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J. Biol. Chem., Vol. 279, Issue 26, 27621-27632, June 25, 2004

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Neuronal Microtubule-associated Protein 2D Is a Dual A-kinase Anchoring Protein Expressed in Rat Ovarian Granulosa Cells^*

Lisa M. Salvador, Maxfield P. Flynn, Jesús Avila¶, Scott Reierstad, Evelyn T. Maizels, Hena Alam, Youngkyu Park, John D. Scott||, Daniel W. Carr**, and Mary Hunzicker-Dunn

From the Department of Cell and Molecular Biology, Northwestern University Feinberg School of Medicine, Chicago, Illinois 60611, ^**Veterans Affairs Medical Center and Oregon Health and Science University, Portland, Oregon 97201-3098, ^¶Centro de Biologia Molecular "Severo Ochoa," Facultad de Ciencias, Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain, ^||Howard Hughes Medical Institute, Vollum Institute, Oregon Health and Science University, Portland, Oregon 97201-3098

A-kinase anchoring proteins (AKAPs) function to target protein kinase A (PKA) to specific locations within the cell. AKAPs are functionally identified by their ability to bind the type II regulatory subunits (RII) of PKA in an in vitro overlay assay. We previously showed that follicle-stimulating hormone (FSH) induces the expression of an 80-kDa AKAP (AKAP 80) in ovarian granulosa cells as they mature from a preantral to a preovulatory phenotype. In this report, we identify AKAP 80 as microtubule-associated protein 2D (MAP2D), a low molecular weight splice variant of the neuronal MAP2 protein. MAP2D is induced in granulosa cells by dexamethasone and by FSH in a time-dependent manner that mimics that of AKAP 80, and immunoprecipitation of MAP2D depletes extracts of AKAP 80. MAP2D is the only MAP2 protein present in ovaries and is localized to granulosa cells of preovulatory follicles and to luteal cells. MAP2D is concentrated at the Golgi apparatus along with RI and RII and, based on coimmunoprecipitation results, appears to bind both RI and RII in granulosa cells. Reduced expression of MAP2D resulting from treatment of granulosa cells with antisense oligonucleotides to MAP2 inhibited the phosphorylation of cAMP-response element-binding protein. These results suggest that this classic neuronal RII AKAP is a dual RI/RII AKAP that performs unique functions in ovarian granulosa cells that contribute to the preovulatory phenotype.

Received for publication, March 17, 2004

^* This work was funded by National Institutes of Health (NIH) Grant P01 HD21921 (to M. H. D.), a Veterans Affairs Merit Grant and NIH Grants HD36408 (to D. W. C.), and NIH Grant DK48239 (to J. D. S.). 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.

Present address: Center for Research in Reproduction and Women's Health, BRB II/II Rm. 1349A, 421 Curie Blvd., Philadelphia, PA 19104.

To whom correspondence should be addressed: Northwestern University Medical School, 303 E. Chicago Ave., Chicago, IL 60611. Tel.: 312-503-8940; Fax: 312-503-0566; mhd{at}Northwestern.edu.

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