메뉴 건너뛰기




Volumn 1423, Issue 2, 1999, Pages

Merlin: The neurofibromatosis 2 tumor suppressor

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; AMINO ACID; CYCLIC AMP DEPENDENT PROTEIN KINASE; EZRIN; HERMES ANTIGEN; INTERCELLULAR ADHESION MOLECULE 1; INTERCELLULAR ADHESION MOLECULE 2; LEUKOSIALIN; MEMBRANE PROTEIN; MERLIN; MOESIN; RADIXIN; RECEPTOR;

EID: 0033602365     PISSN: 0304419X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-419X(99)00005-0     Document Type: Review
Times cited : (114)

References (49)
  • 11
    • 0028907620 scopus 로고
    • Neurofibromatosis type 2 (NF2) gene is somatically mutated in mesothelioma but not in lung cancer
    • Sekido Y., Pass H.I., Bader S., Mew D.J., Christman M.F., Gazdar A.F., Minna J.D. Neurofibromatosis type 2 (NF2) gene is somatically mutated in mesothelioma but not in lung cancer. Cancer Res. 55:1995;1227-1231.
    • (1995) Cancer Res. , vol.55 , pp. 1227-1231
    • Sekido, Y.1    Pass, H.I.2    Bader, S.3    Mew, D.J.4    Christman, M.F.5    Gazdar, A.F.6    Minna, J.D.7
  • 12
    • 0031471375 scopus 로고    scopus 로고
    • Ezrin: A protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures
    • Bretscher A., Reczek D., Berryman M. Ezrin: a protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures. J. Cell. Sci. 110:1997;3011-3018.
    • (1997) J. Cell. Sci. , vol.110 , pp. 3011-3018
    • Bretscher, A.1    Reczek, D.2    Berryman, M.3
  • 13
    • 0031081475 scopus 로고    scopus 로고
    • ERM proteins: Head-to-tail regulation of actin-plasma membrane interaction
    • Tsukita S., Yonemura S., Tsukita S. ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. Trends Biochem. Sci. 22:1997;53-58.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 53-58
    • Tsukita, S.1    Yonemura, S.2    Tsukita, S.3
  • 15
    • 0031043523 scopus 로고    scopus 로고
    • ERM (ezrin/radixin/moesin) family: From cytoskeleton to signal transduction
    • Tsukita S., Yonemura S. ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction. Curr. Opin. Cell. Biol. 9:1997;70-75.
    • (1997) Curr. Opin. Cell. Biol. , vol.9 , pp. 70-75
    • Tsukita, S.1    Yonemura, S.2
  • 16
    • 0032482323 scopus 로고    scopus 로고
    • Identification and functional analysis of the ezrin-binding site in the hyaluronan receptor, CD44
    • Legg J.W., Isacke C.M. Identification and functional analysis of the ezrin-binding site in the hyaluronan receptor, CD44. Curr. Biol. 8:1998;705-708.
    • (1998) Curr. Biol. , vol.8 , pp. 705-708
    • Legg, J.W.1    Isacke, C.M.2
  • 17
    • 0028229539 scopus 로고
    • ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons
    • Tsukita S., Oishi K., Sato N., Sagara J., Kawai A., Tsukita S. ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J. Cell Biol. 126:1994;391-401.
    • (1994) J. Cell Biol. , vol.126 , pp. 391-401
    • Tsukita, S.1    Oishi, K.2    Sato, N.3    Sagara, J.4    Kawai, A.5    Tsukita, S.6
  • 18
    • 0032555599 scopus 로고    scopus 로고
    • Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4,5-bisphosphate
    • Heiska L., Alfthan K., Gronholm M., Vilja P., Vaheri A., Carpen O. Association of ezrin with intercellular adhesion molecule-1 and -2 (ICAM-1 and ICAM-2). Regulation by phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 273:1998;21893-21900.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21893-21900
    • Heiska, L.1    Alfthan, K.2    Gronholm, M.3    Vilja, P.4    Vaheri, A.5    Carpen, O.6
  • 20
    • 0032559637 scopus 로고    scopus 로고
    • 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. 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. 140:1998;885-895.
    • (1998) J. Cell Biol. , vol.140 , pp. 885-895
    • Yonemura, S.1    Hirao, M.2    Doi, Y.3    Takahashi, N.4    Kondo, T.5    Tsukita, S.6
  • 21
    • 0027933858 scopus 로고
    • Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family
    • Turunen O., Wahlstrom T., Vaheri A. Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family. J. Cell Biol. 126:1994;1445-1453.
