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Volumn 115, Issue 21, 2002, Pages 3991-4000

Protein 4.1 tumor suppressors: Getting a FERM grip on growth regulation

Author keywords

DAL 1; Merlin; Schwannomin; Tumor suppressor

Indexed keywords

ACTIN; CELL SURFACE PROTEIN; ERYTHROCYTE BAND 4.1 PROTEIN; EZRIN; HERMES ANTIGEN; MERLIN; MOESIN; RADIXIN; TUMOR SUPPRESSOR PROTEIN; CYTOSKELETON PROTEIN; MEMBRANE PROTEIN; NEURONAL MEMBRANE CYTOSKELETAL PROTEIN 4.1; NEUROPEPTIDE;

EID: 0036860545     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00094     Document Type: Review
Times cited : (166)

References (104)
  • 1
    • 0036148093 scopus 로고    scopus 로고
    • The neurofibromatosis type 2 gene product, merlin, reverses the F-actin cytoskeletal defects in primary human schwannoma cells
    • Bashour, A. M., Meng, J. J., Ip, W., MacCollin, M. and Ratner, N. (2002). The neurofibromatosis type 2 gene product, merlin, reverses the F-actin cytoskeletal defects in primary human schwannoma cells. Mol. Cell. Biol. 22, 1150-1157.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1150-1157
    • Bashour, A.M.1    Meng, J.J.2    Ip, W.3    MacCollin, M.4    Ratner, N.5
  • 3
    • 0034695446 scopus 로고    scopus 로고
    • CD44 interaction with tiam1 promotes Rac1 signaling and hyaluronic acid-mediated breast tumor cell migration
    • Bourguignon, L. Y., Zhu, H., Shao, L. and Chen, Y. W. (2000). CD44 interaction with tiam1 promotes Rac1 signaling and hyaluronic acid-mediated breast tumor cell migration. J. Biol. Chem. 275, 1829-1838.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1829-1838
    • Bourguignon, L.Y.1    Zhu, H.2    Shao, L.3    Chen, Y.W.4
  • 4
    • 0035966019 scopus 로고    scopus 로고
    • Hyaluronan promotes CD44v3-Vav2 interaction with Grb2-p185(HER2) and induces Rac1 and Ras signaling during ovarian tumor cell migration and growth
    • Bourguignon, L. Y., Zhu, H., Zhou, B., Diedrich, F., Singleton, P. A. and Hung, M. C. (2001). Hyaluronan promotes CD44v3-Vav2 interaction with Grb2-p185(HER2) and induces Rac1 and Ras signaling during ovarian tumor cell migration and growth. J. Biol. Chem. 276, 48679-48692.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48679-48692
    • Bourguignon, L.Y.1    Zhu, H.2    Zhou, B.3    Diedrich, F.4    Singleton, P.A.5    Hung, M.C.6
  • 5
    • 0034987492 scopus 로고    scopus 로고
    • Normal membrane localization and actin association of the NF2 tumor suppressor protein are dependent on folding of its N-terminal domain
    • Brault, E., Gautreau, A., Lamarine, M., Callebaut, I., Thomas, G. and Goutebroze, L. (2001). Normal membrane localization and actin association of the NF2 tumor suppressor protein are dependent on folding of its N-terminal domain. J Cell Sci. 114, 1901-1912.
    • (2001) J. Cell Sci. , vol.114 , pp. 1901-1912
    • Brault, E.1    Gautreau, A.2    Lamarine, M.3    Callebaut, I.4    Thomas, G.5    Goutebroze, L.6
  • 6
    • 0033005974 scopus 로고    scopus 로고
    • Regulation of cortical structure by the ezrin-radixinmoesin protein family
    • Bretscher, A. (1999). Regulation of cortical structure by the ezrin-radixinmoesin protein family. Curr. Opin. Cell Biol. 11, 109-116.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 109-116
    • Bretscher, A.1
  • 7
    • 0020999298 scopus 로고
    • Talin: A cytoskeletal component concentrated in adhesion plaques and other sites of actin-membrane interaction
    • Burridge, K. and Connell, L. (1983). Talin: a cytoskeletal component concentrated in adhesion plaques and other sites of actin-membrane interaction. Cell Motil. 3, 405-417.
    • (1983) Cell Motil. , vol.3 , pp. 405-417
    • Burridge, K.1    Connell, L.2
  • 8
    • 0035831517 scopus 로고    scopus 로고
    • Hrs interacts with sorting nexin 1 and regulates degradation of epidermal growth factor receptor
    • Chin, L.-S., Raynor, M. C., Wei, X., Chen, H.-Q. and Li, L. (2001). Hrs interacts with sorting nexin 1 and regulates degradation of epidermal growth factor receptor. J. Biol. Chem. 276, 7069-7078.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7069-7078
    • Chin, L.-S.1    Raynor, M.C.2    Wei, X.3    Chen, H.-Q.4    Li, L.5
  • 10
    • 0034794184 scopus 로고    scopus 로고
    • The interface of receptor trafficking and signaling
    • Clague, M. J. and Urbe, S. (2001). The interface of receptor trafficking and signaling. J. Cell Sci. 114, 3075-3081.
    • (2001) J. Cell Sci. , vol.114 , pp. 3075-3081
    • Clague, M.J.1    Urbe, S.2
  • 11
    • 0023793054 scopus 로고
    • Erythrocyte protein 4.1 associates with tubulin
    • Correas, I. and Avila, J. (1988). Erythrocyte protein 4.1 associates with tubulin. Biochem. J. 255, 217-221.
