Research Topics
Genomes and Genes | S YonemuraSummaryAffiliation: Kyoto University Country: Japan Publications
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Detail Information
Publications
Direct involvement of ezrin/radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteinsS Yonemura
Department of Cell Biology, Faculty of Medicine, Kyoto University, Kyoto 606 8501, Japan
J Cell Biol 145:1497-509. 1999..Furthermore, immunodetection with a phosphorylated ERM-specific antibody and site-directed mutagenesis suggested that ERM proteins phosphorylated at their COOH-terminal threonine residue represent activated ERM proteins...- Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2S Yonemura
Department of Cell Biology, Faculty of Medicine, Kyoto University, Sakyo ku, Kyoto 606 01, Japan
J Cell Biol 140:885-95. 1998..From these findings, we conclude that ERM proteins bind to integral membrane proteins bearing a positively charged amino acid cluster in their juxta-membrane cytoplasmic domain... - Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathwayM Hirao
Department of Cell Biology, Faculty of Medicine, Kyoto University, Japan
J Cell Biol 135:37-51. 1996..These findings indicate that Rho regulates the CD44/ERM complex formation in vivo and that the phosphatidylinositol turnover may be involved in this regulation mechanism... - ERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosisT Kondo
Department of Cell Biology, Faculty of Medicine, Kyoto University, Sakyo ku, Kyoto 606, Japan
J Cell Biol 139:749-58. 1997..The physiological relevance of this ERM protein-based microvillar breakdown in apoptosis will be discussed... - Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail associationT Matsui
Department of Cell Biology, Faculty of Medicine, Kyoto University, Sakyo ku, Kyoto 606, Japan
J Cell Biol 140:647-57. 1998.... 
Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteinsS Tsukita
College of Medical Technology, Kyoto University, Sakyo-ku, Kyoto 606, Japan
J Biol Chem 274:34507-10. 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 knockoutY Doi
Department of Cell Biology, Faculty of Medicine, Kyoto University, Sakyo ku, Kyoto 606, Japan
J Biol Chem 274:2315-21. 1999..These findings favor the notion that ERM proteins are functionally redundant at the cellular as well as the whole body level... - ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transductionS Tsukita
Department of Cell Biology, Faculty of Medicine, Kyoto University, Yoshida Konoe, Sakyo ku, Kyoto 606, Japan
Curr Opin Cell Biol 9:70-5. 1997..Furthermore, identification of the neurofibromatosis type 2 tumour suppressor, which shows striking sequence similarity to ERM proteins, has increased interest in this family... - ERM proteins: head-to-tail regulation of actin-plasma membrane interactionS Tsukita
College of Medical Technology, Kyoto University, Japan
Trends Biochem Sci 22:53-8. 1997..Specific signals activate ERM proteins to bind actin filaments and the plasma membrane; these include phosphoinositides and/or phosphorylation mechanisms, which might be located downstream from the Rho-dependent pathway... - Interspecies diversity of the occludin sequence: cDNA cloning of human, mouse, dog, and rat-kangaroo homologuesY Ando-Akatsuka
Department of Cell Biology, Faculty of Medicine, Kyoto University, Japan
J Cell Biol 133:43-7. 1996..Implications of these data and novel experimental options in cell biological research are discussed... - A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sitesN Sato
Department of Information Physiology, National Institute for Physiological Sciences, Aichi, Japan
J Cell Sci 103:131-43. 1992..We conclude that at least one of the members of the ezrin-radixin-moesin family is concentrated at specific regions where actin filaments are densely associated with plasma membranes... - The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopyM Itoh
Department of Information Physiology, National Institute for Physiological Sciences, Aichi, Japan
J Cell Biol 121:491-502. 1993..Possible functions of the 220-kD protein (ZO-1) are discussed with special reference to the molecular mechanism for adherens and tight junction formation... - Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctionsM Furuse
Department of Information Physiology, National Institute for Physiological Sciences, Okazaki, Aichi, Japan
J Cell Biol 127:1617-26. 1994..The coincidence of the sequence necessary for the ZO-1 association with that for the TJ localization suggests that the association with underlying cytoskeletons through ZO-1 is required for occludin to be localized at TJ... - Kid, a novel kinesin-like DNA binding protein, is localized to chromosomes and the mitotic spindleN Tokai
The Institute of Medical Science, The University of Tokyo, Japan
EMBO J 15:457-67. 1996..Thus, we propose that Kid might play a role(s) in regulating the chromosomal movement along microtubules during mitosis... - Occludin: a novel integral membrane protein localizing at tight junctionsM Furuse
Department of Information Physiology, National Institute for Physiological Sciences, Aichi, Japan
J Cell Biol 123:1777-88. 1993..These findings revealed that an integral membrane protein localizing at tight junctions is now identified, which we designated as "occludin.".. - Rho-dependent transfer of Citron-kinase to the cleavage furrow of dividing cellsM Eda
Department of Pharmacology, Kyoto University Faculty of Medicine, Sakyo, Kyoto 606-8501, Japan
J Cell Sci 114:3273-84. 2001..Rho is then activated, binds to Citron-K and translocates it to cell cortex, where the complex is then concentrated in the cleavage furrow by the action of actin cytoskeleton beneath the equator of dividing cells...