Pollen aquaporins: The solute factor

In the recent years, the biophysical properties and presumed physiological role of aquaporins (AQPs) have been expanded to specialized cells where water and solute exchange are crucial traits. Complex but unique processes such as stomatal movement or pollen hydration and germination have been addres...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Soto, Gabriela Cynthia, Muschietti, Jorge P.
Publicado:	2016
Materias:	Aquaporin Fertilization Membrane intrinsic protein Plant fitness Pollen germination Solute permeability Water and solute transport Water channel
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1664462X_v7_nNovember2016_p_PerezDiGiorgio http://hdl.handle.net/20.500.12110/paper_1664462X_v7_nNovember2016_p_PerezDiGiorgio
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_1664462X_v7_nNovember2016_p_PerezDiGiorgio
record_format	dspace
spelling	paper:paper_1664462X_v7_nNovember2016_p_PerezDiGiorgio2023-06-08T16:26:08Z Pollen aquaporins: The solute factor Soto, Gabriela Cynthia Muschietti, Jorge P. Aquaporin Fertilization Membrane intrinsic protein Plant fitness Pollen germination Solute permeability Water and solute transport Water channel In the recent years, the biophysical properties and presumed physiological role of aquaporins (AQPs) have been expanded to specialized cells where water and solute exchange are crucial traits. Complex but unique processes such as stomatal movement or pollen hydration and germination have been addressed not only by identifying the specific AQP involved but also by studying how these proteins integrate and coordinate cellular activities and functions. In this review, we referred specifically to pollen-specific AQPs and analyzed what has been assumed in terms of transport properties and what has been found in terms of their physiological role. Unlike that in many other cells, the AQP machinery in mature pollen lacks plasma membrane intrinsic proteins, which are extensively studied for their high water capacity exchange. Instead, a variety of TIPs and NIPs are expressed in pollen. These findings have altered the initial understanding of AQPs and water exchange to consider specific and diverse solutes that might be critical to sustaining pollen’s success. The spatial and temporal distribution of the pollen AQPs also reflects a regulatory mechanism that allowing a properly adjusting water and solute exchange. © 2016 Pérez Di Giorgio, Soto, Muschietti and Amodeo. Fil:Soto, G.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Muschietti, J.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2016 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1664462X_v7_nNovember2016_p_PerezDiGiorgio http://hdl.handle.net/20.500.12110/paper_1664462X_v7_nNovember2016_p_PerezDiGiorgio
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Aquaporin Fertilization Membrane intrinsic protein Plant fitness Pollen germination Solute permeability Water and solute transport Water channel
spellingShingle	Aquaporin Fertilization Membrane intrinsic protein Plant fitness Pollen germination Solute permeability Water and solute transport Water channel Soto, Gabriela Cynthia Muschietti, Jorge P. Pollen aquaporins: The solute factor
topic_facet	Aquaporin Fertilization Membrane intrinsic protein Plant fitness Pollen germination Solute permeability Water and solute transport Water channel
description	In the recent years, the biophysical properties and presumed physiological role of aquaporins (AQPs) have been expanded to specialized cells where water and solute exchange are crucial traits. Complex but unique processes such as stomatal movement or pollen hydration and germination have been addressed not only by identifying the specific AQP involved but also by studying how these proteins integrate and coordinate cellular activities and functions. In this review, we referred specifically to pollen-specific AQPs and analyzed what has been assumed in terms of transport properties and what has been found in terms of their physiological role. Unlike that in many other cells, the AQP machinery in mature pollen lacks plasma membrane intrinsic proteins, which are extensively studied for their high water capacity exchange. Instead, a variety of TIPs and NIPs are expressed in pollen. These findings have altered the initial understanding of AQPs and water exchange to consider specific and diverse solutes that might be critical to sustaining pollen’s success. The spatial and temporal distribution of the pollen AQPs also reflects a regulatory mechanism that allowing a properly adjusting water and solute exchange. © 2016 Pérez Di Giorgio, Soto, Muschietti and Amodeo.
author	Soto, Gabriela Cynthia Muschietti, Jorge P.
author_facet	Soto, Gabriela Cynthia Muschietti, Jorge P.
author_sort	Soto, Gabriela Cynthia
title	Pollen aquaporins: The solute factor
title_short	Pollen aquaporins: The solute factor
title_full	Pollen aquaporins: The solute factor
title_fullStr	Pollen aquaporins: The solute factor
title_full_unstemmed	Pollen aquaporins: The solute factor
title_sort	pollen aquaporins: the solute factor
publishDate	2016
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1664462X_v7_nNovember2016_p_PerezDiGiorgio http://hdl.handle.net/20.500.12110/paper_1664462X_v7_nNovember2016_p_PerezDiGiorgio
work_keys_str_mv	AT sotogabrielacynthia pollenaquaporinsthesolutefactor AT muschiettijorgep pollenaquaporinsthesolutefactor
_version_	1768544057799213056

Pollen aquaporins: The solute factor

Ejemplares similares