Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5 |
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| Authors: | Graeme B Bolger Angela McCahill Stephen J Yarwood Michael R Steele Jim Warwicker Miles D Houslay |
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| Affiliation: | (1) Molecular Pharmacology Group, Division of Biochemistry & Molecular Biology, Davidson Building, Institute of Biomedical & Life Sciences, University of Glasgow, Glasgow, G12 8QQ, Scotland, UK;(2) Dept of Biomolecular Sciences, UMIST, Sackville Street, Manchester, M60 1QD, UK;(3) Veterans Affairs Medical Center, Huntsman Cancer Institute, Departments of Medicine (Division of Oncology) and Oncological Science, University of Utah Health Sciences Center, Salt Lake City, UT 84148, USA;(4) University of Alabama at Birmingham, Comprehensive Cancer Center, WTI 520, 1530 3rd Ave. S., Birmingham, AL 35294-3300, USA |
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| Abstract: | Background The cyclic AMP specific phosphodiesterase, PDE4D5 interacts with the β-propeller protein RACK1 to form a signaling scaffold complex in cells. Two-hybrid analysis of truncation and mutant constructs of the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5 were used to define a domain conferring interaction with the signaling scaffold protein, RACK1. |
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