Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP
Article Abstract:
The Ras-like GTPase, Rap1, is activated by certain extracellular stimuli and may have a function in cellular processes. It is activated by diacylglycerol, calcium and cyclic AMP. Activation of Rap1 by forskolin and cAMP is found to be independent of protein kinase A. The gene encoding a guanine-nucleotide-exchange factor (GEF), Epac, was cloned and was found to contain a homologous cAMP-binding site and domain to domains of known GEFs for Ras and Rap1.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Structure of the cyclic-AMP-responsive exchange factor Epac2 in its auto-inhibited state
Article Abstract:
A three-dimensional structure of full-length Epac2, a 110-kDa protein that contains an amino-terminal regulatory region with two cyclic-nucleotide-binding domains and a carboxyl-terminal catalytic region is presented. The mutational analysis suggested a model for cAMP-induced Epac activation with rigid body movement of the regulatory region, the features of which are universally conserved in cAMP-regulated proteins.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
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A new family of RhoGEFs activates the Rop molecular switch in plants
Article Abstract:
A new family of Rop proteins guanine nucleotide exchange factors (RhoGEF) that are exclusive to plants are described in terms of a unique domain within the RopGEFs, plant-specific Rop nucleotide exchanger (PRONE), which is exclusively active towards members of the Rop nucleotide exchanger. PRONE increases nucleotide dissociation from Rop more than a thousand-fold and forms a tight complex with nucleotide-free Rop.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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