発表論文｜月田研究室（帝京大学先端総合研究機構）

発表論文

#：corresponding author

～2000
Hamada, K., Matsui, T., Tsukita, S., Tsukita, S., and ^#Hakoshima, T. 2000. Crystallographic characterization of the membrane-binding domain of radixin. Acta Crystallogr D Biol Crystallogr. 56(Pt 7):922-3. https://doi.org/10.1107/s0907444900006363
^#Tsukita, S., and Yonemura, S. 1999. Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins. J Biol Chem. 274(49):34507-10. https://doi.org/10.1074/jbc.274.49.34507
Matsui, T., Yonemura, S., Tsukita, S., and ^#Tsukita, S. 1999. Activation of ERM proteins in vivo by Rho involves phosphatidyl-inositol 4-phosphate 5-kinase and not ROCK kinases. Curr Biol. 9(21):1259-62. https://doi.org/10.1016/s0960-9822(99)80508-9
Maeda, M., Matsui, T., Imamura, M., Tsukita, S., and ^#Tsukita, S. 1999. Expression level, subcellular distribution and rho-GDI binding affinity of merlin in comparison with Ezrin/Radixin/Moesin proteins. Oncogene. 18(34):4788-97. https://doi.org/10.1038/sj.onc.1202871
^#Yonemura, S., Tsukita, S., and Tsukita, S. 1999. Direct involvement of ezrin/radixin/moesin (ERM)-binding membrane proteins in the organization of microvilli in collaboration with activated ERM proteins. J Cell Biol. 145(7):1497-509. https://doi.org/10.1083/jcb.145.7.1497
Doi, Y., Itoh, M., Yonemura, S., Ishihara, S., Takano, H., Noda, T., and ^#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(4):2315-21. https://doi.org/10.1074/jbc.274.4.2315
^#Chishti, A.H., Kim, A.C., Marfatia, S.M., Lutchman, M., Hanspal, M., Jindal, H., Liu, S.C., Low, P.S., Rouleau, G.A., Mohandas, N., Chasis, J.A., Conboy, J.G., Gascard, P., Takakuwa, Y., Huang, S.C., Benz, E.J Jr., Bretscher, A., Fehon, R.G., Gusella, J.F., Ramesh, V., Solomon, F., Marchesi, V.T., Tsukita, S., Tsukita, S., and ^#Hoover, K.B. et al. 1998. The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane. Trends Biochem Sci. 23(8):281-2. https://doi.org/10.1016/s0968-0004(98)01237-7
^#Yonemura, S., Hirao, M., Doi, Y., Takahashi, N., Kondo, T., Tsukita, S., and 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. J Cell Biol. 140(4):885-95. https://doi.org/10.1083/jcb.140.4.885
Matsui, T., Maeda, M., Doi, Y., Yonemura, S., Amano, M., Kaibuchi, K., Tsukita, S., and ^#Tsukita, S. 1998. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J Cell Biol. 140(3):647-57. https://doi.org/10.1083/jcb.140.3.647
Doi, Y., Kurita, M., Matsumoto, M., Kondo, T., Noda, T., Tsukita, S., Tsukita, S., and ^#Seya, T. 1998. Moesin is not a receptor for measles virus entry into mouse embryonic stem cells. J Virol. 72(2):1586-92. https://doi.org/10.1128/JVI.72.2.1586-1592.1998
Sagara, J., Tochikura, T.S., Tanaka, H., Baba, Y., Tsukita, S., Tsukita, S., and ^#Kawai, A. 1998. The 21-kDa polypeptide (VAP21) in the rabies virion is a CD99-related host cell protein. Microbiol Immunol. 42(4):289-97. https://doi.org/10.1111/j.1348-0421.1998.tb02285.x
Kondo, T., Takeuchi, K., Doi, Y., Yonemura, S., Nagata, S., Tsukita, S., and ^#Tsukita, S. 1997. ERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis. J Cell Biol. 139(3):749-58. https://doi.org/10.1083/jcb.139.3.749
Tsukita, S., Yonemura, S., and ^#Tsukita, S. 1997. ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction. Curr Opin Cell Biol. 9(1):70-5. https://doi.org/10.1016/s0955-0674(97)80154-8
Tsukita, S., Yonemura, S., and ^#Tsukita, S. 1997. ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. Trends Biochem Sci. 22(2):53-8. https://doi.org/10.1016/s0968-0004(96)10071-2
Sagara, J., Tochikura, T.S., Yamamoto, T., Tsukita, S., Tsukita, S., and ^#Kawai, A. 1997. Immunological studies of a 21 kDa cellular component efficiently incorporated into rabies virion grown in a BHK-21 cell culture. Microbiol Immunol. 41(12):947-55. https://doi.org/10.1111/j.1348-0421.1997.tb01954.x
Hirao, M., Sato, N., Kondo, T., Yonemura, S., Monden, M., Sasaki, T., Takai, Y., Tsukita, S., and ^#Tsukita, S. 1996. Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J Cell Biol. 135(1):37-51. https://doi.org/10.1083/jcb.135.1.37
Furuse, M., Fujimoto, K., Sato, N., Hirase, T., Tsukita, S., and ^#Tsukita, S. 1996. Overexpression of occludin, a tight junction-associated integral membrane protein, induces the formation of intracellular multilamellar bodies bearing tight junction-like structures. J Cell Sci. 109 ( Pt 2):429-35.