    • (1994) J. Cell Biol. , vol.126 , pp. 1445-1453
    • Turunen, O.1    Wahlstrom, T.2    Vaheri, A.3
  • 22
    • 0030835761 scopus 로고    scopus 로고
    • A dual involvement of the amino-terminal domain of ezrin in F- And G-actin binding
    • Roy C., Martin M., Mangeat P. A dual involvement of the amino-terminal domain of ezrin in F- and G-actin binding. J. Biol. Chem. 272:1997;20088-20095.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20088-20095
    • Roy, C.1    Martin, M.2    Mangeat, P.3
  • 23
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway
    • Hirao M., Sato N., Kondo T., Yonemura S., Monden M., Sasaki T., Takai Y., Tsukita S., Tsukita S. Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J. Cell Biol. 135:1996;37-51.
    • (1996) J. Cell Biol. , vol.135 , pp. 37-51
    • Hirao, M.1    Sato, N.2    Kondo, T.3    Yonemura, S.4    Monden, M.5    Sasaki, T.6    Takai, Y.7    Tsukita, S.8    Tsukita, S.9
  • 24
    • 0030846295 scopus 로고    scopus 로고
    • Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein
    • Takahashi K., Sasaki T., Mammoto A., Takaishi K., Kameyama T., Tsukita S., Takai Y. Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein. J. Biol. Chem. 272:1997;23371-23375.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23371-23375
    • Takahashi, K.1    Sasaki, T.2    Mammoto, A.3    Takaishi, K.4    Kameyama, T.5    Tsukita, S.6    Takai, Y.7
  • 26
    • 0032498528 scopus 로고    scopus 로고
    • 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. Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. J. Cell Biol. 140:1998;647-657.
    • (1998) J. Cell Biol. , vol.140 , pp. 647-657
    • Matsui, T.1    Maeda, M.2    Doi, Y.3    Yonemura, S.4    Amano, M.5    Kaibuchi, K.6    Tsukita, S.7    Tsukita, S.8
  • 27
    • 0030872949 scopus 로고    scopus 로고
    • Rho- And rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
    • Mackay D.J., Esch F., Furthmayr H., Hall A. Rho- and rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin proteins. J. Cell Biol. 138:1997;927-938.
    • (1997) J. Cell Biol. , vol.138 , pp. 927-938
    • MacKay, D.J.1    Esch, F.2    Furthmayr, H.3    Hall, A.4
  • 29
    • 0032476006 scopus 로고    scopus 로고
    • NHE3 kinase A regulatory protein E3KARP binds the epithelial brush border Na+/H+ exchanger NHE3 and the cytoskeletal protein ezrin
    • Yun C.C., Lamprecht G., Forster D.V., Sidor A. NHE3 kinase A regulatory protein E3KARP binds the epithelial brush border Na+/H+ exchanger NHE3 and the cytoskeletal protein ezrin. J. Biol. Chem. 273:1998;25856-25863.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25856-25863
    • Yun, C.C.1    Lamprecht, G.2    Forster, D.V.3    Sidor, A.4
  • 30
    • 0030990430 scopus 로고    scopus 로고
    • CAmp-mediated inhibition of the epithelial brush border Na+/H+ exchanger, Nhe3, requires an associated regulatory protein
    • Yun C.H., Oh S., Zizak M., Steplock D., Tsao S., Tse C.M., Weinman E.J., Donowitz M. cAmp-mediated inhibition of the epithelial brush border Na+/H+ exchanger, Nhe3, requires an associated regulatory protein. Proc. Natl. Acad. Sci. USA. 94:1997;3010-3015.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3010-3015
    • Yun, C.H.1    Oh, S.2    Zizak, M.3    Steplock, D.4    Tsao, S.5    Tse, C.M.6    Weinman, E.J.7    Donowitz, M.8
  • 31
    • 0032541057 scopus 로고    scopus 로고
    • The carboxyl-terminal region of EBP50 binds to a site in the amino-terminal domain of ezrin that is masked in the dormant molecule
    • Reczek D., Bretscher A. 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. 273:1998;18452-18458.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18452-18458
    • Reczek, D.1    Bretscher, A.2
  • 32
    • 0030608877 scopus 로고    scopus 로고
    • Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family
    • Reczek D., Berryman M., Bretscher A. Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family. J. Cell Biol. 139:1997;169-179.
