Radixin is a novel member of the band 4.1 family

doi:10.1083/jcb.115.4.1039

This Article

Full Text (PDF, 1360K)

Alert me when this article is cited

Citation Map

Services

Email this article

Similar articles in this journal

Similar articles in PubMed

Alert me to new content in the JCB

Download to citation manager

Citing Articles

Citing Articles via HighWire

Citing Articles via CrossRef

Citing Articles via Google Scholar

Google Scholar

Articles by Funayama, N.

Articles by Tsukita, S.

Search for Related Content

PubMed

PubMed Citation

Articles by Funayama, N.

Articles by Tsukita, S.

Pubmed/NCBI databases

Gene	GEO Profiles
HomoloGene	Protein
UniGene
Compound via MeSH
Substance via MeSH

Social Bookmarking

What's this?

ARTICLES

Radixin is a novel member of the band 4.1 family

N Funayama, A Nagafuchi, N Sato, S Tsukita and S Tsukita
Department of Information Physiology, National Institute for Physiological Sciences, Okazaki, Aichi, Japan.

Radixin is an actin barbed-end capping protein which is highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively (Tsukita, Sa., Y. Hieda, and Sh. Tsukita. 1989 a.J. Cell Biol. 108:2369- 2382; Sato, N., S. Yonemura, T. Obinata, Sa. Tsukita, and Sh. Tsukita. 1991. J. Cell Biol. 113:321-330). To further understand the structure and functions of the radixin molecule, we isolated and sequenced the cDNA clones encoding mouse radixin. Direct peptide sequencing of radixin and immunological analysis with antiserum to a fusion protein were performed to confirm that the protein encoded by these clones is identical to radixin. The composite cDNA is 4,241 nucleotides long and codes for a 583-amino acid polypeptide with a calculated molecular mass of 68.5 kD. Sequence analysis has demonstrated that mouse radixin shares 75.3% identity with human ezrin, which was reported to be a member of the band 4.1 family. We then isolated the cDNA encoding mouse ezrin. Sequence analysis and Northern blot analysis revealed that radixin and ezrin are similar but distinct (74.9% identity), leading us to conclude that radixin is a novel member of the band 4.1 family. In erythrocytes the band 4.1 protein acts as a key protein in the association of short actin filaments with a plasma membrane protein (glycophorin), together with spectrin. Therefore, the sequence similarity between radixin and band 4.1 protein described in this study favors the idea that radixin plays a crucial role in the association of the barbed ends of actin filaments with the plasma membrane in the cell- to-cell adherens junction and the cleavage furrow.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Facebook Add to Reddit Reddit Add to Technorati Technorati Twitter What's this?

This article has been cited by other articles:

Franke, W. W. (2009). Discovering the Molecular Components of Intercellular Junctions--A Historical View. Cold Spring Harb. Perspect. Biol. 1: a003061-a003061 [Abstract] [Full Text]
Zhu, L., Hatakeyama, J., Zhang, B., Makdisi, J., Ender, C., Forte, J. G. (2009). Novel insights of the gastric gland organization revealed by chief cell specific expression of moesin. Am. J. Physiol. Gastrointest. Liver Physiol. 296: G185-G195 [Abstract] [Full Text]
Ilani, T., Khanna, C., Zhou, M., Veenstra, T. D., Bretscher, A. (2007). Immune synapse formation requires ZAP-70 recruitment by ezrin and CD43 removal by moesin. JCB 179: 733-746 [Abstract] [Full Text]
Grimsley, C. M., Lu, M., Haney, L. B., Kinchen, J. M., Ravichandran, K. S. (2006). Characterization of a Novel Interaction between ELMO1 and ERM Proteins. J. Biol. Chem. 281: 5928-5937 [Abstract] [Full Text]
Bechtel, J. T., Winant, R. C., Ganem, D. (2005). Host and Viral Proteins in the Virion of Kaposi's Sarcoma-Associated Herpesvirus. J. Virol. 79: 4952-4964 [Abstract] [Full Text]
Finnerty, C. M., Chambers, D., Ingraffea, J., Faber, H. R., Karplus, P. A., Bretscher, A. (2004). The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain. J. Cell Sci. 117: 1547-1552 [Abstract] [Full Text]
Smith, W. J., Nassar, N., Bretscher, A., Cerione, R. A., Karplus, P. A. (2003). Structure of the Active N-terminal Domain of Ezrin. CONFORMATIONAL AND MOBILITY CHANGES IDENTIFY KEYSTONE INTERACTIONS. J. Biol. Chem. 278: 4949-4956 [Abstract] [Full Text]
GRUNE, T., REINHECKEL, T., NORTH, J. A., LI, R., BESCOS, P. B., SHRINGARPURE, R., DAVIES, K. J. A. (2002). Ezrin turnover and cell shape changes catalyzed by proteasome in oxidatively stressed cells. FASEB J. 16: 1602-1610 [Abstract] [Full Text]
Prekeris, R., Davies, J. M., Scheller, R. H. (2001). Identification of a Novel Rab11/25 Binding Domain Present in Eferin and Rip Proteins. J. Biol. Chem. 276: 38966-38970 [Abstract] [Full Text]
Theoharides, T. C., Wang, L., Pang, X., Letourneau, R., Culm, K. E., Basu, S., Wang, Y., Correia, I. (2000). Cloning and Cellular Localization of the Rat Mast Cell 78-kDa Protein Phosphorylated in Response to the Mast Cell "Stabilizer" Cromolyn. J. Pharmacol. Exp. Ther. 294: 810-821 [Abstract] [Full Text]
Nunomura, W., Takakuwa, Y., Parra, M., Conboy, J. G., Mohandas, N. (2000). Ca2+-dependent and Ca2+-independent Calmodulin Binding Sites in Erythrocyte Protein 4.1. IMPLICATIONS FOR REGULATION OF PROTEIN 4.1 INTERACTIONS WITH TRANSMEMBRANE PROTEINS. J. Biol. Chem. 275: 6360-6367 [Abstract] [Full Text]
Ko, M., Kitchen, J., Wang, X, Threat, T., Wang, X, Hasegawa, A, Sun, T, Grahovac, M., Kargul, G., Lim, M., Cui, Y, Sano, Y, Tanaka, T, Liang, Y, Mason, S, Paonessa, P., Sauls, A., DePalma, G., Sharara, R, Rowe, L., Eppig, J, Morrell, C, Doi, H (2000). Large-scale cDNA analysis reveals phased gene expression patterns during preimplantation mouse development. Development 127: 1737-1749 [Abstract]
Bonilha, V. L., Finnemann, S. C., Rodriguez-Boulan, E. (1999). Ezrin Promotes Morphogenesis of Apical Microvilli and Basal Infoldings in Retinal Pigment Epithelium. JCB 147: 1533-1548 [Abstract] [Full Text]
Nakamura, F., Huang, L., Pestonjamasp, K., Luna, E. J., Furthmayr, H. (1999). Regulation of F-Actin Binding to Platelet Moesin In Vitro by Both Phosphorylation of Threonine 558 and Polyphosphatidylinositides. Mol. Biol. Cell 10: 2669-2685 [Abstract] [Full Text]
Yonemura, S., Tsukita, S., Tsukita, S. (1999). Direct Involvement of Ezrin/Radixin/Moesin (ERM)-binding Membrane Proteins in the Organization of Microvilli in Collaboration with Activated ERM Proteins. JCB 145: 1497-1509 [Abstract] [Full Text]
Castelo, L., Jay, D. G. (1999). Radixin Is Involved in Lamellipodial Stability during Nerve Growth Cone Motility. Mol. Biol. Cell 10: 1511-1520 [Abstract] [Full Text]
Huang, L., Wong, T. Y.�W., Lin, R. C.�C., Furthmayr, H. (1999). Replacement of Threonine 558,�a Critical Site of Phosphorylation of Moesin in Vivo, with Aspartate Activates F-actin Binding of Moesin. REGULATION BY CONFORMATIONAL CHANGE. J. Biol. Chem. 274: 12803-12810 [Abstract] [Full Text]
Doi, Y., Itoh, M., Yonemura, S., Ishihara, S., Takano, H., Noda, T., Tsukita, S., Tsukita, S. (1999). Normal Development of Mice and Unimpaired Cell Adhesion/Cell Motility/Actin-based Cytoskeleton without Compensatory Up-regulation of Ezrin or Radixin in Moesin Gene Knockout. J. Biol. Chem. 274: 2315-2321 [Abstract] [Full Text]