Takeda, H., Nagafuchi, A., Yonemura, S., Tsukita, S., Behrens, J., Birchmeier, W., and ^#Tsukita, S. 1995. V-src kinase shifts the cadherin-based cell adhesion from the strong to the weak state and beta catenin is not required for the shift. J Cell Biol. 131(6 Pt 2):1839-47. https://doi.org/10.1083/jcb.131.6.1839
Takaishi, K., Sasaki, T., Kameyama, T., Tsukita, S., Tsukita, S., and ^#Takai, Y. 1995. Translocation of activated Rho from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows. Oncogene. 11(1):39-48.
Sagara, J., Tsukita, S., Yonemura, S., Tsukita, S., and ^#Kawai, A. 1995. Cellular actin-binding ezrin-radixin-moesin (ERM) family proteins are incorporated into the rabies virion and closely associated with viral envelope proteins in the cell. Virology. 206(1):485-94. https://doi.org/10.1016/s0042-6822(95)80064-6
Furuse, M., Itoh, M., Hirase, T., Nagafuchi, A., Yonemura, S., Tsukita, S., and ^#Tsukita, S. 1994. Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J Cell Biol. 127(6 Pt 1):1617-26. https://doi.org/10.1083/jcb.127.6.1617
Watabe, M., Nagafuchi, A., Tsukita, S., and ^#Takeichi, M. 1994. Induction of polarized cell-cell association and retardation of growth by activation of the E-cadherin-catenin adhesion system in a dispersed carcinoma line. J Cell Biol. 127(1):247-56. https://doi.org/10.1083/jcb.127.1.247
^#Tsukita, S., Oishi, K., Sato, N., Sagara, J., Kawai, A., and Tsukita, S. 1994. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J Cell Biol. 126(2):391-401. https://doi.org/10.1083/jcb.126.2.391
Takeuchi, K., Sato, N., Kasahara, H., Funayama, N., Nagafuchi, A., Yonemura, S., Tsukita, S., and ^#Tsukita,S. 1994. Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members. J Cell Biol. 125(6):1371-84. https://doi.org/10.1083/jcb.125.6.1371
Kishino, T., Ariga, T., Soejima, H., Tamura, T., Ohta, T., Jinno, Y., Yonemura, S., Sato, N., Tsukita, S., and Tsukita,S., et al. 1994. Assignment of the human moesin gene (MSN) to chromosome region Xq11.2-->q12. Cytogenet Cell Genet. 66(3):167-9. https://doi.org/10.1159/000133692
Tsukita, S., Tsukita, S., Nagafuchi, A., and Yonemura, S. 1994. Possible involvement of adherens junction plaque proteins in tumorigenesis and metastasis. Princess Takamatsu Symp. 24:38-50.
Furuse, M., Hirase, T., Itoh, M., Nagafuchi, A., Yonemura, S., Tsukita, S., and ^#Tsukita, S. 1993. Occludin: a novel integral membrane protein localizing at tight junctions. J Cell Biol. 123(6 Pt 2):1777-88. https://doi.org/10.1083/jcb.123.6.1777
^#Tsukita, S., Itoh, M., Nagafuchi, A., Yonemura, S., and Tsukita, S. 1993. Submembranous junctional plaque proteins include potential tumor suppressor molecules. J Cell Biol. 123(5):1049-53. https://doi.org/10.1083/jcb.123.5.1049
^#Hashimoto, T., Amagai, M., Parry, D.A., Dixon, T.W., Tsukita, S., Tsukita, S., Miki, K., Sakai, K., Inokuchi, Y., and Kudoh, J., et al. 1993. Desmoyokin, a 680 kDa keratinocyte plasma membrane-associated protein, is homologous to the protein encoded by human gene AHNAK. J Cell Sci. 105 ( Pt 2):275-86.