    • (1997) J. Cell Biol. , vol.139 , pp. 169-179
    • Reczek, D.1    Berryman, M.2    Bretscher, A.3
  • 33
    • 0032522603 scopus 로고    scopus 로고
    • Mice heterozygous for a mutation at the Nf2 tumor suppressor locus develop a range of highly metastatic tumors
    • McClatchey A.I., Saotome I., Mercer K., Crowley D., Gusella J.F., Bronson R.T., Jacks T. Mice heterozygous for a mutation at the Nf2 tumor suppressor locus develop a range of highly metastatic tumors. Genes Dev. 12:1998;1121-1133.
    • (1998) Genes Dev. , vol.12 , pp. 1121-1133
    • McClatchey, A.I.1    Saotome, I.2    Mercer, K.3    Crowley, D.4    Gusella, J.F.5    Bronson, R.T.6    Jacks, T.7
  • 34
    • 0032578033 scopus 로고    scopus 로고
    • Structural analysis of Drosophila merlin reveals functional domains important for growth control and subcellular localization
    • LaJeunesse D.R., McCartney B.M., Fehon R.G. Structural analysis of Drosophila merlin reveals functional domains important for growth control and subcellular localization. J. Cell Biol. 141:1998;1589-1599.
    • (1998) J. Cell Biol. , vol.141 , pp. 1589-1599
    • Lajeunesse, D.R.1    McCartney, B.M.2    Fehon, R.G.3
  • 36
    • 0031868907 scopus 로고    scopus 로고
    • Localization and functional domains of the neurofibromatosis type II tumor suppressor, merlin
    • Shaw R.J., McClatchey A.I., Jacks T. Localization and functional domains of the neurofibromatosis type II tumor suppressor, merlin. Cell. Growth Differ. 9:1998;287-296.
    • (1998) Cell. Growth Differ. , vol.9 , pp. 287-296
    • Shaw, R.J.1    McClatchey, A.I.2    Jacks, T.3
  • 37
    • 0031842160 scopus 로고    scopus 로고
    • Analysis of molecular domains of epitope-tagged merlin isoforms in Cos-7 cells and primary rat Schwann cells
    • Xu L., Gonzalez-Agosti C., Beauchamp R., Pinney D., Sterner C., Ramesh V. Analysis of molecular domains of epitope-tagged merlin isoforms in Cos-7 cells and primary rat Schwann cells. Exp. Cell. Res. 238:1998;231-240.
    • (1998) Exp. Cell. Res. , vol.238 , pp. 231-240
    • Xu, L.1    Gonzalez-Agosti, C.2    Beauchamp, R.3    Pinney, D.4    Sterner, C.5    Ramesh, V.6
  • 38
    • 0032005305 scopus 로고    scopus 로고
    • Merlin differentially associates with the microtubule and actin cytoskeleton
    • Xu H.M., Gutmann D.H. Merlin differentially associates with the microtubule and actin cytoskeleton. J. Neurosci. Res. 51:1998;403-415.
    • (1998) J. Neurosci. Res. , vol.51 , pp. 403-415
    • Xu, H.M.1    Gutmann, D.H.2
  • 41
    • 0028245681 scopus 로고
    • Detection of cellular proteins that interact with the NF2 tumor suppressor gene product
    • Takeshima H., Izawa I., Lee P.S., Safdar N., Levin V.A., Saya H. Detection of cellular proteins that interact with the NF2 tumor suppressor gene product. Oncogene. 9:1994;2135-2144.
    • (1994) Oncogene , vol.9 , pp. 2135-2144
    • Takeshima, H.1    Izawa, I.2    Lee, P.S.3    Safdar, N.4    Levin, V.A.5    Saya, H.6
  • 45
    • 0032555156 scopus 로고    scopus 로고
    • A C-terminal motif found in the beta2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins
    • Hall R.A., Ostedgaard L.S., Premont R.T., Blitzer J.T., Rahman N., Welsh M.J., Lefkowitz R.J. A C-terminal motif found in the beta2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins. Proc. Natl. Acad. Sci. USA. 95:1998;8496-8501.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8496-8501
    • Hall, R.A.1    Ostedgaard, L.S.2    Premont, R.T.3    Blitzer, J.T.4    Rahman, N.5    Welsh, M.J.6    Lefkowitz, R.J.7
  • 47
    • 0032080043 scopus 로고    scopus 로고
    • Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR)
    • Wang S., Raab R.W., Schatz P.J., Guggino W.B., Li M. Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR). FEBS Lett. 427:1998;103-108.
    • (1998) FEBS Lett. , vol.427 , pp. 103-108
    • Wang, S.1    Raab, R.W.2    Schatz, P.J.3    Guggino, W.B.4    Li, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.