Molecular dissection of radixin: distinct and interdependent functions of the amino- and carboxy-terminal domains - PubMed (original) (raw)
Molecular dissection of radixin: distinct and interdependent functions of the amino- and carboxy-terminal domains
M D Henry et al. J Cell Biol. 1995 May.
Abstract
The ERM proteins--ezrin, radixin, and moesin--occur in particular cortical cytoskeletal structures. Several lines of evidence suggest that they interact with both cytoskeletal elements and plasma membrane components. Here we described the properties of full-length and truncated radixin polypeptides expressed in transfected cells. In stable transfectants, exogenous full-length radixin behaves much like endogenous ERM proteins, localizing to the same cortical structures. However, the presence of full-length radixin or its carboxy-terminal domain in cortical structures correlates with greatly diminished staining of endogenous moesin in those structures, suggesting that radixin and moesin compete for a limiting factor required for normal associations in the cell. The results also reveal distinct roles for the amino- and carboxy-terminal domains. At low levels relative to endogenous radixin, the carboxy-terminal polypeptide is associated with most of the correct cortical targets except cleavage furrows. In contrast, the amino-terminal polypeptide is diffusely localized throughout the cell. Low level expression of full-length radixin or either of the truncated polypeptides has no detectable effect on cell physiology. However, high level expression of the carboxy-terminal domain dramatically disrupts normal cytoskeletal structures and functions. At these high levels, the amino-terminal polypeptide does localize to cortical structures, but does not affect the cells. We conclude that the behavior of radixin in cells depends upon activities contributed by separate domains of the protein, but also requires modulating interactions between those domains.
Similar articles
- Disruption of dynamic cell surface architecture of NIH3T3 fibroblasts by the N-terminal domains of moesin and ezrin: in vivo imaging with GFP fusion proteins.
Amieva MR, Litman P, Huang L, Ichimaru E, Furthmayr H. Amieva MR, et al. J Cell Sci. 1999 Jan;112 ( Pt 1):111-25. doi: 10.1242/jcs.112.1.111. J Cell Sci. 1999. PMID: 9841908 - Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family.
Reczek D, Berryman M, Bretscher A. Reczek D, et al. J Cell Biol. 1997 Oct 6;139(1):169-79. doi: 10.1083/jcb.139.1.169. J Cell Biol. 1997. PMID: 9314537 Free PMC article. - Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association.
Matsui T, Maeda M, Doi Y, Yonemura S, Amano M, Kaibuchi K, Tsukita S, Tsukita S. Matsui T, et al. J Cell Biol. 1998 Feb 9;140(3):647-57. doi: 10.1083/jcb.140.3.647. J Cell Biol. 1998. PMID: 9456324 Free PMC article. - Radixin: cytoskeletal adopter and signaling protein.
Hoeflich KP, Ikura M. Hoeflich KP, et al. Int J Biochem Cell Biol. 2004 Nov;36(11):2131-6. doi: 10.1016/j.biocel.2003.11.018. Int J Biochem Cell Biol. 2004. PMID: 15313460 Review. - [ERM (ezrin/radixin/moesin) as crosslinkers between actin filaments and plasma membranes].
Tsukita S. Tsukita S. Tanpakushitsu Kakusan Koso. 1996 Sep;41(12 Suppl):1899-905. Tanpakushitsu Kakusan Koso. 1996. PMID: 8890653 Review. Japanese. No abstract available.
Cited by
- RhoA-dependent phosphorylation and relocalization of ERM proteins into apical membrane/actin protrusions in fibroblasts.
Shaw RJ, Henry M, Solomon F, Jacks T. Shaw RJ, et al. Mol Biol Cell. 1998 Feb;9(2):403-19. doi: 10.1091/mbc.9.2.403. Mol Biol Cell. 1998. PMID: 9450964 Free PMC article. - ERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis.
Kondo T, Takeuchi K, Doi Y, Yonemura S, Nagata S, Tsukita S. Kondo T, et al. J Cell Biol. 1997 Nov 3;139(3):749-58. doi: 10.1083/jcb.139.3.749. J Cell Biol. 1997. PMID: 9348291 Free PMC article. - The regulation of actin dynamics during cell division and malignancy.
Gibieža P, Petrikaitė V. Gibieža P, et al. Am J Cancer Res. 2021 Sep 15;11(9):4050-4069. eCollection 2021. Am J Cancer Res. 2021. PMID: 34659876 Free PMC article. Review. - Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane ruffles.
Borowsky ML, Hynes RO. Borowsky ML, et al. J Cell Biol. 1998 Oct 19;143(2):429-42. doi: 10.1083/jcb.143.2.429. J Cell Biol. 1998. PMID: 9786953 Free PMC article. - Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2.
Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S, Tsukita S. Yonemura S, et al. J Cell Biol. 1998 Feb 23;140(4):885-95. doi: 10.1083/jcb.140.4.885. J Cell Biol. 1998. PMID: 9472040 Free PMC article.
References
- Mol Cell Biol. 1988 May;8(5):2159-65 - PubMed
- Proc Natl Acad Sci U S A. 1986 Dec;83(24):9512-6 - PubMed
- J Cell Biol. 1989 Mar;108(3):921-30 - PubMed
- J Cell Biol. 1989 Jun;108(6):2369-82 - PubMed
- J Cell Biol. 1989 Oct;109(4 Pt 1):1609-20 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials