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J Biol Chem, Vol. 275, Issue 7, 4897-4905, February 18, 2000

Binding and Phosphorylation of a Novel Male Germ Cell-specific cGMP-dependent Protein Kinase-anchoring Protein by cGMP-dependent Protein Kinase I^*

Keizo Yuasa, Kenji Omori, and Noriyuki Yanaka^§¶

From the  Discovery Research Laboratory, Tanabe Seiyaku Co. Ltd., 2-50 Kawagishi 2-chome, Toda, Saitama 335-8505 and the ^§ Discovery Research Laboratory, Tanabe Seiyaku Co. Ltd., 16-89 Kashima 3-chome, Yodogawa-ku, Osaka 532-8505, Japan

cGMP-dependent protein kinase (cGK) is a major cellular receptor of cGMP and plays important roles in cGMP-dependent signal transduction pathways. To isolate the components of the cGMP/cGK signaling pathway such as substrates and regulatory proteins of cGK, we employed the yeast two-hybrid system using cGK-I as a bait and isolated a novel male germ cell-specific 42-kDa protein, GKAP42 (42-kDa cGMP-dependent protein kinase anchoring protein). Although the N-terminal region (amino acids 1-66) of cGK-I is sufficient for the association with GKAP42, GKAP42 could not interact with cGK-I, cGK-II, or cAMP-dependent protein kinase. GKAP42 mRNA is specifically expressed in testis, where it is restricted to the spermatocytes and early round spermatids. Endogenous cGK-I is co-immunoprecipitated with anti-GKAP42 antibody from mouse testis tissue, suggesting that cGK-I physiologically interacts with GKAP42. Immunocytochemical observations revealed that GKAP42 is localized to the Golgi complex and that cGK-I is co-localized to the Golgi complex when coexpressed with GKAP42. Although both cGK-I and -I, but not cAMP-dependent protein kinase, phosphorylated GKAP42 in vitro, GKAP42 was a good substrate only for cGK-I in intact cells, suggesting that the association with kinase protein is required for the phosphorylation in vivo. Finally, we demonstrated that the kinase-deficient mutant of cGK-I stably associates with GKAP42 and that binding of cGMP to cGK-I facilitates their release from GKAP42. These findings suggest that GKAP42 functions as an anchoring protein for cGK-I and that cGK-I may participate in germ cell development through phosphorylation of Golgi-associated proteins such as GKAP42.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AB033130.

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