    • (1988) Biochem. J. , vol.255 , pp. 217-221
    • Correas, I.1    Avila, J.2
  • 13
    • 0035912664 scopus 로고    scopus 로고
    • The 2.7 A crystal structure of the activated FERM domain of moesin: An analysis of structural changes on activation
    • Edwards, S. D. and Keep, N. H. (2001). The 2.7 A crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation. Biochemistry 40, 7061-7068.
    • (2001) Biochemistry , vol.40 , pp. 7061-7068
    • Edwards, S.D.1    Keep, N.H.2
  • 16
    • 0029121577 scopus 로고
    • Ezrin self-association involves binding of an N-terminal domain to a normally masked carboxyl terminal domain that includes the F-actin binding site
    • Gary, R. and Bretscher, A. (1995). Ezrin self-association involves binding of an N-terminal domain to a normally masked carboxyl terminal domain that includes the F-actin binding site. Mol. Biol. Cell 6, 1061-1075.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1061-1075
    • Gary, R.1    Bretscher, A.2
  • 17
    • 0037062586 scopus 로고    scopus 로고
    • Functional characterization of spectrin-actin-binding domains in 4.1 family of proteins
    • Gimm, J. A., An, X., Nunomura, W. and Mohandas, N. (2002). Functional characterization of spectrin-actin-binding domains in 4.1 family of proteins. Biochemistry 41, 7275-7282.
    • (2002) Biochemistry , vol.41 , pp. 7275-7282
    • Gimm, J.A.1    An, X.2    Nunomura, W.3    Mohandas, N.4
  • 19
    • 0033607687 scopus 로고    scopus 로고
    • Interdomain interaction of merlin isoforms and its influence on intermolecular binding to NHE-RF
    • Gonzalez-Agosti, C., Wiederhold, T., Herndon, M. E., Gusella, J. and Ramesh, V. (1999). Interdomain interaction of merlin isoforms and its influence on intermolecular binding to NHE-RF. J. Biol. Chem. 274, 34438-34442.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34438-34442
    • Gonzalez-Agosti, C.1    Wiederhold, T.2    Herndon, M.E.3    Gusella, J.4    Ramesh, V.5
  • 20
    • 0033970229 scopus 로고    scopus 로고
    • Cloning and characterization of SCHIP-1 , a novel protein interacting specifically with spliced isoforms and naturally occurring mutant NF2 proteins
    • Goutebroze, L., Brault, E., Muchardt, C., Camonis, J. and Thomas, G. (2000). Cloning and characterization of SCHIP-1 , a novel protein interacting specifically with spliced isoforms and naturally occurring mutant NF2 proteins. Mol. Cell. Biol. 20, 1699-1712.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1699-1712
    • Goutebroze, L.1    Brault, E.2    Muchardt, C.3    Camonis, J.4    Thomas, G.5
  • 21
    • 0025992880 scopus 로고
    • Identification, cloning, and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to cytoskeletal protein 4.1
    • Gu, M. X., York, J. D., Warshawsky, I. and Majerus, P. W. (1991). Identification, cloning, and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to cytoskeletal protein 4.1. Proc. Natl. Acad. Sci. USA. 88, 5867-5871.
    • (1991) Proc. Natl. Acad. Sci. USA. , vol.88 , pp. 5867-5871
    • Gu, M.X.1    York, J.D.2    Warshawsky, I.3    Majerus, P.W.4
  • 22
    • 0030853891 scopus 로고    scopus 로고
    • Loss of merlin expression in sporadic meningiomas, ependymomas and schwannomas
    • Gutmann, D. H., Giordano, M. J., Fishback, A. S. and Guha, A. (1997). Loss of merlin expression in sporadic meningiomas, ependymomas and schwannomas. Neurology 49, 267-270.
    • (1997) Neurology , vol.49 , pp. 267-270
    • Gutmann, D.H.1    Giordano, M.J.2    Fishback, A.S.3    Guha, A.4
  • 23
    • 0033485979 scopus 로고    scopus 로고
    • Neurofibromatosis 2 tumor suppressor protein, merlin, forms two functionally important intramolecular associations
    • Gutmann, D. H., Haipek, C. A. and Lu, K. H. (1999a). Neurofibromatosis 2 tumor suppressor protein, merlin, forms two functionally important intramolecular associations. J. Neurosci. Res. 58, 706-716.
