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Originally published In Press as doi:10.1074/jbc.M011252200 on February 7, 2001

J. Biol. Chem., Vol. 276, Issue 20, 17332-17338, May 18, 2001
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Identification of Sperm-specific Proteins That Interact with A-kinase Anchoring Proteins in a Manner Similar to the Type II Regulatory Subunit of PKA*

Daniel W. CarrDagger §, Akiko Fujita, Carrie L. StentzDagger , Greg A. LibertyDagger , Gary E. Olson||, and Shuh Narumiya

From the Dagger  Veterans Affairs Medical Center and Oregon Health Sciences University, Portland, Oregon 97201, the  Department of Pharmacology, Kyoto University Faculty of Medicine, Kyoto 606-8501, Japan, and the || Department of Cell Biology, Vanderbilt University, Nashville, Tennessee 37232

The cAMP-dependent protein kinase (PKA) is targeted to specific subcellular compartments through its interaction with A-kinase anchoring proteins (AKAPs). AKAPs contain an amphipathic helix domain that binds to the type II regulatory subunit of PKA (RII). Synthetic peptides containing this amphipathic helix domain bind to RII with high affinity and competitively inhibit the binding of PKA with AKAPs. Addition of these anchoring inhibitor peptides to spermatozoa inhibits motility (Vijayaraghavan, S., Goueli, S. A., Davey, M. P., and Carr, D. W. (1997) J. Biol. Chem. 272, 4747-4752). However, inhibition of the PKA catalytic activity does not mimic these peptides, suggesting that the peptides are disrupting the interaction of AKAP(s) with proteins other than PKA. Using the yeast two-hybrid system, we have now identified two sperm-specific human proteins that interact with the amphipathic helix region of AKAP110. These proteins, ropporin (a protein previously shown to interact with the Rho signaling pathway) and AKAP-associated sperm protein, are 39% identical to each other and share a strong sequence similarity with the conserved domain on the N terminus of RII that is involved in dimerization and AKAP binding. Mutation of conserved residues in ropporin or RII prevents binding to AKAP110. These data suggest that sperm contains several proteins that bind to AKAPs in a manner similar to RII and imply that AKAPs may have additional and perhaps unique functions in spermatozoa.

* This research was supported by National Institutes of Health Grants HD36408 (to D. W. C.) and HD20419 (to G. E. O.) and by a grant-in-aid for specially promoted research from the Ministry of Education, Culture, Science and Sports of Japan (to S. N.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF231410 and AF239723.

§ To whom correspondence should be addressed: Veterans Administration Medical Center, R&D-8, 3710 SW Veterans Hospital Rd., Portland, OR 97201. Tel.: 503-721-7918; Fax, 503-721-1082; E-mail: carrd@ohsu.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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