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Volumn 51, Issue 3, 1998, Pages 403-415

Merlin differentially associates with the microtubule and actin cytoskeleton

Author keywords

Actin; Neurofibromatosis 2; Schwannoma; Schwannomin; Tubulin

Indexed keywords

ACTIN; CELL SURFACE PROTEIN; COMPLEMENTARY DNA; MERLIN; TUBULIN; UNCLASSIFIED DRUG;

EID: 0032005305     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4547(19980201)51:3<403::AID-JNR13>3.0.CO;2-7     Document Type: Article
Times cited : (144)

References (38)
  • 1
    • 0027393093 scopus 로고
    • Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker
    • Algrain M, Turunen O, Vaheri A, Louvard D, Arpin M (1993): Ezrin contains cytoskeleton and membrane binding domains accounting for its proposed role as a membrane-cytoskeletal linker. J Cell Biol 120:129-139.
    • (1993) J Cell Biol , vol.120 , pp. 129-139
    • Algrain, M.1    Turunen, O.2    Vaheri, A.3    Louvard, D.4    Arpin, M.5
  • 8
    • 0027364004 scopus 로고
    • Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins
    • Gary R, Bretscher A (1993): Heterotypic and homotypic associations between ezrin and moesin, two putative membrane-cytoskeletal linking proteins. Proc Natl Acad Sci USA 90:10846-10850.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10846-10850
    • Gary, R.1    Bretscher, A.2
  • 9
    • 0029121577 scopus 로고
    • Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site
    • Gary R, Bretscher A (1995): Ezrin self-association involves binding of an N-terminal domain to a normally masked C-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
  • 11
    • 0024814175 scopus 로고
    • cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1
    • Gould KL, Bretscher A, Esch FS, Hunter T (1989): cDNA cloning and sequencing of the protein-tyrosine kinase substrate, ezrin, reveals homology to band 4.1. EMBO J 8:4133-4142.
    • (1989) EMBO J , vol.8 , pp. 4133-4142
    • Gould, K.L.1    Bretscher, A.2    Esch, F.S.3    Hunter, T.4
  • 13
    • 0030853891 scopus 로고    scopus 로고
    • Loss of merlin expression in sporadic meningiomas, ependymomas and schwannomas
    • Gulmann DH, Giordano MJ, Fishback AS, Guha A (1997): Loss of merlin expression in sporadic meningiomas, ependymomas and schwannomas. Neurology 48:267-270.
    • (1997) Neurology , vol.48 , pp. 267-270
    • Gulmann, D.H.1    Giordano, M.J.2    Fishback, A.S.3    Guha, A.4
  • 15
    • 0029033133 scopus 로고
    • Molecular dissection of radixin: Distinct and interdependent functions of the amino- and carboxy-terminal domains
    • Henry MD, Agosti CG, Solomon F (1995): Molecular dissection of radixin: Distinct and interdependent functions of the amino- and carboxy-terminal domains. J Cell Biol 129:1007-1022.
    • (1995) J Cell Biol , vol.129 , pp. 1007-1022
    • Henry, M.D.1    Agosti, C.G.2    Solomon, F.3
  • 16
    • 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 (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
  • 18
    • 0026091353 scopus 로고
    • Moesin: A member of the protein 4.1-talin-ezrin family of proteins
    • Lankes WT, Furthmayr H (1991): Moesin: A member of the protein 4.1-talin-ezrin family of proteins. Proc Natl Acad Sci USA 88:8297-8301.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8297-8301
    • Lankes, W.T.1    Furthmayr, H.2
  • 19
    • 0027745661 scopus 로고
    • Cloning and sequencing of porcine moesin and radixin cDNA and identification of highly conserved domains
    • Lankes WT, Schwartz-Albiez R, Furthmayr H (1993): Cloning and sequencing of porcine moesin and radixin cDNA and identification of highly conserved domains. Biochimica et Biophysica ACTA 1226:479-482.
