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Access through your institution Buy or subscribe Triggered by their observation that serum promotes the dephosphorylation and nuclear translocation of YAP, the authors identified
lysophosphatidic acid (LPA) as the serum component that inhibits the kinase activity of LATS1. Similarly, sphingosine 1-phosphate (S1P) was found to induce YAP dephosphorylation, suggesting
that G protein-coupled receptor (GPCR) ligands such as S1P and LPA might control YAP-dependent transcription. Indeed, blocking LPA receptors inhibited YAP activity, whereas ectopic
expression of LPA and S1P receptors induced YAP activity. Moreover, YAP expression was essential for LPA-induced gene expression and its downstream effects. Next, Guan and colleagues
investigated the role of Gα proteins downstream of GPCRs in the regulation of YAP phosphorylation. Overexpression of active G12/13 proteins (which are downstream of the LPA and S1P
receptors) was sufficient for YAP dephosphorylation and nuclear translocation. Moreover, activation of RHO GTPases by Gα proteins was also essential for YAP dephosphorylation. Interestingly,
RHO GTPases control the dynamics of the actin cytoskeleton, and changes in LATS1 and YAP activity observed upon addition of an actin-depolymerizing factor suggest that normal actin dynamics
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RESEARCH PAPER * Yu, F. -X. et al. Regulation of the Hippo–Yap pathway by G-protein-coupled receptor signaling. _Cell_ 2 Aug 2012 (doi:10.1016/j.cell.2012.06.037) Article CAS Google
Scholar Download references AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * Associate Editor, Nature Reviews Immunology, Maria Papatriantafyllou Authors * Maria Papatriantafyllou View author
publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Papatriantafyllou, M. Hippo
cues. _Nat Rev Mol Cell Biol_ 13, 602–603 (2012). https://doi.org/10.1038/nrm3430 Download citation * Published: 22 August 2012 * Issue Date: October 2012 * DOI:
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