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Volumn 97, Issue 3, 2006, Pages 167-174

Regulatory mechanisms and functions of intermediate filaments: A study using site- and phosphorylation state-specific antibodies

Author keywords

[No Author keywords available]

Indexed keywords

AURORA B KINASE; CYCLIN DEPENDENT KINASE 1; DESMIN; GLIAL FIBRILLARY ACIDIC PROTEIN; INTERMEDIATE FILAMENT PROTEIN; KERATIN; KERATIN 18; KERATIN 8; PHOSPHOSPECIFIC ANTIBODY; POLO LIKE KINASE 1; RHO KINASE; SERINE; TUMOR NECROSIS FACTOR RECEPTOR 1 ASSOCIATED DEATH DOMAIN PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR; UNCLASSIFIED DRUG; VIMENTIN;

EID: 33646004279     PISSN: 13479032     EISSN: 13497006     Source Type: Journal    
DOI: 10.1111/j.1349-7006.2006.00161.x     Document Type: Review
Times cited : (137)

References (69)
  • 1
    • 0037282536 scopus 로고    scopus 로고
    • Functional complexity of intermediate filament cytoskeletons: From structure to assembly to gene ablation
    • Herrmann H, Hesse M, Reichenzeller M, Aebi U, Magin TM. Functional complexity of intermediate filament cytoskeletons: From structure to assembly to gene ablation. Int Rev Cytol 2003; 223: 83-175.
    • (2003) Int Rev Cytol , vol.223 , pp. 83-175
    • Herrmann, H.1    Hesse, M.2    Reichenzeller, M.3    Aebi, U.4    Magin, T.M.5
  • 2
    • 4143134431 scopus 로고    scopus 로고
    • Cytoplasmic intermediate filaments revealed as dynamic and multipurpose scaffolds
    • Coulombe PA, Wong P. Cytoplasmic intermediate filaments revealed as dynamic and multipurpose scaffolds. Nat Cell Biol 2004; 6: 699-706.
    • (2004) Nat Cell Biol , vol.6 , pp. 699-706
    • Coulombe, P.A.1    Wong, P.2
  • 3
    • 0032559341 scopus 로고    scopus 로고
    • A structural scaffolding of intermediate filaments in health and disease
    • Fuchs E, Cleveland DW. A structural scaffolding of intermediate filaments in health and disease. Science 1998; 279: 514-19.
    • (1998) Science , vol.279 , pp. 514-519
    • Fuchs, E.1    Cleveland, D.W.2
  • 4
    • 6344273968 scopus 로고    scopus 로고
    • Intermediate filament proteins and their associated diseases
    • Omary MB, Coulombe PA, McLean WHI. Intermediate filament proteins and their associated diseases. N Engl J Med 2004; 351: 2087-100.
    • (2004) N Engl J Med , vol.351 , pp. 2087-2100
    • Omary, M.B.1    Coulombe, P.A.2    McLean, W.H.I.3
  • 6
    • 0032233043 scopus 로고    scopus 로고
    • Cytokeratins as markers of differentiation in the diagnosis of epithelial tumors
    • Moll R. Cytokeratins as markers of differentiation in the diagnosis of epithelial tumors. Subcell Biochem 1998; 31: 205-62.
    • (1998) Subcell Biochem , vol.31 , pp. 205-262
    • Moll, R.1
  • 8
    • 0023239962 scopus 로고
    • Site-specific phosphorylation induces disassembly of vimentin filaments in vitro
    • Inagaki M, Nishi Y, Nishizawa K, Matsuyama M, Sato C. Site-specific phosphorylation induces disassembly of vimentin filaments in vitro. Nature 1987; 328: 649-52.
    • (1987) Nature , vol.328 , pp. 649-652
    • Inagaki, M.1    Nishi, Y.2    Nishizawa, K.3    Matsuyama, M.4    Sato, C.5
  • 9
    • 0001481064 scopus 로고    scopus 로고
    • Dynamic property of intermediate filaments: Regulation by phosphorylation
    • Inagaki M, Matsuoka Y, Tsujimura K et al. Dynamic property of intermediate filaments: Regulation by phosphorylation. Bioessays 1996; 18: 481-7.
