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- W640762671 abstract "The membrane cytoskeletal linker ezrin, a member of the Ezrin/Radixin/Moesin (ERM) family, has been hypothesized to have an inhibitory interaction between its N-terminal FERM domain and C-terminal ERM association domain (C-ERMAD). The inactive state of ezrin has always been considered to have this head-to-tail association. Activation by phosphorylation was considered to relieve this intra- or intermolecular interaction. Ezrin is also required in gastric parietal cells to both stimulate acid secretion and form extend apical microvilli. In this study, fluorescence resonance energy transfer (FRET) compatible YFP-Ezrin-CFP (Y-Ez-C) was used to probe for the FERM to C-ERMAD interaction. Parietal cells were infected with adenovirus containing this Y-Ez-C construct and then either held in a resting state with cimetidine or stimulated by adding histamine and IBMX. A weak FRET signal at 527 nm (425 nm ex.) was observed and identical for both resting and stimulated states. Unlike endogenous ezrin and cells expressing Ezrin-CFP, which were primarily localized to the apical plasma membrane with some basolateral expression, Y-Ez-C was expressed throughout the cytoplasm. Aminopyrine assays revealed that Y-Ez-C infected cells stimulated acid secretion normally (97.8±9.2% of uninfected control), and confocal microscopy showed these cells to have normal time dependent apical vacuole swelling. These data indicate that the opening of the Y-Ez-C construct does not occur in vivo, whether or not secretion has been turned on, nor does it participate in the functions of endogenous ezrin to support parietal cell secretion." @default.
- W640762671 created "2016-06-24" @default.
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- W640762671 date "2006-03-01" @default.
- W640762671 modified "2023-09-27" @default.
- W640762671 title "Cytosolic localization of YFP‐Ezrin‐CFP prevents participation in the acid secretory pathway" @default.
- W640762671 doi "https://doi.org/10.1096/fasebj.20.5.lb21-b" @default.
- W640762671 hasPublicationYear "2006" @default.
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