Itoh, M., Nagafuchi, A., Yonemura, S., Kitani-Yasuda, T., Tsukita, S., and Tsukita, S. 1993. 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 microscopy. J Cell Biol. 121(3):491-502. https://doi.org/10.1083/jcb.121.3.491
Tsukita, S., Tsukita, S., Nagafuchi, A., and Yonemura, S. 1992. Molecular linkage between cadherins and actin filaments in cell-cell adherens junctions. Curr Opin Cell Biol. 4(5):834-9. https://doi.org/10.1016/0955-0674(92)90108-o
Sato, N., Funayama, N., Nagafuchi, A., Yonemura, S., Tsukita, S., and Tsukita, S. 1992. A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites. J Cell Sci. 103 ( Pt 1):131-43.
Itoh, M., Yonemura, S., Nagafuchi, A., Tsukita, S., and Tsukita, S. 1991. A 220-kD undercoat-constitutive protein: its specific localization at cadherin-based cell-cell adhesion sites. J Cell Biol. 115(5):1449-62. https://doi.org/10.1083/jcb.115.5.1449
Funayama, N., Nagafuchi, A., Sato, N., Tsukita, S., and Tsukita, S. 1991. Radixin is a novel member of the band 4.1 family. J Cell Biol. 115(4):1039-48. https://doi.org/10.1083/jcb.115.4.1039
Tsukita, S., Oishi, K., Akiyama, T., Yamanashi, Y., Yamamoto, T., and Tsukita, S. 1991. Specific proto-oncogenic tyrosine kinases of src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated. J Cell Biol. 113(4):867-79. https://doi.org/10.1083/jcb.113.4.867
Sato, N., Yonemura, S., Obinata, T., Tsukita, S., and Tsukita, S. 1991. Radixin, a barbed end-capping actin-modulating protein, is concentrated at the cleavage furrow during cytokinesis. J Cell Biol. 113(2):321-30. https://doi.org/10.1083/jcb.113.2.321
Nishikawa, S., Tsukita, S., Tsukita, S., and Sasa, S. 1990. Localization of adherens junction proteins along the possible sliding interface between secretory ameloblasts of the rat incisor. Cell Struct Funct. 15(5):245-9. https://doi.org/10.1247/csf.15.245
Tsukita, S., Tsukita, S., and Nagafuchi, A. 1990. The undercoat of adherens junctions: a key specialized structure in organogenesis and carcinogenesis. Cell Struct Funct. 15(1):7-12. https://doi.org/10.1247/csf.15.7
Tsukita, S., Itoh, M., and Tsukita, S. 1989. A new 400-kD protein from isolated adherens junctions: its localization at the undercoat of adherens junctions and at microfilament bundles such as stress fibers and circumferential bundles. J Cell Biol. 109(6 Pt 1):2905-15. https://doi.org/10.1083/jcb.109.6.2905
Hieda, Y., Tsukita, S., and Tsukita, S. 1989. A new high molecular mass protein showing unique localization in desmosomal plaque. J Cell Biol. 109(4 Pt 1):1511-8. https://doi.org/10.1083/jcb.109.4.1511
Tsukita, S., Hieda, Y., and Tsukita, S. 1989. A new 82-kD barbed end-capping protein (radixin) localized in the cell-to-cell adherens junction: purification and characterization. J Cell Biol. 108(6):2369-82. https://doi.org/10.1083/jcb.108.6.2369
Tsukita, S., and Tsukita, S. 1989. Isolation of cell-to-cell adherens junctions from rat liver. J Cell Biol. 108(1):31-41. https://doi.org/10.1083/jcb.108.1.31
Mabuchi, I., Tsukita, S., Tsukita, S., and Sawai, T. 1988. Cleavage furrow isolated from newt eggs: contraction, organization of the actin filaments, and protein components of the furrow. Proc Natl Acad Sci U S A. 85(16):5966-70. https://doi.org/10.1073/pnas.85.16.5966
Tsukita, S., Tsukita, S., and Matsumoto, G. 1988. Light-induced structural changes of cytoskeleton in squid photoreceptor microvilli detected by rapid-freeze method. J Cell Biol. 106(4):1151-60. https://doi.org/10.1083/jcb.106.4.1151
Tsukita, S., Mimura, N., Tsukita, S., Khono, K., Ohtaki, T., Oshima, T., Ishikawa, H., and Asano, A. 1988. Characteristic structures of actin gels induced with hepatic actinogelin or with chicken gizzard alpha-actinin: implication for their function. Cell Motil Cytoskeleton 10(4):451-63. https://doi.org/10.1002/cm.970100402