    • (1999) J. Neurosci. Res. , vol.58 , pp. 706-716
    • Gutmann, D.H.1    Haipek, C.A.2    Lu, K.H.3
  • 24
    • 0032899713 scopus 로고    scopus 로고
    • Increased expression of the NF2 tumor suppressor gene product, merlin, impairs cell motility, adhesion and spreading
    • Gutmann, D. H., Sherman, L., Seftor, L., Haipek, C., Lu, K. H. and Hendrix, M. (1999b). Increased expression of the NF2 tumor suppressor gene product, merlin, impairs cell motility, adhesion and spreading. Hum. Mol. Genet. 8, 267-275.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 267-275
    • Gutmann, D.H.1    Sherman, L.2    Seftor, L.3    Haipek, C.4    Lu, K.H.5    Hendrix, M.6
  • 26
    • 0035394852 scopus 로고    scopus 로고
    • Functional analysis of neurofibromatosis 2 (NF2) missense mutations
    • Gutmann, D. H., Hirbe, A. C. and Haipek, C. A. (2001a). Functional analysis of neurofibromatosis 2 (NF2) missense mutations. Hum. Mol. Genet. 10, 1519-1529.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1519-1529
    • Gutmann, D.H.1    Hirbe, A.C.2    Haipek, C.A.3
  • 27
    • 0035311373 scopus 로고    scopus 로고
    • The NF2 interactor, hepatocyte growth factor-regulated tyrosine kinase substrate (HRS), associates with merlin in the 'open' conformation and suppresses cell growth and motility
    • Gutmann, D. H., Haipek, C. A., Burke, S. P., Sun, C. X., Scoles, D. R. and Pulst, S. M. (2001b). The NF2 interactor, hepatocyte growth factor-regulated tyrosine kinase substrate (HRS), associates with merlin in the 'open' conformation and suppresses cell growth and motility. Hum. Mol. Genet. 10, 825-834.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 825-834
    • Gutmann, D.H.1    Haipek, C.A.2    Burke, S.P.3    Sun, C.X.4    Scoles, D.R.5    Pulst, S.M.6
  • 28
    • 0035029796 scopus 로고    scopus 로고
    • The protein 4.1 tumor suppressor, DAL-1, impairs cell motility, but regulates proliferation in a cell-type-specific fashion
    • Gutmann, D. H., Hirbe, A. C., Huang, Z. Y. and Haipek, C. A. (2001c). The protein 4.1 tumor suppressor, DAL-1, impairs cell motility, but regulates proliferation in a cell-type-specific fashion. Neurobiol. Dis. 8, 266-278.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 266-278
    • Gutmann, D.H.1    Hirbe, A.C.2    Huang, Z.Y.3    Haipek, C.A.4
  • 29
    • 0034283003 scopus 로고    scopus 로고
    • Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain
    • Hamada, K., Shimizu, T., Matsui, T., Tsukita, S. and Hakoshima, T. (2000). Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J. 19, 4449-4462.
    • (2000) EMBO J. , vol.19 , pp. 4449-4462
    • Hamada, K.1    Shimizu, T.2    Matsui, T.3    Tsukita, S.4    Hakoshima, T.5
  • 30
    • 0034703046 scopus 로고    scopus 로고
    • Early endosomal localization of hrs; requires a sequence within the proline- and glutamine-rich region but not the FYVE finger
    • Hayakawa, A. and Kitamura, N. (2000). Early endosomal localization of hrs; requires a sequence within the proline- and glutamine-rich region but not the FYVE finger. J. Biol. Chem. 275, 29636-29642.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29636-29642
    • Hayakawa, A.1    Kitamura, N.2
  • 31
    • 0028268605 scopus 로고
    • Localization of the protein 4.1-binding site on human erythrocyte glycophorins C and D
    • Hemming, N. J., Anstee, D. J., Mawby, W. J., Reid, M. E. and Tanner, M. J. (1994). Localization of the protein 4.1-binding site on human erythrocyte glycophorins C and D. Biochem. J. 299, 191-196.
    • (1994) Biochem. J. , vol.299 , pp. 191-196
    • Hemming, N.J.1    Anstee, D.J.2    Mawby, W.J.3    Reid, M.E.4    Tanner, M.J.5
  • 32
    • 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. 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, 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
  • 33
    • 0017240365 scopus 로고
    • Heterogeneity in the conformation of different protein fractions from the human erythrocyte membrane
    • Holzwarth, G., Yu, J. and Steck, T. L. (1976). Heterogeneity in the conformation of different protein fractions from the human erythrocyte membrane. J. Supramol. Struct. 4, 161-168.
    • (1976) J. Supramol. Struct. , vol.4 , pp. 161-168
    • Holzwarth, G.1    Yu, J.2    Steck, T.L.3
  • 34
    • 0034661516 scopus 로고    scopus 로고
    • Protein 4.1R binding to eIF3-p44 suggests an interaction between the cytoskeletal network and the translational apparatus
    • Hou, C. L., Tang, C. C., Roffler, S. R. and Tang, T. K. (2000). Protein 4.1R binding to eIF3-p44 suggests an interaction between the cytoskeletal network and the translational apparatus. Blood 96, 747-753.
    • (2000) Blood , vol.96 , pp. 747-753
    • Hou, C.L.1    Tang, C.C.2    Roffler, S.R.3    Tang, T.K.4
  • 36
    • 0033800738 scopus 로고    scopus 로고
    • Protein 4.1R-135 interacts with a novel centrosomal protein (CPAP) which is associated with the gamma-tubulin complex
    • Hung, L. Y., Tang, C. C. and Tang, T. K. (2000). Protein 4.1R-135 interacts with a novel centrosomal protein (CPAP) which is associated with the gamma-tubulin complex. Mol. Cell. Biol. 20, 7813-7825.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7813-7825
    • Hung, L.Y.1    Tang, C.C.2    Tang, T.K.3
  • 37
    • 0032747316 scopus 로고    scopus 로고
    • Inhibition of NF2-negative and NF2-positive primary human meningioma cell proliferation by overexpression of merlin due to vector-mediated gene transfer
    • Ikeda, K., Saeki, Y., Gonzalez-Agosti, C., Ramesh, V. and Chiocca, E. A. (1999). Inhibition of NF2-negative and NF2-positive primary human meningioma cell proliferation by overexpression of merlin due to vector-mediated gene transfer. Neurosurgery 91, 85-92.
