English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/108923
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Citado 4 veces en Web of Knowledge®  |  Pub MebCentral Ver citas en PubMed Central  |  Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar otros formatos: Exportar EndNote (RIS)Exportar EndNote (RIS)Exportar EndNote (RIS)
Título

A dominant-negative form of Arabidopsis AP-3 β-adaptin demonstrates a connection between pH homeostasis and ABA sensitivity

Autor Niñoles, Regina; Rubio, Lourdes; García-Sánchez, María J.; Fernández, José A.; Alejandro, Santiago
Palabras clave Arabidopsis thaliana
H+-ATPase
membrane potential
ion channels
acetic acid
Fecha de publicación 21-mar-2013
EditorJohn Wiley & Sons
Citación The Plant Journal 74 (4): 557-568 (2013)
ResumenIntracellular pH (pHi) is a crucial parameter in cellular physiology but its mechanisms of homeostasis are only partially understood. To uncover novel roles and participants of the pHi regulatory system, we have screened an Arabidopsis mutant collection for resistance of seed germination to intracellular acidification induced by weak organic acids (acetic, propionic, sorbic). The phenotypes of one identified mutant, weak acid-tolerant 1-1D (wat1-1D) are due to the expression of a truncated form of AP-3 β-adaptin (encoded by the PAT2 gene) that behaves as a as dominant-negative. During acetic acid treatment the root epidermal cells of the mutant maintain a higher pHi and a more depolarized plasma membrane electrical potential than wild-type cells. Additional phenotypes of wat1-1D roots include increased rates of acetate efflux, K+ uptake and H+ efflux, the latter reflecting the in vivo activity of the plasma membrane H+-ATPase. The in vitro activity of the enzyme was not increased but, as the H+-ATPase is electrogenic, the increased ion permeability would allow a higher rate of H+ efflux. The AP-3 adaptor complex is involved in traffic from Golgi to vacuoles but its function in plants is not much known. The phenotypes of the wat1-1D mutant can be explained if loss of function of the AP-3 β-adaptin causes activation of channels or transporters for organic anions (acetate) and for K+ at the plasma membrane, perhaps through miss-localization of tonoplast proteins. This suggests a role of this adaptin in trafficking of ion channels or transporters to the tonoplast.
Versión del editorhttp://dx.doi.org/10.1111/tpj.12138
URI http://hdl.handle.net/10261/108923
DOI10.1111/tpj.12138
Aparece en las colecciones: (IBMCP) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
Postprint_Serrano_dominant_negative_Arabidopsis_2013.doc6,51 MBMicrosoft WordVisualizar/Abrir
Mostrar el registro completo
 



NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.