2012
DOI: 10.1074/jbc.m112.401547
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Regulation of RhoA Signaling by the cAMP-dependent Phosphorylation of RhoGDIα

Abstract: Background: cAMP-induced phosphorylation of RhoA has been considered to inhibit RhoA signaling, causing cell rounding. Results: Knockdown of RhoGDI␣ blocks cAMP-induced cell rounding, and RhoGDI␣-WT expression but not RhoGDI␣-S174A expression recovers. Conclusion: Phosphorylation of RhoGDI␣ likely inhibits RhoA by stabilizing a active RhoA-RhoGDI␣ complex. Significance: This may underlie G s /cAMP-induced cross-talk with G q /G 13 /RhoA signaling.

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Cited by 48 publications
(45 citation statements)
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References 53 publications
(73 reference statements)
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“…*p \ 0.05 compared with 0 h or control group, # p \ 0.05 compared with PAN group. 2Me: 2Me-cAMP, pCPT: pCPT-cAMP PKA-dependent or -independent manner to activate RhoA [25]. Our results supported cAMP/PKA signaling activated RhoA.…”
Section: Discussionsupporting
confidence: 83%
“…*p \ 0.05 compared with 0 h or control group, # p \ 0.05 compared with PAN group. 2Me: 2Me-cAMP, pCPT: pCPT-cAMP PKA-dependent or -independent manner to activate RhoA [25]. Our results supported cAMP/PKA signaling activated RhoA.…”
Section: Discussionsupporting
confidence: 83%
“…PKA-mediated phosphorylation on Ser174 of RhoGDI1 stabilizes a RhoA-RhoGDI1 complex, thereby inhibiting RhoA signalling 126 . This mechanism might complement the PKA-mediated phosphoryl ation of RhoA described at the beginning of this Review, which enhances its interaction with RhoGDI.…”
Section: Dynamic Regulation Of Rhogdis By Post-translational Modificamentioning
confidence: 99%
“…cAMP-induced activation of PKA is known to promote dramatic morphological changes in cells, including loss of stress fibers and cell-rounding. [13] In the absence of illumination, Cbl-cAMP has no effect on the morphology of REF52 cells. Upon illumination in the presence of Cbl-cAMP , REF52 cells undergo the expected loss of their stress fiber content as well as cell shrinking and rounding (Fig.…”
mentioning
confidence: 99%