生物
警卫室
拟南芥
内质网
基因亚型
细胞生物学
细胞内
互动者
ATP酶
质子泵
拟南芥
分子生物学
生物化学
突变体
基因
酶
作者
Maria Cristina Bonza,Tiziana Fusca,Ulrike Homann,Gerhard Thiel,Maria Ida De Michelis
出处
期刊:Plant Biology
[Wiley]
日期:2009-01-28
卷期号:11 (6): 869-877
被引量:8
标识
DOI:10.1111/j.1438-8677.2008.00181.x
摘要
Abstract PPI1 (proton pump interactor isoform 1) is a novel protein able to interact with the C‐terminal autoinhibitory domain of the Arabidopsis thaliana plasma membrane (PM) H + ‐ATPase. In vitro, PPI1 binds the PM H + ‐ATPase in a site different from the known 14‐3‐3 binding site and stimulates its activity. In this study, we analysed the intracellular localisation of PPI1. The intracellular distribution was monitored in A. thaliana cultured cells by immunolocalisation using an antiserum against the PPI1 N‐terminus and in Vicia faba guard cells and epidermal cells by transient expression of a GFP::PPI1 fusion. The results indicate that the bulk of PPI1 is localised at the endoplasmic reticulum, from which it might be recruited to the PM for interaction with the H + ‐ATPase in response to as yet unidentified signals.
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