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Vol. 56, Issue 3, 644-650, September 1999

The N Terminus Domain of Type VI Adenylyl Cyclase Mediates Its Inhibition by Protein Kinase C

Hsing-Lin Lai,1 Ting-Hui Lin,1 2 Yu-Ya Kao, Wu-Ja Lin, Ming-Jing Hwang, and Yijuang Chern

Division of Neuroscience, Institute of Biomedical Sciences, Academia Sinica, Taipei (H.-L. L., T.-H. L., W.-J. L., M.-J. H., Y.C.); and Institute of Neuroscience, National Yang-Ming University, Taipei 112, (Y.-Y. K.) Taiwan, Republic of China

Previous results from our laboratory have shown that phosphorylation of type VI adenylyl cyclase (ACVI) by protein kinase C (PKC) caused suppression of adenylyl cyclase activity. In the present study, we investigated the role of the N terminus cytosolic domain of ACVI in this PKC-mediated inhibition of ACVI. Removal of amino acids 1 to 86 of ACVI or mutation of Ser10 (a potential PKC phosphorylation site) into alanine significantly relieved the PKC-mediated inhibition and markedly reduced the PKC-evoked protein phosphorylation. PKC also effectively phosphorylated a recombinant N terminus cytosolic domain (amino acids 1-160) protein of ACVI and a synthetic peptide representing Ser10. In addition, the amino acids 1 to 86 truncated mutant exhibited kinetic properties similar to those of the wild type. Taken together, these data demonstrate that the highly variable N terminus cytoplasmic domain of ACVI is a regulatory domain with a critical role in PKC-mediated suppression, which is a hallmark of this adenylyl cyclase isozyme. In addition, Ser10 was found to serve as an acceptor for the PKC-mediated phosphorylating transfer of ACVI.

Copyright © 1999 by The American Society for Pharmacology and Experimental Therapeutics


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