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Bicarbonate-responsive "soluble" adenylyl cyclase defines a nuclear cAMP microdomain

¹ Department of Pharmacology, Joan and Sanford I. Weill Medical College and Graduate School of Medical Sciences of Cornell University, New York, NY 10021
² Tri-Institutional MD/PhD Program, Joan and Sanford I. Weill Medical College and Graduate School of Medical Sciences of Cornell University, New York, NY 10021
³ Department of Cell and Developmental Biology, Joan and Sanford I. Weill Medical College and Graduate School of Medical Sciences of Cornell University, New York, NY 10021

Address correspondence to Lonny R. Levin, Dept. of Pharmacology, Joan and Sanford I. Weill Medical College and Graduate School of Medical Sciences of Cornell University, 1300 York Ave., New York, NY 10021. Tel.: (212) 746-6752. Fax: (212) 747-6241. email: llevin{at}med.cornell.edu

Bicarbonate-responsive "soluble" adenylyl cyclase resides, in part, inside the mammalian cell nucleus where it stimulates the activity of nuclear protein kinase A to phosphorylate the cAMP response element binding protein (CREB). The existence of this complete and functional, nuclear-localized cAMP pathway establishes that cAMP signals in intracellular microdomains and identifies an alternate pathway leading to CREB activation.

Key Words: CREB; PKA; gene expression; compartmentalization; signal transduction

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