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J. Biol. Chem., Vol. 277, Issue 13, 11497-11504, March 29, 2002
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From the The recent discovery of Epac, a novel cAMP
receptor protein, opens up a new dimension in studying cAMP-mediated
cell signaling. It is conceivable that many of the cAMP functions
previously attributed to cAMP-dependent protein kinase
(PKA) are in fact also Epac-dependent. The finding of an
additional intracellular cAMP receptor provides an opportunity to
further dissect the divergent roles that cAMP exerts in different cell
types. In this study, we probed cross-talk between cAMP signaling and
the phosphatidylinositol 3-kinase/PKB pathways. Specifically, we
examined the modulatory effects of cAMP on PKB activity by monitoring
the specific roles that Epac and PKA play individually in regulating
PKB activity. Our study suggests a complex regulatory scheme in which
Epac and PKA mediate the opposing effects of cAMP on PKB regulation.
Activation of Epac leads to a phosphatidylinositol
3-kinase-dependent PKB activation, while stimulation of PKA
inhibits PKB activity. Furthermore, activation of PKB by Epac requires
the proper subcellular targeting of Epac. The opposing effects of Epac
and PKA on PKB activation provide a potential mechanism for the cell
type-specific differential effects of cAMP. It is proposed that the net
outcome of cAMP signaling is dependent upon the dynamic abundance and
distribution of intracellular Epac and PKA.
Differential Signaling of Cyclic AMP
OPPOSING EFFECTS OF EXCHANGE PROTEIN DIRECTLY ACTIVATED BY
CYCLIC AMP AND cAMP-DEPENDENT PROTEIN KINASE ON PROTEIN KINASE B
ACTIVATION*
,,
Department of Pharmacology and Toxicology
and Sealy Center for Structural Biology, School of Medicine, The
University of Texas Medical Branch, Galveston, Texas 77555, the
§ Department of Pharmacology, University of Pennsylvania
School of Medicine, Philadelphia, Pennsylvania 19104-6084, and the
¶ Department of Biochemistry and Molecular Biology and Walther
Oncology Center, Indiana University School of Medicine,
Indianapolis, Indiana 46202-5122
*
This work was supported in part by startup funds from the
Department of Pharmacology and Toxicology, The University of Texas Medical Branch, a recruitment grant from the John Sealy Memorial Endorsement Fund, American Cancer Society Research Scholar Grant RSG-01-035-01-TBE and Center Grant ES06676 from the National Institutes of Health.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.
To whom correspondence should be addressed: Dept. of
Pharmacology and Toxicology, The University of Texas Medical Branch, 301 University Blvd., Galveston, TX 77555-1031. Tel.: 409-772-9656; Fax: 409-772-9642; E-mail: xcheng@utmb.edu.
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