    • (1996) Bioessays , vol.18 , pp. 481-487
    • Inagaki, M.1    Matsuoka, Y.2    Tsujimura, K.3
  • 10
    • 3543113113 scopus 로고    scopus 로고
    • Intermediate filaments mediate cytoskeletal crosstalk
    • Chang L, Goldman RD. Intermediate filaments mediate cytoskeletal crosstalk. Nat Rev Mol Cell Biol 2004; 5: 601-13.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 601-613
    • Chang, L.1    Goldman, R.D.2
  • 11
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter M, Nakagawa J, Dorée M, Labbé JC, Nigg EA. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell 1990; 61: 591-602.
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Dorée, M.3    Labbé, J.C.4    Nigg, E.A.5
  • 13
    • 0028131997 scopus 로고
    • Spatiotemporal distribution of protein kinase and phosphatase activities
    • Inagaki N, Ito M, Nakano T, Inagaki M. Spatiotemporal distribution of protein kinase and phosphatase activities. Trends Biochem Sci 1994; 19: 448-52.
    • (1994) Trends Biochem Sci , vol.19 , pp. 448-452
    • Inagaki, N.1    Ito, M.2    Nakano, T.3    Inagaki, M.4
  • 14
    • 0031002831 scopus 로고    scopus 로고
    • Phosphorylation-dependent control of structures of intermediate filaments: A novel approach using site- and phosphorylation state-specific antibodies
    • Inagaki M, Inagaki N, Takahashi T, Takai Y. Phosphorylation-dependent control of structures of intermediate filaments: A novel approach using site- and phosphorylation state-specific antibodies. J Biochem 1997; 121: 407-14.
    • (1997) J Biochem , vol.121 , pp. 407-414
    • Inagaki, M.1    Inagaki, N.2    Takahashi, T.3    Takai, Y.4
  • 15
    • 0034866917 scopus 로고    scopus 로고
    • A decade of site- and phosphorylation state-specific antibodies: Recent advances in studies of spatiotemporal protein phosphorylation
    • Nagata K, Izawa I, Inagaki M. A decade of site- and phosphorylation state-specific antibodies: Recent advances in studies of spatiotemporal protein phosphorylation. Genes Cells 2001; 6: 653-64.
    • (2001) Genes Cells , vol.6 , pp. 653-664
    • Nagata, K.1    Izawa, I.2    Inagaki, M.3
  • 16
    • 0025801842 scopus 로고
    • Specific localization of phospho-intermediate filament protein in the constricted area of dividing cells
    • Nishizawa K, Yano T, Shibata M et al. Specific localization of phospho-intermediate filament protein in the constricted area of dividing cells. J Biol Chem 1991; 266: 3074 - 9.
    • (1991) J Biol Chem , vol.266
    • Nishizawa, K.1    Yano, T.2    Shibata, M.3
  • 17
    • 0025804191 scopus 로고
    • A monoclonal antibody to the phosphorylated form of glial fibrillary acidic protein: Application to a non-radioactive method for measuring protein kinase activities
    • Yano T, Taura C, Shibata M et al. A monoclonal antibody to the phosphorylated form of glial fibrillary acidic protein: Application to a non-radioactive method for measuring protein kinase activities. Biochem Biophys Res Commun 1991; 175: 1144-51.
    • (1991) Biochem Biophys Res Commun , vol.175 , pp. 1144-1151
    • Yano, T.1    Taura, C.2    Shibata, M.3
  • 18
    • 0026734350 scopus 로고
    • Two different protein kinases act on a different time schedule as glial filament kinase during mitosis
    • Matsuoka Y, Nishizawa K, Yano T et al. Two different protein kinases act on a different time schedule as glial filament kinase during mitosis. EMBO J 1992; 11: 2895-902.
    • (1992) EMBO J , vol.11 , pp. 2895-2902
    • Matsuoka, Y.1    Nishizawa, K.2    Yano, T.3
  • 19
    • 0030063171 scopus 로고    scopus 로고
    • Detection of protein kinase activity specifically activated at metaphase-anaphase transition
    • Sekimata M, Tsujimura K, Tanaka J, Takeuchi Y, Inagaki N, Inagaki M. Detection of protein kinase activity specifically activated at metaphase-anaphase transition. J Cell Biol 1996; 132: 635-41.
