Ezrin has properties to self-associate at the plasma membrane
| Autor: | C. Andreoli, Paul Mangeat, Hubert Reggio, R. Le Borgne, Marianne Martin |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Microinjections
Immunoprecipitation Recombinant Fusion Proteins Moesin macromolecular substances Moths Biology Microfilament environment and public health Cell Line Ezrin Radixin Escherichia coli Animals Humans Cytoskeleton Binding protein Cell Membrane Microfilament Proteins Stomach Peripheral membrane protein Membrane Proteins Proteins Biological Transport Blood Proteins Cell Biology Phosphoproteins Nucleopolyhedroviruses Cell biology Cytoskeletal Proteins Biochemistry Protein Processing Post-Translational Protein Binding |
| Zdroj: | Europe PubMed Central |
| ISSN: | 1477-9137 0021-9533 |
| Popis: | Ezrin, a member of a family of proteins involved in the interaction of the microfilament cytoskeleton with the plasma membrane, plays a role in membrane translocation in gastric parietal cells (Hanzel, D., Reggio, H., Bretscher, A., Forte, J. G. and Mangeat, P. (1991). EMBO J. 10, 2363–2373). Human ezrin was expressed in and purified from Escherichia coli. It possesses all the major biophysical, immunological and physiological properties of natural ezrin. Upon microinjection in live gastric HGT-1 cells, ezrin was incorporated into the dorsal microvilli, a site where the endogeneous protein is localized. By coimmunoprecipitation and ezrin-affinity assays, two HGT-1 cell proteins of 77 and 72 kDa behaved as ezrin-binding proteins. In enriched gastric apical membranes, 125I-ezrin labelled proteins of 80, 77 and 72 kDa by overlay assay. The 80 kDa protein was identified as ezrin and the 77 and 72 kDa proteins as gastric forms of proteins structurally related to ezrin, such as radixin and moesin. In insect cells infected with a recombinant baculovirus, one-third of over-expressed ezrin accumulated at the plasma membrane. Ezrin bound a 77 kDa endogenous peripheral membrane protein, behaving as an insect counterpart of the mammalian ezrin family. In addition to the respective role of the amino- and carboxyl-terminal domains of ezrin in linking the membrane and the cytoskeleton (Algrain, M., Turunen, O., Vaheri, A., Louvard, D. and Arpin, M. (1993). J. Cell Biol. 120, 129–139), both domains interacted synergistically in a salt-dependent manner to trigger self-association of ezrin. Ezrin's self-association properties could represent another way of regulating the number of ezrin molecules bound at specific membrane sites. |
| Databáze: | OpenAIRE |
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