Cargando…

Casein kinase 1 controls the activation threshold of an α-arrestin by multisite phosphorylation of the interdomain hinge

α-Arrestins play a key role as trafficking adaptors in both yeast and mammals. The yeast Rim8/Art9 α-arrestin mediates the recruitment of endosomal sorting complex required for transport (ESCRT) to the seven-transmembrane protein Rim21 in the ambient pH signaling RIM pathway. ESCRT is believed to fu...

Descripción completa

Detalles Bibliográficos
Autores principales: Herrador, Antonio, Livas, Daniela, Soletto, Lucía, Becuwe, Michel, Léon, Sébastien, Vincent, Olivier
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4472021/
https://www.ncbi.nlm.nih.gov/pubmed/25851600
http://dx.doi.org/10.1091/mbc.E14-11-1552
_version_ 1782376993240645632
author Herrador, Antonio
Livas, Daniela
Soletto, Lucía
Becuwe, Michel
Léon, Sébastien
Vincent, Olivier
author_facet Herrador, Antonio
Livas, Daniela
Soletto, Lucía
Becuwe, Michel
Léon, Sébastien
Vincent, Olivier
author_sort Herrador, Antonio
collection PubMed
description α-Arrestins play a key role as trafficking adaptors in both yeast and mammals. The yeast Rim8/Art9 α-arrestin mediates the recruitment of endosomal sorting complex required for transport (ESCRT) to the seven-transmembrane protein Rim21 in the ambient pH signaling RIM pathway. ESCRT is believed to function as a signaling platform that enables the proteolytic activation of the Rim101 transcription factor upon external alkalization. Here we provide evidence that the pH signal promotes the stable association of Rim8 with Rim21 at the plasma membrane. We show that Rim8 is phosphorylated in a pH-independent but Rim21-dependent manner by the plasma membrane–associated casein kinase 1 (CK1). We further show that this process involves a cascade of phosphorylation events within the hinge region connecting the arrestin domains. Strikingly, loss of casein kinase 1 activity causes constitutive activation of the RIM pathway, and, accordingly, pH signaling is activated in a phosphodeficient Rim8 mutant and impaired in the corresponding phosphomimetic mutant. Our results indicate that Rim8 phosphorylation prevents its accumulation at the plasma membrane at acidic pH and thereby inhibits RIM signaling. These findings support a model in which CK1-mediated phosphorylation of Rim8 contributes to setting a signaling threshold required to inhibit the RIM pathway at acidic pH.
format Online
Article
Text
id pubmed-4472021
institution National Center for Biotechnology Information
language English
publishDate 2015
publisher The American Society for Cell Biology
record_format MEDLINE/PubMed
spelling pubmed-44720212015-08-16 Casein kinase 1 controls the activation threshold of an α-arrestin by multisite phosphorylation of the interdomain hinge Herrador, Antonio Livas, Daniela Soletto, Lucía Becuwe, Michel Léon, Sébastien Vincent, Olivier Mol Biol Cell Articles α-Arrestins play a key role as trafficking adaptors in both yeast and mammals. The yeast Rim8/Art9 α-arrestin mediates the recruitment of endosomal sorting complex required for transport (ESCRT) to the seven-transmembrane protein Rim21 in the ambient pH signaling RIM pathway. ESCRT is believed to function as a signaling platform that enables the proteolytic activation of the Rim101 transcription factor upon external alkalization. Here we provide evidence that the pH signal promotes the stable association of Rim8 with Rim21 at the plasma membrane. We show that Rim8 is phosphorylated in a pH-independent but Rim21-dependent manner by the plasma membrane–associated casein kinase 1 (CK1). We further show that this process involves a cascade of phosphorylation events within the hinge region connecting the arrestin domains. Strikingly, loss of casein kinase 1 activity causes constitutive activation of the RIM pathway, and, accordingly, pH signaling is activated in a phosphodeficient Rim8 mutant and impaired in the corresponding phosphomimetic mutant. Our results indicate that Rim8 phosphorylation prevents its accumulation at the plasma membrane at acidic pH and thereby inhibits RIM signaling. These findings support a model in which CK1-mediated phosphorylation of Rim8 contributes to setting a signaling threshold required to inhibit the RIM pathway at acidic pH. The American Society for Cell Biology 2015-06-01 /pmc/articles/PMC4472021/ /pubmed/25851600 http://dx.doi.org/10.1091/mbc.E14-11-1552 Text en © 2015 Herrador et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.
spellingShingle Articles
Herrador, Antonio
Livas, Daniela
Soletto, Lucía
Becuwe, Michel
Léon, Sébastien
Vincent, Olivier
Casein kinase 1 controls the activation threshold of an α-arrestin by multisite phosphorylation of the interdomain hinge
title Casein kinase 1 controls the activation threshold of an α-arrestin by multisite phosphorylation of the interdomain hinge
title_full Casein kinase 1 controls the activation threshold of an α-arrestin by multisite phosphorylation of the interdomain hinge
title_fullStr Casein kinase 1 controls the activation threshold of an α-arrestin by multisite phosphorylation of the interdomain hinge
title_full_unstemmed Casein kinase 1 controls the activation threshold of an α-arrestin by multisite phosphorylation of the interdomain hinge
title_short Casein kinase 1 controls the activation threshold of an α-arrestin by multisite phosphorylation of the interdomain hinge
title_sort casein kinase 1 controls the activation threshold of an α-arrestin by multisite phosphorylation of the interdomain hinge
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4472021/
https://www.ncbi.nlm.nih.gov/pubmed/25851600
http://dx.doi.org/10.1091/mbc.E14-11-1552
work_keys_str_mv AT herradorantonio caseinkinase1controlstheactivationthresholdofanaarrestinbymultisitephosphorylationoftheinterdomainhinge
AT livasdaniela caseinkinase1controlstheactivationthresholdofanaarrestinbymultisitephosphorylationoftheinterdomainhinge
AT solettolucia caseinkinase1controlstheactivationthresholdofanaarrestinbymultisitephosphorylationoftheinterdomainhinge
AT becuwemichel caseinkinase1controlstheactivationthresholdofanaarrestinbymultisitephosphorylationoftheinterdomainhinge
AT leonsebastien caseinkinase1controlstheactivationthresholdofanaarrestinbymultisitephosphorylationoftheinterdomainhinge
AT vincentolivier caseinkinase1controlstheactivationthresholdofanaarrestinbymultisitephosphorylationoftheinterdomainhinge