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J. Biol. Chem., Vol. 278, Issue 49, 49230-49238, December 5, 2003

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The Unique Amino-terminal Region of the PDE4D5 cAMP Phosphodiesterase Isoform Confers Preferential Interaction with -Arrestins^*

Graeme B. Bolger¶, Angela McCahill||, Elaine Huston||, York-Fong Cheung||, Theresa McSorley||, George S. Baillie||, and Miles D. Houslay||

From the University of Alabama at Birmingham, Comprehensive Cancer Center, Birmingham, Alabama 35294-3300 and ^||Molecular Pharmacology Group, Division of Biochemistry and Molecular Biology, Wolfson Building, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ, Scotland, United Kingdom

Isoproterenol challenge of Hek-B2 cells causes a transient recruitment of the endogenous PDE4D isoforms found in these cells, namely PDE4D3 and PDE4D5, to the membrane fraction. PDE4D5 provides around 80% of the total PDE4D protein so recruited, although it only comprises about 40% of the total PDE4D protein in Hek-B2 cells. PDE4D5 provides about 80% of the total PDE4D protein found associated with -arrestins immunopurified from Hek-B2, COS1, and A549 cells as well as cardiac myocytes, whereas its overall level in these cells is between 15 and 50% of the total PDE4D protein. Truncation analyses indicate that two sites in PDE4D5 are involved in mediating its interaction with -arrestins, one associated with the common PDE4 catalytic region and the other located within its unique amino-terminal region. Truncation analyses indicate that two sites in -arrestin 2 are involved in mediating its interaction with PDE4D5, one associated with its extreme amino-terminal region and the other located within the carboxyl-terminal domain of the protein. We suggest that the unique amino-terminal region of PDE4D5 allows it to preferentially interact with -arrestins. This specificity appears likely to account for the preferential recruitment of PDE4D5, compared with PDE4D3, to membranes of Hek-B2 cells and cardiac myocytes upon challenge with isoproterenol.

Received for publication, April 10, 2003 , and in revised form, September 11, 2003.

^* This work was supported in part by National Institutes of Health Grant R01-GM58553 (to G. B. B.), by Medical Research Council (UK) Grant G8604010 (to M. D. H.), and by European Union Grants QLG2-CT-2001-02278 and QLK3-CT-2002-02149 (to M. D. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Recipient of Biomedical Research Collaborative Travel Grant 061247/Z/00/Z from the Wellcome Trust, UK.

^¶ To whom correspondence should be addressed: University of Alabama at Birmingham, Comprehensive Cancer Center, WTI 520, 1530 3rd Ave. S., Birmingham, AL 35294-3300. Tel.: 205-975-9375; Fax: 205-975-6911; E-mail: Graeme.Bolger{at}ccc.uab.edu.

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