Endosomal GPCR signaling turned off by negative feedback actions of PKA and v-ATPase

The PTH receptor is one of the first GPCR found to sustain cAMP signaling after internalization of the ligand–receptor complex in endosomes. This unexpected model is adding a new dimension on how we think about GPCR signaling, but its mechanism is incompletely understood. We report here that endosom...

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Autores principales: Gidon, Alexandre, Al-Bataineh, Mohammad M., Jean-Alphonse, Frederic G., Stevenson, Hilary, Watanabe, Tomoyuki, Louet, Claire, Khatri, Ashok, Calero, Guillermo, Pastor-Soler, Núria M., Gardella, Thomas J., Vilardaga, Jean-Pierre
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2014
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4138287/
https://www.ncbi.nlm.nih.gov/pubmed/25064832
http://dx.doi.org/10.1038/nchembio.1589
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author Gidon, Alexandre
Al-Bataineh, Mohammad M.
Jean-Alphonse, Frederic G.
Stevenson, Hilary
Watanabe, Tomoyuki
Louet, Claire
Khatri, Ashok
Calero, Guillermo
Pastor-Soler, Núria M.
Gardella, Thomas J.
Vilardaga, Jean-Pierre
author_facet Gidon, Alexandre
Al-Bataineh, Mohammad M.
Jean-Alphonse, Frederic G.
Stevenson, Hilary
Watanabe, Tomoyuki
Louet, Claire
Khatri, Ashok
Calero, Guillermo
Pastor-Soler, Núria M.
Gardella, Thomas J.
Vilardaga, Jean-Pierre
author_sort Gidon, Alexandre
collection PubMed
description The PTH receptor is one of the first GPCR found to sustain cAMP signaling after internalization of the ligand–receptor complex in endosomes. This unexpected model is adding a new dimension on how we think about GPCR signaling, but its mechanism is incompletely understood. We report here that endosomal acidification mediated by the PKA action on the v-ATPase provides a negative feedback mechanism by which endosomal receptor signaling is turned-off.
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spelling pubmed-41382872015-03-01 Endosomal GPCR signaling turned off by negative feedback actions of PKA and v-ATPase Gidon, Alexandre Al-Bataineh, Mohammad M. Jean-Alphonse, Frederic G. Stevenson, Hilary Watanabe, Tomoyuki Louet, Claire Khatri, Ashok Calero, Guillermo Pastor-Soler, Núria M. Gardella, Thomas J. Vilardaga, Jean-Pierre Nat Chem Biol Article The PTH receptor is one of the first GPCR found to sustain cAMP signaling after internalization of the ligand–receptor complex in endosomes. This unexpected model is adding a new dimension on how we think about GPCR signaling, but its mechanism is incompletely understood. We report here that endosomal acidification mediated by the PKA action on the v-ATPase provides a negative feedback mechanism by which endosomal receptor signaling is turned-off. 2014-07-27 2014-09 /pmc/articles/PMC4138287/ /pubmed/25064832 http://dx.doi.org/10.1038/nchembio.1589 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Gidon, Alexandre
Al-Bataineh, Mohammad M.
Jean-Alphonse, Frederic G.
Stevenson, Hilary
Watanabe, Tomoyuki
Louet, Claire
Khatri, Ashok
Calero, Guillermo
Pastor-Soler, Núria M.
Gardella, Thomas J.
Vilardaga, Jean-Pierre
Endosomal GPCR signaling turned off by negative feedback actions of PKA and v-ATPase
title Endosomal GPCR signaling turned off by negative feedback actions of PKA and v-ATPase
title_full Endosomal GPCR signaling turned off by negative feedback actions of PKA and v-ATPase
title_fullStr Endosomal GPCR signaling turned off by negative feedback actions of PKA and v-ATPase
title_full_unstemmed Endosomal GPCR signaling turned off by negative feedback actions of PKA and v-ATPase
title_short Endosomal GPCR signaling turned off by negative feedback actions of PKA and v-ATPase
title_sort endosomal gpcr signaling turned off by negative feedback actions of pka and v-atpase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4138287/
https://www.ncbi.nlm.nih.gov/pubmed/25064832
http://dx.doi.org/10.1038/nchembio.1589
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