Fujii, I., Iijima, H., Tsukita, S., Ebizuka, Y., and Sankawa, U. 1987. Purification and properties of dihydrogeodin oxidase fro Aspergillus terreus. J Biochem. 101(1):11-8. https://doi.org/10.1093/oxfordjournals.jbchem.a121881
Tsukita, S., Tsukita, S., Kobayashi, T., and Matsumoto, G. 1986. Subaxolemmal cytoskeleton in squid giant axon. II. Morphological identification of microtubule- and microfilament-associated domains of axolemma. J Cell Biol. 102(5):1710-25. https://doi.org/10.1083/jcb.102.5.1710
Kobayashi, T., Tsukita, S., Tsukita, S., Yamamoto, Y., and Matsumoto, G. 1986. Subaxolemmal cytoskeleton in squid giant axon. I. Biochemical analysis of microtubules, microfilaments, and their associated high-molecular-weight proteins. J Cell Biol. 102(5):1699-709. https://doi.org/10.1083/jcb.102.5.1699
Ohtaki, T., Tsukita, S., Mimura, N., Tsukita, S., and Asano, A. 1985. Interaction of actinogelin with actin. No nucleation but high gelation activity. Eur J Biochem. 153(3):609-20. https://doi.org/10.1111/j.1432-1033.1985.tb09344.x
Tsukita, S., and Tsukita, S. 1985. Desmocalmin: a calmodulin-binding high molecular weight protein isolated from desmosomes. J Cell Biol. 101(6):2070-80. https://doi.org/10.1083/jcb.101.6.2070
Tsukita, S., Tsukita, S., Hosoya, H., and Mabuchi, I. 1985. Barbed end-capping protein regulates polarity of actin filaments from the human erythrocyte membrane. Exp Cell Res. 158(1):280-5. https://doi.org/10.1016/0014-4827(85)90453-7
Mabuchi, I., Hamaguchi, Y., Kobayashi, T., Hosoya, H., Tsukita, S., and Tsukita, S. 1985. Alpha-actinin from sea urchin eggs: biochemical properties, interaction with actin, and distribution in the cell during fertilization and cleavage. J Cell Biol. 100(2):375-83. https://doi.org/10.1083/jcb.100.2.375
Jinbu, Y., Sato, S., Nakao, T., Nakao, M., Tsukita, S., Tsukita, S., and Ishikawa, H. 1984. The role of ankyrin in shape and deformability change of human erythrocyte ghosts. Biochim Biophys Acta. 773(2):237-45. https://doi.org/10.1016/0005-2736(84)90087-7
Jinbu, Y., Sato, S., Nakao, and Tsukita, S. 1984. Ca2+ and Mg2+-ATP-dependent shape change of human erythrocyte ghosts and triton shells. Exp Cell Res. 151(1):160-70. https://doi.org/10.1016/0014-4827(84)90365-3
Tsukita, S., Tsukita, S., and Ishikawa, H. 1984. Bidirectional polymerization of G-actin on the human erythrocyte membrane. J Cell Biol. 98(3):1102-10. https://doi.org/10.1083/jcb.98.3.1102
Tsukita, S., Tsukita, S., Ishikawa, H., Kurokawa, M., Morimoto, K., Sobue, K., and Kakiuchi, S. 1983. Binding sites of calmodulin and actin on the brain spectrin, calspectin. J Cell Biol. 97(2):574-8. https://doi.org/10.1083/jcb.97.2.574
Tsukita, S., Tsukita, S., Usukura, J., and Ishikawa, H. 1983. ATP-dependent structural changes of the outer dynein arm in Tetrahymena cilia: a freeze-etch replica study. J Cell Biol. 96(5):1480-5. https://doi.org/10.1083/jcb.96.5.1480
Tsukita, S., Tsukita, S., and Ishikawa, H. 1983. Association of actin and 10 nm filaments with the dense body in smooth muscle cells of the chicken gizzard. Cell Tissue Res. 229(2):233-42. https://doi.org/10.1007/BF00214972
Tsukita, S., Tsukita, S., Usukura, J., and Ishikawa, H. 1982. Myosin filaments in smooth muscle cells of the guinea pig taenia coli: a freeze-substitution study. Eur J Cell Biol. 28(2):195-201.
Tsukita, S., Usukura, J., Tsukita, S., and Ishikawa, H. 1982. The cytoskeleton in myelinated axons: a freeze-etch replica study. Neuroscience. 7(9):2135-47. https://doi.org/10.1016/0306-4522(82)90125-7
Tsukita, S., Tsukita, S., Ishikawa, H., Sato, S., and Nakao, M. 1981. Electron microscopic study of reassociation of spectrin and actin with the human erythrocyte membrane. J Cell Biol. 1981 Jul;90(1):70-7. https://doi.org/10.1083/jcb.90.1.70
Tsukita, S., Tsukita, S., and Ishikawa, H. 1980. Cytoskeletal network underlying the human erythrocyte membrane. Thin-section electron microscopy. J Cell Biol. 1980 Jun;85(3):567-76. https://doi.org/10.1083/jcb.85.3.567