Gronholm, M, Sainio, M, Zhao, F, Heiska, L, Vaheri, A, Carpen, O (1999). Homotypic and heterotypic interaction of the neurofibromatosis 2 tumor suppressor protein merlin and the ERM protein ezrin. J. Cell Sci. 112: 895-904 [Abstract]
Reczek, D., Bretscher, A. (1998). The Carboxyl-terminal Region of EBP50 Binds to a Site in the Amino-terminal Domain of Ezrin That Is Masked in the Dormant Molecule. J. Biol. Chem. 273: 18452-18458 [Abstract] [Full Text]
Yonemura, S., Hirao, M., Doi, Y., Takahashi, N., Kondo, T., Tsukita, S., Tsukita, S. (1998). 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. JCB 140: 885-895 [Abstract] [Full Text]
Matsui, T., Maeda, M., Doi, Y., Yonemura, S., Amano, M., Kaibuchi, K., Tsukita, S., Tsukita, S. (1998). Rho-Kinase Phosphorylates COOH-terminal Threonines of Ezrin/Radixin/Moesin (ERM) Proteins and Regulates Their Head-to-Tail Association. JCB 140: 647-657 [Abstract] [Full Text]
Nunomura, W., Takakuwa, Y., Tokimitsu, R., Krauss, S. W., Kawashima, M., Mohandas, N. (1997). Regulation of CD44-Protein 4.1�Interaction by Ca2+ and Calmodulin. IMPLICATIONS FOR MODULATION OF CD44-ANKYRIN INTERACTION. J. Biol. Chem. 272: 30322-30328 [Abstract] [Full Text]
Kondo, T., Takeuchi, K., Doi, Y., Yonemura, S., Nagata, S., Tsukita, S., Tsukita, S. (1997). ERM (Ezrin/Radixin/Moesin)-based Molecular Mechanism of Microvillar Breakdown at an Early Stage of Apoptosis. JCB 139: 749-758 [Abstract] [Full Text]
Nakamura, H., Ozawa, H. (1997). Immunolocalization of CD44 and the Ezrin-Radixin-Moesin (ERM) Family in the Stratum Intermedium and Papillary Layer of the Mouse Enamel Organ. J. Histochem. Cytochem. 45: 1481-1492 [Abstract] [Full Text]
Reczek, D., Berryman, M., Bretscher, A. (1997). Identification of EBP50: A PDZ-containing Phosphoprotein that Associates with Members of the Ezrin-Radixin-Moesin Family. JCB 139: 169-179 [Abstract] [Full Text]
Roy, C., Martin, M., Mangeat, P. (1997). A Dual Involvement of the Amino-terminal Domain of Ezrin in F- and G-actin Binding. J. Biol. Chem. 272: 20088-20095 [Abstract] [Full Text]
Yanagisawa, J., Takahashi, M., Kanki, H., Yano-Yanagisawa, H., Tazunoki, T., Sawa, E., Nishitoba, T., Kamishohara, M., Kobayashi, E., Kataoka, S., Sato, T. (1997). The Molecular Interaction of Fas and FAP-1. A TRIPEPTIDE BLOCKER OF HUMAN Fas INTERACTION WITH FAP-1 PROMOTES Fas-INDUCED APOPTOSIS. J. Biol. Chem. 272: 8539-8545 [Abstract] [Full Text]
Bretscher, A, Reczek, D, Berryman, M (1997). Ezrin: a protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures. J. Cell Sci. 110: 3011-3018 [Abstract]
Sainio, M, Zhao, F, Heiska, L, Turunen, O, den Bakker, M, Zwarthoff, E, Lutchman, M, Rouleau, G., Jaaskelainen, J, Vaheri, A, Carpen, O (1997). Neurofibromatosis 2 tumor suppressor protein colocalizes with ezrin and CD44 and associates with actin-containing cytoskeleton. J. Cell Sci. 110: 2249-2260 [Abstract]
Yao, X., Cheng, L., Forte, J. G. (1996). Biochemical Characterization of Ezrin-Actin Interaction. J. Biol. Chem. 271: 7224-7229 [Abstract] [Full Text]
Takeuchi, K., Kawashima, A., Nagafuchi, A., Tsukita, S. (1994). Structural diversity of band 4.1 superfamily members. J. Cell Sci. 107: 1921-1928 [Abstract]
Andreoli, C, Martin, M, Le Borgne, R, Reggio, H, Mangeat, P (1994). Ezrin has properties to self-associate at the plasma membrane. J. Cell Sci. 107: 2509-2521 [Abstract]
Winckler, B, Gonzalez Agosti, C, Magendantz, M, Solomon, F (1994). Analysis of a cortical cytoskeletal structure: a role for ezrin-radixin-moesin (ERM proteins) in the marginal band of chicken erythrocytes. J. Cell Sci. 107: 2523-2534 [Abstract]
Berryman, M, Franck, Z, Bretscher, A (1993). Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells. J. Cell Sci. 105: 1025-1043 [Abstract]
Franck, Z, Gary, R, Bretscher, A (1993). Moesin, like ezrin, colocalizes with actin in the cortical cytoskeleton in cultured cells, but its expression is more variable. J. Cell Sci. 105: 219-231 [Abstract]
Nunomura, W., Takakuwa, Y., Parra, M., Conboy, J., Mohandas, N. (2000). Regulation of Protein 4.1R, p55, and Glycophorin C Ternary Complex in Human Erythrocyte Membrane. J. Biol. Chem. 275: 24540-24546 [Abstract] [Full Text]