    • (1996) J Cell Biol , vol.132 , pp. 635-641
    • Sekimata, M.1    Tsujimura, K.2    Tanaka, J.3    Takeuchi, Y.4    Inagaki, N.5    Inagaki, M.6
  • 20
    • 0030929849 scopus 로고    scopus 로고
    • Phosphorylation of glial fibrillary acidic protein at the same sites by cleavage furrow kinase and Rho-associated kinase
    • Kosako H, Amano M, Yanagida M et al. Phosphorylation of glial fibrillary acidic protein at the same sites by cleavage furrow kinase and Rho-associated kinase. J Biol Chem 1997; 272: 10 333-6.
    • (1997) J Biol Chem , vol.272 , Issue.10 , pp. 333-336
    • Kosako, H.1    Amano, M.2    Yanagida, M.3
  • 21
    • 0032496146 scopus 로고    scopus 로고
    • Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis
    • Goto H, Kosako H, Tanabe K et al. Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis. J Biol Chem 1998; 273: 11 728-36.
    • (1998) J Biol Chem , vol.273 , Issue.11 , pp. 728-736
    • Goto, H.1    Kosako, H.2    Tanabe, K.3
  • 22
    • 0032583123 scopus 로고    scopus 로고
    • Roles of Rho-associated kinase in cytokinesis: Mutations in Rho-associated kinase phosphorylation sites impair cytokinetic segregation of glial filaments
    • Yasui Y, Amano M, Nagata K et al. Roles of Rho-associated kinase in cytokinesis: Mutations in Rho-associated kinase phosphorylation sites impair cytokinetic segregation of glial filaments. J Cell Biol 1998; 143: 1249-58.
    • (1998) J Cell Biol , vol.143 , pp. 1249-1258
    • Yasui, Y.1    Amano, M.2    Nagata, K.3
  • 23
    • 0033520998 scopus 로고    scopus 로고
    • Balance between activities of Rho-kinase and type 1 protein phosphatase modulates turnover of phosphorylation and dynamics of desmin/vimentin filaments
    • Inada H, Togashi H, Nakamura Y, Kaibuchi K, Nagata K, Inagaki M. Balance between activities of Rho-kinase and type 1 protein phosphatase modulates turnover of phosphorylation and dynamics of desmin/vimentin filaments. J Biol Chem 1999; 274: 34 932-9.
    • (1999) J Biol Chem , vol.274 , Issue.34 , pp. 932-939
    • Inada, H.1    Togashi, H.2    Nakamura, Y.3    Kaibuchi, K.4    Nagata, K.5    Inagaki, M.6
  • 24
    • 0037424487 scopus 로고    scopus 로고
    • Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process
    • Goto H, Yasui Y, Kawajiri A et al. Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process. J Biol Chem 2003; 278: 8526-30.
    • (2003) J Biol Chem , vol.278 , pp. 8526-8530
    • Goto, H.1    Yasui, Y.2    Kawajiri, A.3
  • 25
    • 0038371015 scopus 로고    scopus 로고
    • Functional significance of the specific sites phosphorylated in desmin at cleavage furrow: Aurora-B may phosphorylate and regulate type III intermediate filaments during cytokinesis coordinately with Rho-kinase
    • Kawajiri A, Yasui Y, Goto H et al. Functional significance of the specific sites phosphorylated in desmin at cleavage furrow: Aurora-B may phosphorylate and regulate type III intermediate filaments during cytokinesis coordinately with Rho-kinase. Mol Biol Cell 2003; 14: 1489-500.
    • (2003) Mol Biol Cell , vol.14 , pp. 1489-1500
    • Kawajiri, A.1    Yasui, Y.2    Goto, H.3
  • 26
    • 14244251720 scopus 로고    scopus 로고
    • Aurora-B and Rho-kinase/ROCK, the two cleavage furrow kinases, independently regulate the progression of cytokinesis: Possible existence of a novel cleavage furrow kinase phosphorylates ezrin/radixin/ moesin (ERM)
    • Yokoyama T, Goto H, Izawa I, Mizutani H, Inagaki M. Aurora-B and Rho-kinase/ROCK, the two cleavage furrow kinases, independently regulate the progression of cytokinesis: Possible existence of a novel cleavage furrow kinase phosphorylates ezrin/radixin/moesin (ERM). Genes Cells 2005; 10: 127-37.
    • (2005) Genes Cells , vol.10 , pp. 127-137
    • Yokoyama, T.1    Goto, H.2    Izawa, I.3    Mizutani, H.4    Inagaki, M.5
  • 27
    • 27744497121 scopus 로고    scopus 로고
    • Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis
    • Yamaguchi T, Goto H, Yokoyama T et al. Phosphorylation by Cdk1 induces Plk1-mediated vimentin phosphorylation during mitosis. J Cell Biol 2005; 171: 431-6.