    • (1999) Neurosurgery , vol.91 , pp. 85-92
    • Ikeda, K.1    Saeki, Y.2    Gonzalez-Agosti, C.3    Ramesh, V.4    Chiocca, E.A.5
  • 41
    • 0037155916 scopus 로고    scopus 로고
    • Merlin Phosphorylation by p2l-activated Kinase 2 and Effects of Phosphorylation on Merlin Localization
    • Kissil, J. L., Johnson, K. C., Eckman, M. S. and Jacks, T. (2002). Merlin Phosphorylation by p2l-activated Kinase 2 and Effects of Phosphorylation on Merlin Localization. J. Biol. Chem. 277, 10394-10399.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10394-10399
    • Kissil, J.L.1    Johnson, K.C.2    Eckman, M.S.3    Jacks, T.4
  • 42
    • 0035092616 scopus 로고    scopus 로고
    • Merlin, the Drosophila homologue of neurofibromatosis-2, is specifically required in posterior follicle cells for axis formation in the oocyte
    • MacDougall, N., Lad, Y., Wilkie, G. S., Francis-Lang, H., Sullivan, W. and Davis, I. (2001). Merlin, the Drosophila homologue of neurofibromatosis-2, is specifically required in posterior follicle cells for axis formation in the oocyte. Development 128, 665-673.
    • (2001) Development , vol.128 , pp. 665-673
    • MacDougall, N.1    Lad, Y.2    Wilkie, G.S.3    Francis-Lang, H.4    Sullivan, W.5    Davis, I.6
  • 44
    • 0028917977 scopus 로고
    • Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein
    • Marfatia, S. M., Leu, R. A., Branton, D. and Chishti, A. H. (1995). Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein. J. Biol. Chem. 270, 715-719.
    • (1995) J. Biol. Chem. , vol.270 , pp. 715-719
    • Marfatia, S.M.1    Leu, R.A.2    Branton, D.3    Chishti, A.H.4
  • 45
    • 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. 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, 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
  • 46
    • 0033523986 scopus 로고    scopus 로고
    • Activation of ERM proteins in vivo by Rho involves phosphatidyl-inositol 4-phosphate 5-kinase and not ROCK kinases
    • 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, 1259-1262.
    • (1999) Curr. Biol. , vol.9 , pp. 1259-1262
    • Matsui, T.1    Yonemura, S.2    Tsukita, S.3    Tsukita, S.4
  • 47
  • 48
    • 0034033896 scopus 로고    scopus 로고
    • The neurofibromatosis-2 homologue, Merlin, and the tumor suppressor expanded function together in Drosophila to regulate cell proliferation and differentiation
    • McCartney, B. M., Kulikauskas, R. M., LaJeunesse, D. R. and Fehon, R. G. (2000). The neurofibromatosis-2 homologue, Merlin, and the tumor suppressor expanded function together in Drosophila to regulate cell proliferation and differentiation. Development 127, 1315-1324.
    • (2000) Development , vol.127 , pp. 1315-1324
    • McCartney, B.M.1    Kulikauskas, R.M.2    LaJeunesse, D.R.3    Fehon, R.G.4
  • 49
    • 0030924657 scopus 로고    scopus 로고
    • The Nf2 tumor suppressor gene product is essential for extraembryonic development immediately prior to gastrulation
    • McClatchey, A. I., Saotome, I., Ramesh, V., Gusella, J. F. and Jacks, T. (1997). The Nf2 tumor suppressor gene product is essential for extraembryonic development immediately prior to gastrulation. Genes Dev. 11, 1253-1265.
    • (1997) Genes Dev. , vol.11 , pp. 1253-1265
    • McClatchey, A.I.1    Saotome, I.2    Ramesh, V.3    Gusella, J.F.4    Jacks, T.5
  • 50
    • 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. and Jacks, T. (1998). Mice heterozygous for a mutation at the Nf2 tumor suppressor locus develop a range of highly metastatic tumors. Genes Dev. 12, 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
  • 51
    • 0034670030 scopus 로고    scopus 로고
    • Interaction between two isoforms of the NF2 tumor suppressor protein, merlin, and between merlin and ezrin, suggests modulation of ERM proteins by merlin
    • Meng, J. J., Lowrie, D. J., Sun, H., Dorsey, E., Pelton, P. D., Bashour, A. M., Groden, J., Ratner, N. and Ip, W. (2000). Interaction between two isoforms of the NF2 tumor suppressor protein, merlin, and between merlin and ezrin, suggests modulation of ERM proteins by merlin. J. Neurosci. Res. 62, 491-502.
    • (2000) J. Neurosci. Res. , vol.62 , pp. 491-502
    • Meng, J.J.1    Lowrie, D.J.2    Sun, H.3    Dorsey, E.4    Pelton, P.D.5    Bashour, A.M.6    Groden, J.7    Ratner, N.8    Ip, W.9
  • 54
    • 0035871299 scopus 로고    scopus 로고
    • The NF2 tumor suppressor gene product, merlin, mediates contact inhibition of growth through interactions with CD44
    • Morrison, H., Sherman, L. S., Legg, J., Banine, F., Isacke, C., Haipek, C. A., Gutmann, D. H., Ponta, H. and Herrlich, P. (2001). The NF2 tumor suppressor gene product, merlin, mediates contact inhibition of growth through interactions with CD44. Genes Dev. 15, 968-980.
