Response to hyperosmotic stress

An appropriate response and adaptation to hyperosmolarity, i.e., an external osmolarity that is higher than the physiological range, can be a matter of life or death for all cells. It is especially important for free-living organisms such as the yeast Saccharomyces cerevisiae. When exposed to hypero...

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Detalhes bibliográficos
Autores: Saito, Haruo, Posas Garriga, Francesc
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2012
País:España
Recursos:Universitat Pompeu Fabra
Repositorio:Repositorio Digital de la UPF
OAI Identifier:oai:repositori.upf.edu:10230/25359
Acesso em linha:http://hdl.handle.net/10230/25359
http://dx.doi.org/10.1534/genetics.112.140863
Access Level:acceso abierto
Palavra-chave:Saccharomyces cerevisiae -- Fisiologia
Proteïnes quinases
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spelling Response to hyperosmotic stressSaito, HaruoPosas Garriga, FrancescSaccharomyces cerevisiae -- FisiologiaProteïnes quinasesAn appropriate response and adaptation to hyperosmolarity, i.e., an external osmolarity that is higher than the physiological range, can be a matter of life or death for all cells. It is especially important for free-living organisms such as the yeast Saccharomyces cerevisiae. When exposed to hyperosmotic stress, the yeast initiates a complex adaptive program that includes temporary arrest of cell-cycle progression, adjustment of transcription and translation patterns, and the synthesis and retention of the compatible osmolyte glycerol. These adaptive responses are mostly governed by the high osmolarity glycerol (HOG) pathway, which is composed of membrane-associated osmosensors, an intracellular signaling pathway whose core is the Hog1 MAP kinase (MAPK) cascade, and cytoplasmic and nuclear effector functions. The entire pathway is conserved in diverse fungal species, while the Hog1 MAPK cascade is conserved even in higher eukaryotes including humans. This conservation is illustrated by the fact that the mammalian stress-responsive p38 MAPK can rescue the osmosensitivity of hog1Δ mutations in response to hyperosmotic challenge. As the HOG pathway is one of the best-understood eukaryotic signal transduction pathways, it is useful not only as a model for analysis of osmostress responses, but also as a model for mathematical analysis of signal transduction pathways. In this review, we have summarized the current understanding of both the upstream signaling mechanism and the downstream adaptive responses to hyperosmotic stress in yeast.The laboratory of H.S. is supported by Grants-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology of Japan. The laboratory of F.P. is supported by grants from the Ministerio de Economia y Competitividad (Spanish Government), the Consolider Ingenio 2010 Programme, and a FP7 UNICELLSYS grant. F.P. is also supported by the Fundación Marcelino Botín and by the Acadèmia program from Institució Catalana de Recerca i Estudis Avançats (Generalitat de Catalunya).Genetics Society of America201520152012info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttp://hdl.handle.net/10230/25359http://dx.doi.org/10.1534/genetics.112.140863reponame:Repositorio Digital de la UPFinstname:Universitat Pompeu FabraInglésGenetics. 2012;192(2):289-318info:eu-repo/grantAgreement/EC/FP7/201142© 2012 Saito et al. This is an open-access article.info:eu-repo/semantics/openAccessoai:repositori.upf.edu:10230/253592026-06-12T07:21:37Z
dc.title.none.fl_str_mv Response to hyperosmotic stress
title Response to hyperosmotic stress
spellingShingle Response to hyperosmotic stress
Saito, Haruo
Saccharomyces cerevisiae -- Fisiologia
Proteïnes quinases
title_short Response to hyperosmotic stress
title_full Response to hyperosmotic stress
title_fullStr Response to hyperosmotic stress
title_full_unstemmed Response to hyperosmotic stress
title_sort Response to hyperosmotic stress
dc.creator.none.fl_str_mv Saito, Haruo
Posas Garriga, Francesc
author Saito, Haruo
author_facet Saito, Haruo
Posas Garriga, Francesc
author_role author
author2 Posas Garriga, Francesc
author2_role author
dc.subject.none.fl_str_mv Saccharomyces cerevisiae -- Fisiologia
Proteïnes quinases
topic Saccharomyces cerevisiae -- Fisiologia
Proteïnes quinases
description An appropriate response and adaptation to hyperosmolarity, i.e., an external osmolarity that is higher than the physiological range, can be a matter of life or death for all cells. It is especially important for free-living organisms such as the yeast Saccharomyces cerevisiae. When exposed to hyperosmotic stress, the yeast initiates a complex adaptive program that includes temporary arrest of cell-cycle progression, adjustment of transcription and translation patterns, and the synthesis and retention of the compatible osmolyte glycerol. These adaptive responses are mostly governed by the high osmolarity glycerol (HOG) pathway, which is composed of membrane-associated osmosensors, an intracellular signaling pathway whose core is the Hog1 MAP kinase (MAPK) cascade, and cytoplasmic and nuclear effector functions. The entire pathway is conserved in diverse fungal species, while the Hog1 MAPK cascade is conserved even in higher eukaryotes including humans. This conservation is illustrated by the fact that the mammalian stress-responsive p38 MAPK can rescue the osmosensitivity of hog1Δ mutations in response to hyperosmotic challenge. As the HOG pathway is one of the best-understood eukaryotic signal transduction pathways, it is useful not only as a model for analysis of osmostress responses, but also as a model for mathematical analysis of signal transduction pathways. In this review, we have summarized the current understanding of both the upstream signaling mechanism and the downstream adaptive responses to hyperosmotic stress in yeast.
publishDate 2012
dc.date.none.fl_str_mv 2012
2015
2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10230/25359
http://dx.doi.org/10.1534/genetics.112.140863
url http://hdl.handle.net/10230/25359
http://dx.doi.org/10.1534/genetics.112.140863
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Genetics. 2012;192(2):289-318
info:eu-repo/grantAgreement/EC/FP7/201142
dc.rights.none.fl_str_mv © 2012 Saito et al. This is an open-access article.
info:eu-repo/semantics/openAccess
rights_invalid_str_mv © 2012 Saito et al. This is an open-access article.
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Genetics Society of America
publisher.none.fl_str_mv Genetics Society of America
dc.source.none.fl_str_mv reponame:Repositorio Digital de la UPF
instname:Universitat Pompeu Fabra
instname_str Universitat Pompeu Fabra
reponame_str Repositorio Digital de la UPF
collection Repositorio Digital de la UPF
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repository.mail.fl_str_mv
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