    • (1993) Biochimica et Biophysica ACTA , vol.1226 , pp. 479-482
    • Lankes, W.T.1    Schwartz-Albiez, R.2    Furthmayr, H.3
  • 21
    • 0030883688 scopus 로고    scopus 로고
    • Three determinants in ezrin are responsible for cell extension activity
    • Martin M, Roy C, Montcourrier P, Sahuquet A, Mangeat P (1997): Three determinants in ezrin are responsible for cell extension activity. J Cell Biol 8:1543-1557.
    • (1997) J Cell Biol , vol.8 , pp. 1543-1557
    • Martin, M.1    Roy, C.2    Montcourrier, P.3    Sahuquet, A.4    Mangeat, P.5
  • 22
    • 0023854155 scopus 로고
    • Neurofibromatosis 2 (Bilateral Acoustic Neurofibromatosis)
    • Martuza RL, Eldridge R (1988): Neurofibromatosis 2 (Bilateral Acoustic Neurofibromatosis). New Engl J Med 318:685-688.
    • (1988) New Engl J Med , vol.318 , pp. 685-688
    • Martuza, R.L.1    Eldridge, R.2
  • 25
    • 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 (1997): A dual involvement of the amino-terminal domain of ezrin in F- and G-actin binding. J Biol Chem 272:20088-20095.
    • (1997) J Biol Chem , vol.272 , pp. 20088-20095
    • Roy, C.1    Martin, M.2    Mangeat, P.3
  • 26
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley AJ, Hall A (1992): The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 29
    • 0028343217 scopus 로고
    • Mutations of the neurofibromatosis type 2 gene and lack of the gene product in vestibular schwannomas
    • Sainz J, Huynh DP, Figueroa K, Ragge NK, Baser ME, Pulst SM (1994): Mutations of the neurofibromatosis type 2 gene and lack of the gene product in vestibular schwannomas. Human Mol Genet 3:885-891.
    • (1994) Human Mol Genet , vol.3 , pp. 885-891
    • Sainz, J.1    Huynh, D.P.2    Figueroa, K.3    Ragge, N.K.4    Baser, M.E.5    Pulst, S.M.6
  • 30
    • 0029851536 scopus 로고    scopus 로고
    • Expression of the neurofibromatosis 2 tumor suppressor gene product, merlin, in Schwann cells
    • Scherer SS, Gutmann DH (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
  • 33
    • 0029131982 scopus 로고
    • Translocation of activated RhoA from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows
    • Takaishi K, Sasaki T, Kameyama T, Tsukita S, Tsukita S, Takai Y (1995): Translocation of activated RhoA from the cytoplasm to membrane ruffling area, cell-cell adhesion sites and cleavage furrows. Oncogene 11:39-48.
    • (1995) Oncogene , vol.11 , pp. 39-48
    • Takaishi, K.1    Sasaki, T.2    Kameyama, T.3    Tsukita, S.4    Tsukita, S.5    Takai, Y.6
  • 35
    • 0024320199 scopus 로고
    • A new 82 kD barbed end-capping protein (radixin) localized in the cell-to-cell adherens junction: Purification and characterization
    • Tsukita S, Heida Y, 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 108:2369-2382.
    • (1989) J Cell Biol , vol.108 , pp. 2369-2382
    • Tsukita, S.1    Heida, Y.2    Tsukita, S.3
  • 36
    • 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 (1994): ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons. J Cell Biol 126:391-401.
    • (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
  • 38
    • 0030749515 scopus 로고    scopus 로고
    • Mutations in the GAP-related domain impair the ability of neurofibromin to associate with microtubules
    • Xu H-M, Gutmann DH (1997): Mutations in the GAP-related domain impair the ability of neurofibromin to associate with microtubules. Brain Res 759:149-152.
    • (1997) Brain Res , vol.759 , pp. 149-152
    • Xu, H.-M.1    Gutmann, D.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.