    • (2001) Genes Dev. , vol.15 , pp. 968-980
    • Morrison, H.1    Sherman, L.S.2    Legg, J.3    Banine, F.4    Isacke, C.5    Haipek, C.A.6    Gutmann, D.H.7    Ponta, H.8    Herrlich, P.9
  • 56
    • 0034528346 scopus 로고    scopus 로고
    • 14-3-3 proteins: Regulation of subcellular localization by molecular interference
    • Muslin, A. J. and Xing, H. (2000). 14-3-3 proteins: regulation of subcellular localization by molecular interference. Cell Signal. 12, 703-709.
    • (2000) Cell Signal , vol.12 , pp. 703-709
    • Muslin, A.J.1    Xing, H.2
  • 57
    • 0035831501 scopus 로고    scopus 로고
    • Hierarchy of merlin and ezrin N- and carboxyl terminal domain interactions in homo- and heterotypic associations and their relationship to binding of scaffolding proteins EBP50 and E3KARP
    • Nguyen, R., Reczek, D. and Bretscher, A. (2001). Hierarchy of merlin and ezrin N- and carboxyl terminal domain interactions in homo- and heterotypic associations and their relationship to binding of scaffolding proteins EBP50 and E3KARP. J. Biol. Chem. 276, 7621-7629.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7621-7629
    • Nguyen, R.1    Reczek, D.2    Bretscher, A.3
  • 58
    • 0030730935 scopus 로고    scopus 로고
    • Regulation of CD44-protein 4.1 interaction by Ca2+ and calmodulin. Implications for modulation of CD44-ankyrin interaction
    • Nunomura, W., Takakuwa, Y., Tokimitsu, R., Krauss, S. W., Kawashima, M. and 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.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30322-30328
    • Nunomura, W.1    Takakuwa, Y.2    Tokimitsu, R.3    Krauss, S.W.4    Kawashima, M.5    Mohandas, N.6
  • 59
    • 0031738241 scopus 로고    scopus 로고
    • Merlin, the neurofibromatosis type 2 gene product, and beta1 integrin associate in isolated and differentiating Schwann cells
    • Obremski, V. J., Hall, A. M. and Fernandez-Valle, C. (1998). Merlin, the neurofibromatosis type 2 gene product, and beta1 integrin associate in isolated and differentiating Schwann cells. J. Neurobiol. 37, 487-501.
    • (1998) J. Neurobiol. , vol.37 , pp. 487-501
    • Obremski, V.J.1    Hall, A.M.2    Fernandez-Valle, C.3
  • 60
    • 0021193967 scopus 로고
    • Analysis of the ternary interaction of the red cell membrane skeletal proteins spectrin, actin, and 4.1
    • Ohanian, V., Wolfe, L. C., John, K. M., Pinder, J. C., Lux, S. E. and Gratzer, W. B. (1984). Analysis of the ternary interaction of the red cell membrane skeletal proteins spectrin, actin, and 4.1. Biochemistry 23, 4416-4420.
    • (1984) Biochemistry , vol.23 , pp. 4416-4420
    • Ohanian, V.1    Wolfe, L.C.2    John, K.M.3    Pinder, J.C.4    Lux, S.E.5    Gratzer, W.B.6
  • 61
    • 0032567361 scopus 로고    scopus 로고
    • Phosphorylation of moesin by Rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microviulli-like structures
    • Oshira, N., Fukata, Y. and Kaibuchi, K. (1998). Phosphorylation of moesin by Rho-associated kinase (Rho-kinase) plays a crucial role in the formation of microviulli-like structures. J. Biol. Chem. 273, 34663-34666.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34663-34666
    • Oshira, N.1    Fukata, Y.2    Kaibuchi, K.3
  • 62
    • 0034603033 scopus 로고    scopus 로고
    • Molecular and functional characterization of protein 4.1B, a novel member of the protein 4.1 family with high level, focal expression in brain
    • Parra, M., Gascard, P., Walensky, L. D., Gimm, J. A., Blackshaw, S., Chan, N., Takakuwa, Y., Berger, T., Lee, G., Chasis, J. A. et al. (2000). Molecular and functional characterization of protein 4.1B, a novel member of the protein 4.1 family with high level, focal expression in brain. J. Biol. Chem. 275, 3247-3255.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3247-3255
    • Parra, M.1    Gascard, P.2    Walensky, L.D.3    Gimm, J.A.4    Blackshaw, S.5    Chan, N.6    Takakuwa, Y.7    Berger, T.8    Lee, G.9    Chasis, J.A.10
  • 63
    • 0021940465 scopus 로고
    • Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton
    • Pasternack, G. R., Anderson, R. A., Leto, T. L. and Marchesi, V. T. (1985). Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton. J. Biol. Chem. 260, 3676-3683.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3676-3683
    • Pasternack, G.R.1    Anderson, R.A.2    Leto, T.L.3    Marchesi, V.T.4
  • 64
    • 0027269982 scopus 로고
    • Identification of hyaluronic acid binding sites in the extracellular domain of CD44
    • Peach, R. J., Hollenbaugh, D., Stamenkovic, I. and Aruffo, A. (1993). Identification of hyaluronic acid binding sites in the extracellular domain of CD44. J. Cell Biol. 122, 257-264.
    • (1993) J. Cell Biol. , vol.122 , pp. 257-264
    • Peach, R.J.1    Hollenbaugh, D.2    Stamenkovic, I.3    Aruffo, A.4
  • 65
    • 0034724536 scopus 로고    scopus 로고
    • Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain
    • Pearson, M. A., Reczek, D., Bretscher, A. and Karplus, P, A. (2000). Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell 101, 259-270.