    • (2005) J Cell Biol , vol.171 , pp. 431-436
    • Yamaguchi, T.1    Goto, H.2    Yokoyama, T.3
  • 28
    • 0020328231 scopus 로고
    • An alteration in the phosphorylation of vimentin-type intermediate filaments is associated with mitosis in cultured mammalian cells
    • Evans RM, Fink LM. An alteration in the phosphorylation of vimentin-type intermediate filaments is associated with mitosis in cultured mammalian cells. Cell 1982; 29: 43-52.
    • (1982) Cell , vol.29 , pp. 43-52
    • Evans, R.M.1    Fink, L.M.2
  • 29
    • 0021044471 scopus 로고
    • Phosphorylation of keratin and vimentin polypeptides in normal and transformed mitotic human epithelial amnion cells: Behavior of keratin and vimentin filaments during mitosis
    • Celis JE, Lasen PM, Fey SJ, Celis A. Phosphorylation of keratin and vimentin polypeptides in normal and transformed mitotic human epithelial amnion cells: Behavior of keratin and vimentin filaments during mitosis. J Cell Biol 1983; 97: 1429-34.
    • (1983) J Cell Biol , vol.97 , pp. 1429-1434
    • Celis, J.E.1    Lasen, P.M.2    Fey, S.J.3    Celis, A.4
  • 30
    • 0023899197 scopus 로고
    • Cyclic AMP-dependent protein kinase-induced vimentin filament disassembly involves modification of N-terminal of intermediate filaments subunits
    • Evans RM. Cyclic AMP-dependent protein kinase-induced vimentin filament disassembly involves modification of N-terminal of intermediate filaments subunits. FEBS Lett 1988; 234: 73-8.
    • (1988) FEBS Lett , vol.234 , pp. 73-78
    • Evans, R.M.1
  • 31
    • 0024512061 scopus 로고
    • Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure
    • Ando S, Tanabe K, Gonda Y, Sato C, Inagaki M. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. Biochemistry 1989; 28: 2974-9.
    • (1989) Biochemistry , vol.28 , pp. 2974-2979
    • Ando, S.1    Tanabe, K.2    Gonda, Y.3    Sato, C.4    Inagaki, M.5
  • 32
    • 0025130177 scopus 로고
    • Intermediate filament reorganization during mitosis is mediated by p34cdc2 phosphorylation of vimentin
    • Chou YH, Bischoff JR, Beach D, Goldman RD. Intermediate filament reorganization during mitosis is mediated by p34cdc2 phosphorylation of vimentin. Cell 1990; 62: 1063-71.
    • (1990) Cell , vol.62 , pp. 1063-1071
    • Chou, Y.H.1    Bischoff, J.R.2    Beach, D.3    Goldman, R.D.4
  • 33
    • 0026612454 scopus 로고
    • SUC1 suppresses the catalytic function of p34 cdc2 kinase for intermediate filament proteins, in vitro
    • SUC1 suppresses the catalytic function of p34 cdc2 kinase for intermediate filament proteins, in vitro. J Biol Chem 1992; 267: 20 937-42.
    • (1992) J Biol Chem , vol.267 , Issue.20 , pp. 937-942
    • Kusubata, M.1    Tokui, T.2    Matsuoka, Y.3
  • 34
    • 0025248451 scopus 로고
    • Phosphorylation sites linked to glial filament disassembly in vitro locate in a non-α-helical head domain
    • Inagaki M, Gonda Y, Nishizawa K et al. Phosphorylation sites linked to glial filament disassembly in vitro locate in a non-α-helical head domain. J Biol Chem 1990; 265: 4722-9.
    • (1990) J Biol Chem , vol.265 , pp. 4722-4729
    • Inagaki, M.1    Gonda, Y.2    Nishizawa, K.3
  • 35
    • 0023928876 scopus 로고
    • Intermediate filament reconstitution in vitro. The role of phosphorylation on the assembly-disassembly of desmin
    • Inagaki M, Gonda Y, Matsuyama M, Nishizawa K, Nishi Y, Sato C. Intermediate filament reconstitution in vitro. The role of phosphorylation on the assembly-disassembly of desmin. J Biol Chem 1988; 263: 5970-8.
