Regular ArticleActivation of the Small G Protein Rap1 in Dog Thyroid Cells by Both cAMP-Dependent and -Independent Pathways
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Exchange proteins directly activated by cAMP induce the proliferation of rat anterior pituitary GH3 cells via the activation of extracellular signal-regulated kinase
2017, Biochemical and Biophysical Research CommunicationsCitation Excerpt :cAMP activated MAPK pathway through the stimulation of B-Raf, which was itself activated by Rap1 [21,22]. Because Epac could directly target and activate Rap [23], we determined the role of B-Raf in Epac mediated ERK phosphorylation. Our data show that the inhibition of B-Raf could totally abolish Epac mediated phosphorylation of ERK, and also inhibit 8-pCPT induced GH3 cell proliferation.
Rap-linked cAMP signaling Epac proteins: Compartmentation, functioning and disease implications
2011, Cellular SignallingEpac, in synergy with cAMP-dependent protein kinase (PKA), is required for cAMP-mediated mitogenesis
2008, Journal of Biological ChemistryCitation Excerpt :In PCCL3, the PKA-independent effect of cAMP in mitogenesis appears to solely involve Epac activation of Rap1b. PKA-independent Epac activation of Rap1 by cAMP has been reported in other thyroid cells (20, 22–24, 29). Surprisingly, in primary dog thyrocyte, apart from Rap1 activation, Epac action played no apparent role in any aspect of cAMP biology, including mitogenesis (30).
Role of Rap1 in promoting sickle red blood cell adhesion to laminin via BCAM/LU
2005, BloodCitation Excerpt :To understand Rap1 function in SS RBCs, it is important to identify the pathway by which Rap1 becomes activated. A common upstream activator of Rap1 in a number of cell types is cAMP.22,23 Also, our recent studies have shown that that cAMP production in SS RBCs enhances SS RBC adhesion to laminin in a significant subset of patients (46% of the SCD patients studied).1
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These authors collaborated equally in this work.