    • (2000) Cell , vol.101 , pp. 259-270
    • Pearson, M.A.1    Reczek, D.2    Bretscher, A.3    Karplus, P.A.4
  • 66
    • 0032578798 scopus 로고    scopus 로고
    • Ruffling membrane, stress fiber, cell spreading and proliferation abnormalities in human Schwannoma cells
    • Pelton, P. D., Sherman, L. S., Rizvi, T. A., Marchionni, M. A., Wood, P., Friedman, R. A. and Ratner, N. (1998). Ruffling membrane, stress fiber, cell spreading and proliferation abnormalities in human Schwannoma cells. Oncogene 17, 2195-2209.
    • (1998) Oncogene , vol.17 , pp. 2195-2209
    • Pelton, P.D.1    Sherman, L.S.2    Rizvi, T.A.3    Marchionni, M.A.4    Wood, P.5    Friedman, R.A.6    Ratner, N.7
  • 67
    • 0033786149 scopus 로고    scopus 로고
    • Merlin, DAL-1, and progesterone receptor expression in clinicopathologic subsets of meningioma: A correlative immunohistochemical study of 175 cases
    • Perry, A., Cai, D. X., Scheithauer, B. W., Swanson, P. E., Lohse, C. M., Newsham, I. F., Weaver, A. and Gutmann, D. H. (2000). Merlin, DAL-1, and progesterone receptor expression in clinicopathologic subsets of meningioma: a correlative immunohistochemical study of 175 cases. J. Neuropathol. Exp. Neurol. 59, 872-879.
    • (2000) J. Neuropathol. Exp. Neurol. , vol.59 , pp. 872-879
    • Perry, A.1    Cai, D.X.2    Scheithauer, B.W.3    Swanson, P.E.4    Lohse, C.M.5    Newsham, I.F.6    Weaver, A.7    Gutmann, D.H.8
  • 69
    • 0034941051 scopus 로고    scopus 로고
    • FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes
    • Raiborg, C., Bremnes, B., Mehlum, A., Gillooly, D. J., D'Arrigo, A., Stang, E. and Stenmark, H. (2001). FYVE and coiled-coil domains determine the specific localisation of Hrs to early endosomes. J. Cell Sci. 114, 2255-2263.
    • (2001) J. Cell Sci. , vol.114 , pp. 2255-2263
    • Raiborg, C.1    Bremnes, B.2    Mehlum, A.3    Gillooly, D.J.4    D'Arrigo, A.5    Stang, E.6    Stenmark, H.7
  • 70
    • 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. and 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.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18452-18458
    • Reczek, D.1    Bretscher, A.2
  • 71
    • 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. and Bretscher, A. (1997). Identification of EBP50: A PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family. J. Cell Biol. 139, 169-179.
    • (1997) J. Cell Biol. , vol.139 , pp. 169-179
    • Reczek, D.1    Berryman, M.2    Bretscher, A.3
  • 72
    • 0035057686 scopus 로고    scopus 로고
    • Tumorigenesis in neurofibromatosis: New insights and potential therapies
    • Reed, N. and Gutmann, D. H. (2001). Tumorigenesis in neurofibromatosis: new insights and potential therapies. Trends Mol. Med. 7, 157-162.
    • (2001) Trends Mol. Med. , vol.7 , pp. 157-162
    • Reed, N.1    Gutmann, D.H.2
  • 76
    • 0029851536 scopus 로고    scopus 로고
    • Expression of the neurofibromatosis 2 tumor suppressor gene product, merlin, in Schwann cells
    • Scherer, S. S. and Gutmann, D. H. (1996). Expression of the neurofibromatosis 2 tumor suppressor gene product, merlin, in Schwann cells. J. Neurosci. Res. 46, 595-605.
    • (1996) J. Neurosci. Res. , vol.46 , pp. 595-605
    • Scherer, S.S.1    Gutmann, D.H.2
  • 77
    • 0035879768 scopus 로고    scopus 로고
    • Ezrin, radixin, and moesin are components of Schwarm cell microvilli
    • Scherer, S. S., Xu, T., Crino, P., Arroyo, E. J. and Gutmann, D. H. (2001). Ezrin, radixin, and moesin are components of Schwarm cell microvilli. J. Neurosci. Res. 65, 150-164.
    • (2001) J. Neurosci. Res. , vol.65 , pp. 150-164
    • Scherer, S.S.1    Xu, T.2    Crino, P.3    Arroyo, E.J.4    Gutmann, D.H.5
  • 79
    • 0034234579 scopus 로고    scopus 로고
    • The neurofibromatosis 2 tumor suppressor protein interacts with hepatocyte growth factor-regulated tyrosine kinase substrate
    • Scoles, D. R., Huynh, D. P., Chen, M. S., Burke, S. P., Gutmann, D. H. and Pulst, S.-M. (2000). The neurofibromatosis 2 tumor suppressor protein interacts with hepatocyte growth factor-regulated tyrosine kinase substrate. Hum. Mol. Genet. 9, 1567-1574.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1567-1574
    • Scoles, D.R.1    Huynh, D.P.2    Chen, M.S.3    Burke, S.P.4    Gutmann, D.H.5    Pulst, S.-M.6
  • 80
    • 0032571272 scopus 로고    scopus 로고
    • Regulation of the neurofibromatosis type 2 tumor suppressor protein, merlin, by adhesion and growth arrest stimuli
    • Shaw, R. J., McClatchey, A. I. and Jacks, T. (1998). Regulation of the neurofibromatosis type 2 tumor suppressor protein, merlin, by adhesion and growth arrest stimuli. J. Biol. Chem. 273, 7757-7764.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7757-7764
    • Shaw, R.J.1    McClatchey, A.I.2    Jacks, T.3
  • 82
    • 0034332508 scopus 로고    scopus 로고
    • Regulation of AMPA receptor GluR1 subunit surface expression by a 4.1N-linked actin cytoskeletal association
    • Shen, L., Liang, F., Walensky, L. D. and Huagnir, R. L. (2000). Regulation of AMPA receptor GluR1 subunit surface expression by a 4.1N-linked actin cytoskeletal association. J. Neurosci. 20, 7932-7940.
