The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family.
Open accessAbstract
Ezrin, previously also known as cytovillin, p81, and 80K, is a cytoplasmic protein enriched in microvilli and other cell surface structures. Ezrin is postulated to have a membrane-cytoskeleton linker role. Recent findings have also revealed that the NH2-terminal domain of ezrin is associated with the plasma membrane and the COOH-terminal domain with the cytoskeleton (Algrain, M., O. Turunen, A. Vaheri, D. Louvard, and M. Arpin. 1993. J. Cell Biol. 120: 129-139). Using bacterially expressed fragments of ezrin we now demonstrate that ezrin has an actin-binding capability. We used glutathione-S-transferase fusion proteins of truncated ezrin in affinity chromatography to bind actin from the cell extract or purified rabbit muscle actin. We detected a binding site for filamentous actin that was localized to the COOH-terminal 34 amino acids of ezrin. No binding of monomeric actin was detected in the assay. The region corresponding to the COOH-terminal actin-binding site in ezrin is highly conserved in moesin, actin-capping protein radixin and EM10 protein of E. multilocularis, but not in merlin/schwannomin. Consequently, this site is a potential actin-binding site also in the other members of the protein family. Furthermore, the actin-binding site in ezrin shows sequence homology to the actin-binding site in the COOH terminus of the beta subunit of the actin-capping protein CapZ and one of the potential actin-binding sites in myosin heavy chain. The actin-binding capability of ezrin supports its proposed role as a membrane-cytoskeleton linker.
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Cites
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Cytoskeleton—Plasma Membrane Interactions
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Self-citationThe 14-fold periodicity in α-tropomyosin and the interaction with actin
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Cited by
ERM proteins and merlin: integrators at the cell cortex
Bretscher, A., Edwards, K., & Fehon, R. G. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm882 · Cited by 1,306
Organizing the cell cortex: the role of ERM proteins
Fehon, R. G., McClatchey, A. I., & Bretscher, A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2866 · Cited by 1,044
Regulation of the Cytoskeleton and Cell Adhesion by the Rho Family GTPases in Mammalian Cells
Kaibuchi, K., Kuroda, S., & Amano, M. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.459 · Cited by 1,017
Barreiro, O., Yáñez-Mó, M., Serrador, J. M., Montoya, M. C., Vicente-Manzanares, M., Tejedor, R., Furthmayr, H., & Sánchez-Madrid, F. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200112126 · Cited by 594
Hirao, M., Sato, N., Kondo, T., Yonemura, S., Monden, M., Sasaki, T., Takai, Y., Tsukita, S., & Tsukita, S. (1996) · The Journal of cell biology · doi:10.1083/jcb.135.1.37 · Cited by 593
Metadata
- Authors
- Turunen, O., Wahlström, T., & Vaheri, A.
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1994-09-15
- Volume
- 126
- Issue
- 6
- Pages
- 1445-1453
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2117822148
- Cited by
- 401
- References
- 42
- FWCI
- 6.83
- Type
- journal article
- Language
- en
- Open access
- green
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- Turunen, O., Wahlström, T., & Vaheri, A. (1994). Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family. The Journal of cell biology. https://doi.org/10.1083/jcb.126.6.1445
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