Abstract
Ezrin, an 80 kDa protein originally found in chicken intestinal microvilli, is localized to microvilli and other plasma membrane structures in a variety of cell types (Bretscher 1991). In A431 cells, ezrin is constitutively phosphorylated on serine and threonine, and EGF treatment leads to an increase in tyrosine and threonine phosphorylation along with EGF-induced membrane ruffling (Gould et al. 1986; Bretscher 1989). Ezrin is also a prominent cytoskeletal protein in gastric parietal cells, where it has been associated with remodeling of apical cell membrane that occurs with cAMP-dependent protein kinase stimulation (Hanzel et al. 1991).
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© 1994 Springer-Verlag Berlin Heidelberg
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Yao, X., Forte, J.G. (1994). Activation of calpain in gastric parietal cells. In: Hirst, B.H. (eds) Molecular and Cellular Mechanisms of H+ Transport. NATO ASI Series, vol 89. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79301-1_39
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DOI: https://doi.org/10.1007/978-3-642-79301-1_39
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