    • (2000) J. Neurosci. , vol.20 , pp. 7932-7940
    • Shen, L.1    Liang, F.2    Walensky, L.D.3    Huagnir, R.L.4
  • 83
    • 0035500494 scopus 로고    scopus 로고
    • Merlin: Hanging tumor suppression on the Rac
    • Sherman, L. S. and Gutmann, D. H. (2001). Merlin: hanging tumor suppression on the Rac. Trends Cell Biol. 11, 442-444.
    • (2001) Trends Cell Biol. , vol.11 , pp. 442-444
    • Sherman, L.S.1    Gutmann, D.H.2
  • 86
    • 0034655545 scopus 로고    scopus 로고
    • Molecular cloning of a nove1 NF2/ERM/4.1 superfamily gene, ehm2, that is expressed in high-metastatic K1735 murine melanoma cells
    • Shimizu, T., Nagamuchi, Y. Tani, M., Kimura, K., Shiroishi, T., Wakana, S. and Yokota, J. (2000). Molecular cloning of a nove1 NF2/ERM/4.1 superfamily gene, ehm2, that is expressed in high-metastatic K1735 murine melanoma cells. Genomics 65, 113-120.
    • (2000) Genomics , vol.65 , pp. 113-120
    • Shimizu, T.1    Nagamuchi, Y.2    Tani, M.3    Kimura, K.4    Shiroishi, T.5    Wakana, S.6    Yokota, J.7
  • 87
    • 0037155867 scopus 로고    scopus 로고
    • Structural basis for neurofibromatosis type 2: Crystal structure of the merlin FERM domain
    • Shimizu, T., Seto, A., Maita, N., Hamada, K., Tsukita, S., Tsukita, S. and Hakoshima, T. (2002). Structural basis for neurofibromatosis type 2: Crystal structure of the merlin FERM domain. J. Biol. Chem. 277, 10332-10336.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10332-10336
    • Shimizu, T.1    Seto, A.2    Maita, N.3    Hamada, K.4    Tsukita, S.5    Tsukita, S.6    Hakoshima, T.7
  • 88
    • 0028304535 scopus 로고
    • Structural diversity of band 4.1 superfamily members
    • Takeuchi, K., Kawashima, A., Nagafuchi, A. and Tsukita, S. (1994). Structural diversity of band 4.1 superfamily members. J. Cell Sci. 107, 1921-1928.
    • (1994) J. Cell Sci. , vol.107 , pp. 1921-1928
    • Takeuchi, K.1    Kawashima, A.2    Nagafuchi, A.3    Tsukita, S.4
  • 89
    • 0025924751 scopus 로고
    • Ca2(+)-dependent regulation of the spectrin/actin interaction by calmodulin and protein 4.1
    • Tanaka, T., Kadowaki, K., Lazarides, E. and Sobue, K. (1991). Ca2(+)-dependent regulation of the spectrin/actin interaction by calmodulin and protein 4.1. J. Biol. Chem. 266, 1134-1140.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1134-1140
    • Tanaka, T.1    Kadowaki, K.2    Lazarides, E.3    Sobue, K.4
  • 90
    • 0032529271 scopus 로고    scopus 로고
    • The 30-kD domain of Protein 4.1 mediates its binding to the carboxyl terminus of pIC1n, a protein involved in cellular volume regulation
    • Tang, C. C. and Tang, T. K. (1998). The 30-kD domain of Protein 4.1 mediates its binding to the carboxyl terminus of pIC1n, a protein involved in cellular volume regulation. Blood 92, 1442-1447.
    • (1998) Blood , vol.92 , pp. 1442-1447
    • Tang, C.C.1    Tang, T.K.2
  • 91
    • 0019406583 scopus 로고
    • Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability
    • Tchernia, G., Mohandas, N. and Shohet, S. B. (1981). Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability. J. Clin. Invest. 68, 454-460.
    • (1981) J. Clin. Invest. , vol.68 , pp. 454-460
    • Tchernia, G.1    Mohandas, N.2    Shohet, S.B.3
  • 92
    • 0345252019 scopus 로고    scopus 로고
    • A Novel Member of the NF2/ERM/4.1 Superfamily with Growth Suppressing Properties in Lung Cancer
    • Tran, Y. K., Bogler, O., Gorse, K. M., Wieland, I., Green, M. R. and Newsham, I. F. (1999). A Novel Member of the NF2/ERM/4.1 Superfamily with Growth Suppressing Properties in Lung Cancer. Cancer Res. 59, 35-43.
