, Jie Cheng, Cecilia Y. Taylor, Susan S. Blumenthal, Donald K.
Description	Author Affiliation: Cheng CY ( Departments of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92037-0654, USA.)
Abstract	The catalytic (C) and regulatory (R) subunits of protein kinase A are exceptionally dynamic proteins. Interactions between the R- and C-subunits are regulated by cAMP binding to the two cyclic nucleotide-binding domains in the R-subunit. Mammalian cells express four different isoforms of the R-subunit (RIα, RIβ, RIIα, and RIIβ) that all interact with the C-subunit in different ways. Here, we investigate the dynamic behavior of protein complexes between RIα and C-subunits using small angle x-ray scattering. We show that a single point mutation in RIα, R333K (which alters the cAMP-binding properties of Domain B) results in a compact shape compared with the extended shape of the wild-type R·C complex. A double mutant complex that disrupts the interaction site between the C-subunit and Domain B in RIα, $RIα_{AB}R333K·C(K285P),$ results in a broader P(r) curve that more closely resembles the P(r) profiles of wild-type complexes. These results together suggest that interactions between RIα Domain B and the C-subunit in the RIα·C complex involve large scale dynamics that can be disrupted by single point mutations in both proteins. In contrast to RIα·C complexes. Domain B in the RIIβ·C heterodimer is not dynamic and is critical for both inhibition and complex formation. Our study highlights the functional differences of domain dynamics between protein kinase A isoforms, providing a framework for elucidating the global organization of each holoenzyme and the cross-talk between the R- and C-subunits.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	51
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-12-18
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cyclic AMP-Dependent Protein Kinase RIalpha Subunit Chemistry Animals Cyclic AMP Genetics Metabolism Isoenzymes Point Mutation Protein Structure, Quaternary Physiology Protein Structure, Tertiary X-Ray Diffraction 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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