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Involvement of the exomer complex in the polarized transport of Ena1 required for Saccharomyces cerevisiae survival against toxic cations.
Anton, Carlos; Zanolari, Bettina; Arcones, Irene; Wang, Congwei; Mulet, Jose Miguel; Spang, Anne; Roncero, Cesar.
Afiliación
  • Anton C; Instituto de Biología Funcional y Genómica (IBFG) and Departamento de Microbiología y Genética, CSIC-Universidad de Salamanca, 37007 Salamanca, Spain.
  • Zanolari B; Biozentrum, Growth & Development, University of Basel, CH-4056 Basel, Switzerland.
  • Arcones I; Instituto de Biología Funcional y Genómica (IBFG) and Departamento de Microbiología y Genética, CSIC-Universidad de Salamanca, 37007 Salamanca, Spain.
  • Wang C; Biozentrum, Growth & Development, University of Basel, CH-4056 Basel, Switzerland.
  • Mulet JM; Instituto de Biología Molecular y Celular de Plantas, CSIC-Universitat Politécnica de Valencia, 46011 Valencia, Spain.
  • Spang A; Biozentrum, Growth & Development, University of Basel, CH-4056 Basel, Switzerland crm@usal.es anne.spang@unibas.ch.
  • Roncero C; Instituto de Biología Funcional y Genómica (IBFG) and Departamento de Microbiología y Genética, CSIC-Universidad de Salamanca, 37007 Salamanca, Spain crm@usal.es anne.spang@unibas.ch.
Mol Biol Cell ; 28(25): 3672-3685, 2017 Dec 01.
Article en En | MEDLINE | ID: mdl-29021337
ABSTRACT
Exomer is an adaptor complex required for the direct transport of a selected number of cargoes from the trans-Golgi network (TGN) to the plasma membrane in Saccharomyces cerevisiae However, exomer mutants are highly sensitive to increased concentrations of alkali metal cations, a situation that remains unexplained by the lack of transport of any known cargoes. Here we identify several HAL genes that act as multicopy suppressors of this sensitivity and are connected to the reduced function of the sodium ATPase Ena1. Furthermore, we find that Ena1 is dependent on exomer function. Even though Ena1 can reach the plasma membrane independently of exomer, polarized delivery of Ena1 to the bud requires functional exomer. Moreover, exomer is required for full induction of Ena1 expression after cationic stress by facilitating the plasma membrane recruitment of the molecular machinery involved in Rim101 processing and activation of the RIM101 pathway in response to stress. Both the defective localization and the reduced levels of Ena1 contribute to the sensitivity of exomer mutants to alkali metal cations. Our work thus expands the spectrum of exomer-dependent proteins and provides a link to a more general role of exomer in TGN organization.
Asunto(s)

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / ATPasa Intercambiadora de Sodio-Potasio / Proteínas de Saccharomyces cerevisiae / Proteínas Adaptadoras del Transporte Vesicular Idioma: En Revista: Mol Biol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2017 Tipo del documento: Article País de afiliación: España

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Saccharomyces cerevisiae / ATPasa Intercambiadora de Sodio-Potasio / Proteínas de Saccharomyces cerevisiae / Proteínas Adaptadoras del Transporte Vesicular Idioma: En Revista: Mol Biol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 2017 Tipo del documento: Article País de afiliación: España