    • (1999) Cancer Res. , vol.59 , pp. 35-43
    • Tran, Y.K.1    Bogler, O.2    Gorse, K.M.3    Wieland, I.4    Green, M.R.5    Newsham, I.F.6
  • 96
    • 0033800735 scopus 로고    scopus 로고
    • Endosomal localization and receptor dynamics determine tyrosine phosphorylation of hepatocyte growth factor-regulated tyrosine kinase substrate
    • Urbe, S., Mills, I. G., Stenmark, H., Kitamura, N. and Clague, M. J. (2000). Endosomal localization and receptor dynamics determine tyrosine phosphorylation of hepatocyte growth factor-regulated tyrosine kinase substrate. Mol. Cell. Biol. 20, 7685-7692.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7685-7692
    • Urbe, S.1    Mills, I.G.2    Stenmark, H.3    Kitamura, N.4    Clague, M.J.5
  • 97
    • 0035475318 scopus 로고    scopus 로고
    • Expanding the role of NHERF, a PDZ-domain containing protein adapter, to growth regulation
    • Voltz, J. W., Weinman, E. J. and Shenolikar, S. (2001). Expanding the role of NHERF, a PDZ-domain containing protein adapter, to growth regulation. Oncogene 20, 6309-6314.
    • (2001) Oncogene , vol.20 , pp. 6309-6314
    • Voltz, J.W.1    Weinman, E.J.2    Shenolikar, S.3
  • 98
    • 0032489868 scopus 로고    scopus 로고
    • The 13-kD FK506 binding protein, FKBP13, interacts with a novel homologue of the erythrocyte membrane cytoskeletal protein 4.1
    • 141
    • Walensky, L. D., Gascard, P., Fields, M. E., Blackshaw, S., Conboy, J. G., Mohandas, N. and Snyder, S. H. (1998). The 13-kD FK506 binding protein, FKBP13, interacts with a novel homologue of the erythrocyte membrane cytoskeletal protein 4.1. J. Cell Biol. 6, 141, 143-153.
    • (1998) J. Cell Biol. , vol.6 , pp. 143-153
    • Walensky, L.D.1    Gascard, P.2    Fields, M.E.3    Blackshaw, S.4    Conboy, J.G.5    Mohandas, N.6    Snyder, S.H.7
  • 99
    • 0037059807 scopus 로고    scopus 로고
    • p2l-activated kinase links Rac/Cdc42 signaling to merlin
    • Xiao, G. H., Beeser, A., Chernoff, J. and Testa, J. R. (2002). p2l-activated kinase links Rac/Cdc42 signaling to merlin. J. Biol. Chem. 277, 883-886.
    • (2002) J. Biol. Chem. , vol.277 , pp. 883-886
    • Xiao, G.H.1    Beeser, A.2    Chernoff, J.3    Testa, J.R.4
  • 100
    • 0032005305 scopus 로고    scopus 로고
    • Merlin differentially associates with the microtubule and actin cytoskeleton
    • Xu, H. M. and Gutmann, D. H. (1998). Merlin differentially associates with the microtubule and actin cytoskeleton. J. Neurosci. Res. 51, 403-415.
    • (1998) J. Neurosci. Res. , vol.51 , pp. 403-415
    • Xu, H.M.1    Gutmann, D.H.2
  • 101
    • 0033573561 scopus 로고    scopus 로고
    • Protein 4.1N binding to nuclear mitotic apparatus protein in PC12 cells mediates the antiproliferative actions of nerve growth factor
    • Ye, K., Compton, D. A., Lai, M. M., Walensky, L. D. and Snyder, S. H. (1999). Protein 4.1N binding to nuclear mitotic apparatus protein in PC12 cells mediates the antiproliferative actions of nerve growth factor. J Neurosci. 19, 10747-10756.
    • (1999) J. Neurosci. , vol.19 , pp. 10747-10756
    • Ye, K.1    Compton, D.A.2    Lai, M.M.3    Walensky, L.D.4    Snyder, S.H.5
  • 102
    • 0033637979 scopus 로고    scopus 로고
    • PIKE: A nuclear GTPase that enhances PI3Kinase activity and is regulated by Protein 4.1N
    • Ye, K., Hurt, J., Wu, F. Y., Fang, M., Luo, H. R., Hong, J. J., Blacksaw, S., Ferris, C. D. and Snyder, S. H. (2000). PIKE: a nuclear GTPase that enhances PI3Kinase activity and is regulated by Protein 4.1N. Cell 103, 919-930.
    • (2000) Cell , vol.103 , pp. 919-930
    • Ye, K.1    Hurt, J.2    Wu, F.Y.3    Fang, M.4    Luo, H.R.5    Hong, J.J.6    Blacksaw, S.7    Ferris, C.D.8    Snyder, S.H.9
  • 103
    • 0036684547 scopus 로고    scopus 로고
    • The 4.1/ezrin/radixin/moesin domain of the DAL-1/Protein 4.1B tumor suppressor interacts with 14-3-3 proteins
    • Yu, T., Robb, V. A., Singh, V., Gutmann, D. H. and Newsham, I. F. (2002). The 4.1/ezrin/radixin/moesin domain of the DAL-1/Protein 4.1B tumor suppressor interacts with 14-3-3 proteins. Biochem. J. 365, 783-789.
    • (2002) Biochem. J. , vol.365 , pp. 783-789
    • Yu, T.1    Robb, V.A.2    Singh, V.3    Gutmann, D.H.4    Newsham, I.F.5


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