Anton, C.; Zanolari, B.; Arcones, I.; Wang, C.; Mulet, JM.; Spang, A.; Roncero, C. (2017). Involvement of the exomer complex in the polarized transport of Ena1 required for Saccharomyces cerevisiae survival against toxic cations. Molecular Biology of the Cell. 28(25):3672-3685. https://doi.org/10.1091/mbc.E17-09-0549
Por favor, use este identificador para citar o enlazar este ítem: http://hdl.handle.net/10251/149933
Title:
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Involvement of the exomer complex in the polarized transport of Ena1 required for Saccharomyces cerevisiae survival against toxic cations
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Author:
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Anton, C.
Zanolari, B.
Arcones, I.
Wang, C.
Mulet, José Miguel
Spang, A.
Roncero, C.
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UPV Unit:
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Universitat Politècnica de València. Departamento de Biotecnología - Departament de Biotecnologia
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Issued date:
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Abstract:
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[EN] 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 ...[+]
[EN] 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.
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Subjects:
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Vesicle cargo adapter
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Plasma-Membrane
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Salt tolerance
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RIM101 pathway
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Potassium transporter
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Chitin synthesis
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Gene disruption
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Golgi network
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Coat proteins
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Yeast
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Copyrigths:
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Reconocimiento - No comercial - Compartir igual (by-nc-sa)
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Source:
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Molecular Biology of the Cell. (issn:
1059-1524
)
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DOI:
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10.1091/mbc.E17-09-0549
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Publisher:
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American Society for Cell Biology
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Publisher version:
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https://doi.org/10.1091/mbc.E17-09-0549
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Project ID:
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SNSF/31003A-141207
...[+]
SNSF/31003A-141207
SNSF/310030B-163480
JCYL/SA073U14
CICYT/BFU2013-48582-C2-1-P
UPV-VIN/PAID-06-10-1496
UPV-VIN/2726
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Thanks:
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We acknowledge Emma Keck for English language revision. We also thank members of the Translucent group, J. Arino, J. Ramos, and L. Yenush, for many useful discussions throughout this work and especially L. Yenush for her ...[+]
We acknowledge Emma Keck for English language revision. We also thank members of the Translucent group, J. Arino, J. Ramos, and L. Yenush, for many useful discussions throughout this work and especially L. Yenush for her generous gift of strains and reagents. The help of O. Vincent was essential for developing the work involving RIM101. We also thank R. Valle for her technical assistance at the CR Laboratory. M. Trautwein is acknowledged for data acquisition and discussions during the early stages of the project. C.A. is supported by a USAL predoctoral fellowship. Work at the Spang laboratory was supported by the University of Basel and the Swiss National Science Foundation (31003A-141207 and 310030B-163480). C.R. was supported by grant SA073U14 from the Regional Government of Castilla y Leon and by grant BFU2013-48582-C2-1-P from the CICYT/FEDER Spanish program. J.M.M. acknowledges the financial support from Universitat Politecnica de Valencia project PAID-06-10-1496.
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Type:
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Artículo
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