Aquaporins in the plant kingdom: the regulatory mechanisms revisited

Autores
Alleva, Karina; Amodeo, Gabriela
Año de publicación
2006
Idioma
inglés
Tipo de recurso
reseña artículo
Estado
versión publicada
Descripción
More than 30 years ago, biophysicist and animal physiologists supported the hypothesis of the existence of pores facilitating water transport through membranes since certain animal structures were unusually permeable to water. Although plant physiologists also discussed the existence of water channels since the early 1960s, the survey remained marginal in the field (reviewed by Chrispeels and Maurel 1994). It was in 1992 that the hypothetical proteinaceous water channel was identified (named CHIP28, now AQP1) by Preston et. al. This discovery opened the molecular detection of homologous proteins in all kingdoms. The term “aquaporins” (AQPs) was suggested later, when other two proteins belonging to the MIP26 family (WCH-CD -from mammalian collecting ductand g-TIP -from tonoplast of Arabidopsis thaliana-) were also characterized as water channels (Agre et al., 1993). The first cloned and functionally expressed aquaporin from plants was therefore g-TIP (now TIP1;1) (Maurel et al., 1993). Since this event, plant aquaporins captured significant attention. This article intends to explore the regulatory mechanisms in plant aquaporins and to contrast them with those achievements made on their animal homologues. The aim is to merge the contributions made by both fields of research.
Sociedad Argentina de Fisiología
Materia
Ciencias Médicas
Fisiología
Aquaporins
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/146974

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network_name_str SEDICI (UNLP)
spelling Aquaporins in the plant kingdom: the regulatory mechanisms revisitedAlleva, KarinaAmodeo, GabrielaCiencias MédicasFisiologíaAquaporinsMore than 30 years ago, biophysicist and animal physiologists supported the hypothesis of the existence of pores facilitating water transport through membranes since certain animal structures were unusually permeable to water. Although plant physiologists also discussed the existence of water channels since the early 1960s, the survey remained marginal in the field (reviewed by Chrispeels and Maurel 1994). It was in 1992 that the hypothetical proteinaceous water channel was identified (named CHIP28, now AQP1) by Preston et. al. This discovery opened the molecular detection of homologous proteins in all kingdoms. The term “aquaporins” (AQPs) was suggested later, when other two proteins belonging to the MIP26 family (WCH-CD -from mammalian collecting ductand g-TIP -from tonoplast of Arabidopsis thaliana-) were also characterized as water channels (Agre et al., 1993). The first cloned and functionally expressed aquaporin from plants was therefore g-TIP (now TIP1;1) (Maurel et al., 1993). Since this event, plant aquaporins captured significant attention. This article intends to explore the regulatory mechanisms in plant aquaporins and to contrast them with those achievements made on their animal homologues. The aim is to merge the contributions made by both fields of research.Sociedad Argentina de Fisiología2006-02info:eu-repo/semantics/reviewinfo:eu-repo/semantics/publishedVersionRevisionhttp://purl.org/coar/resource_type/c_dcae04bcinfo:ar-repo/semantics/resenaArticuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/146974enginfo:eu-repo/semantics/altIdentifier/url/https://pmr.safisiol.org.ar/wp-content/uploads/2022/09/vol1_n7_february.pdfinfo:eu-repo/semantics/altIdentifier/issn/1669-5410info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:37:32Zoai:sedici.unlp.edu.ar:10915/146974Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:37:32.634SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Aquaporins in the plant kingdom: the regulatory mechanisms revisited
title Aquaporins in the plant kingdom: the regulatory mechanisms revisited
spellingShingle Aquaporins in the plant kingdom: the regulatory mechanisms revisited
Alleva, Karina
Ciencias Médicas
Fisiología
Aquaporins
title_short Aquaporins in the plant kingdom: the regulatory mechanisms revisited
title_full Aquaporins in the plant kingdom: the regulatory mechanisms revisited
title_fullStr Aquaporins in the plant kingdom: the regulatory mechanisms revisited
title_full_unstemmed Aquaporins in the plant kingdom: the regulatory mechanisms revisited
title_sort Aquaporins in the plant kingdom: the regulatory mechanisms revisited
dc.creator.none.fl_str_mv Alleva, Karina
Amodeo, Gabriela
author Alleva, Karina
author_facet Alleva, Karina
Amodeo, Gabriela
author_role author
author2 Amodeo, Gabriela
author2_role author
dc.subject.none.fl_str_mv Ciencias Médicas
Fisiología
Aquaporins
topic Ciencias Médicas
Fisiología
Aquaporins
dc.description.none.fl_txt_mv More than 30 years ago, biophysicist and animal physiologists supported the hypothesis of the existence of pores facilitating water transport through membranes since certain animal structures were unusually permeable to water. Although plant physiologists also discussed the existence of water channels since the early 1960s, the survey remained marginal in the field (reviewed by Chrispeels and Maurel 1994). It was in 1992 that the hypothetical proteinaceous water channel was identified (named CHIP28, now AQP1) by Preston et. al. This discovery opened the molecular detection of homologous proteins in all kingdoms. The term “aquaporins” (AQPs) was suggested later, when other two proteins belonging to the MIP26 family (WCH-CD -from mammalian collecting ductand g-TIP -from tonoplast of Arabidopsis thaliana-) were also characterized as water channels (Agre et al., 1993). The first cloned and functionally expressed aquaporin from plants was therefore g-TIP (now TIP1;1) (Maurel et al., 1993). Since this event, plant aquaporins captured significant attention. This article intends to explore the regulatory mechanisms in plant aquaporins and to contrast them with those achievements made on their animal homologues. The aim is to merge the contributions made by both fields of research.
Sociedad Argentina de Fisiología
description More than 30 years ago, biophysicist and animal physiologists supported the hypothesis of the existence of pores facilitating water transport through membranes since certain animal structures were unusually permeable to water. Although plant physiologists also discussed the existence of water channels since the early 1960s, the survey remained marginal in the field (reviewed by Chrispeels and Maurel 1994). It was in 1992 that the hypothetical proteinaceous water channel was identified (named CHIP28, now AQP1) by Preston et. al. This discovery opened the molecular detection of homologous proteins in all kingdoms. The term “aquaporins” (AQPs) was suggested later, when other two proteins belonging to the MIP26 family (WCH-CD -from mammalian collecting ductand g-TIP -from tonoplast of Arabidopsis thaliana-) were also characterized as water channels (Agre et al., 1993). The first cloned and functionally expressed aquaporin from plants was therefore g-TIP (now TIP1;1) (Maurel et al., 1993). Since this event, plant aquaporins captured significant attention. This article intends to explore the regulatory mechanisms in plant aquaporins and to contrast them with those achievements made on their animal homologues. The aim is to merge the contributions made by both fields of research.
publishDate 2006
dc.date.none.fl_str_mv 2006-02
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