Submit Data |  Help |  Video Tutorials |  News |  Publications |  FTP Download |  REST API |  Citing RGD |  Contact   

A family of cAMP-binding proteins that directly activate Rap1.

Authors: Kawasaki, H  Springett, GM  Mochizuki, N  Toki, S  Nakaya, M  Matsuda, M  Housman, DE  Graybiel, AM 
Citation: Kawasaki H, etal., Science 1998 Dec 18;282(5397):2275-9.
Pubmed: (View Article at PubMed) PMID:9856955

cAMP (3',5' cyclic adenosine monophosphate) is a second messenger that in eukaryotic cells induces physiological responses ranging from growth, differentiation, and gene expression to secretion and neurotransmission. Most of these effects have been attributed to the binding of cAMP to cAMP-dependent protein kinase A (PKA). Here, a family of cAMP-binding proteins that are differentially distributed in the mammalian brain and body organs and that exhibit both cAMP-binding and guanine nucleotide exchange factor (GEF) domains is reported. These cAMP-regulated GEFs (cAMP-GEFs) bind cAMP and selectively activate the Ras superfamily guanine nucleotide binding protein Rap1A in a cAMP-dependent but PKA-independent manner. Our findings suggest the need to reformulate concepts of cAMP-mediated signaling to include direct coupling to Ras superfamily signaling.


Gene Ontology Annotations
Objects Annotated
Objects referenced in this article

Additional Information

RGD Object Information
RGD ID: 632397
Created: 2003-08-29
Species: All species
Last Modified: 2004-05-25
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.