    • (1988) J Biol Chem , vol.263 , pp. 5970-5978
    • Inagaki, M.1    Gonda, Y.2    Matsuyama, M.3    Nishizawa, K.4    Nishi, Y.5    Sato, C.6
  • 36
    • 0025906619 scopus 로고
    • Phosphorylation of keratin intermediate filaments by protein kinase C, by calmodulin-dependent protein kinase and by cAMP-dependent protein kinase
    • Yano T, Tokui T, Nishi Y et al. Phosphorylation of keratin intermediate filaments by protein kinase C, by calmodulin-dependent protein kinase and by cAMP-dependent protein kinase. Eur J Biochem 1991; 197: 281-90.
    • (1991) Eur J Biochem , vol.197 , pp. 281-290
    • Yano, T.1    Tokui, T.2    Nishi, Y.3
  • 37
    • 0024473081 scopus 로고
    • 2+-dependent deimination-induced disassembly of intermediate filaments involves specific modification of the amino-terminal head domain
    • 2+ -dependent deimination-induced disassembly of intermediate filaments involves specific modification of the amino-terminal head domain. J Biol Chem 1989; 264: 18 119-27.
    • (1989) J Biol Chem , vol.264 , Issue.18 , pp. 119-127
    • Inagaki, M.1    Takahara, H.2    Nishi, Y.3    Sugawara, K.4    Sato, C.5
  • 39
    • 0004122394 scopus 로고
    • Specific antibodies to phospho-glial fibrillary acidic protein: Production and characterization
    • Yano T, Taura C, Hirono Y et al. Specific antibodies to phospho-glial fibrillary acidic protein: Production and characterization. Cell Struct Funct 1990; 15: 497.
    • (1990) Cell Struct Funct , vol.15 , pp. 497
    • Yano, T.1    Taura, C.2    Hirono, Y.3
  • 40
    • 0026693966 scopus 로고
    • Animal cell cycles and their control
    • Norbury C, Nurse P. Animal cell cycles and their control. Annu Rev Biochem 1992; 61: 441-70.
    • (1992) Annu Rev Biochem , vol.61 , pp. 441-470
    • Norbury, C.1    Nurse, P.2
  • 42
    • 0025895855 scopus 로고
    • The regulation of intermediate filament reorganization in mitosis: p34cdc2 phosphorylates vimentin at a unique N-terminal site
    • Chou YH, Ngai KL, Goldman R. The regulation of intermediate filament reorganization in mitosis: P34cdc2 phosphorylates vimentin at a unique N-terminal site. J Biol Chem 1991; 266: 7325 - 8.
    • (1991) J Biol Chem , vol.266 , pp. 7325-7328
    • Chou, Y.H.1    Ngai, K.L.2    Goldman, R.3
  • 43
    • 0028151022 scopus 로고
    • Visualization and function of vimentin phosphorylation by cdc2 kinase during mitosis
    • Tsujimura K, Ogawara M, Takeuchi Y, Imajoh-Ohmi S, Ha MH, Inagaki M. Visualization and function of vimentin phosphorylation by cdc2 kinase during mitosis. J Biol Chem 1994; 269: 31 097-106.
    • (1994) J Biol Chem , vol.269 , Issue.31 , pp. 097-106
    • Tsujimura, K.1    Ogawara, M.2    Takeuchi, Y.3    Imajoh-Ohmi, S.4    Ha, M.H.5    Inagaki, M.6
  • 44
    • 0032860424 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton and cell adhesion by Rho family GTPases in mammalian cells
    • Kaibuchi K, Kuroda S, Amano M. Regulation of the cytoskeleton and cell adhesion by Rho family GTPases in mammalian cells. Annu Rev Biochem 1999; 68: 459-86.
    • (1999) Annu Rev Biochem , vol.68 , pp. 459-486
    • Kaibuchi, K.1    Kuroda, S.2    Amano, M.3
  • 45
    • 0033614371 scopus 로고    scopus 로고
    • Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: Cleavage furrow-specific phosphorylation of intermediate filaments
    • Kosako H, Goto H, Yanagida M et al. Specific accumulation of Rho-associated kinase at the cleavage furrow during cytokinesis: cleavage furrow-specific phosphorylation of intermediate filaments. Oncogene 1999; 18: 2783-8.
    • (1999) Oncogene , vol.18 , pp. 2783-2788
    • Kosako, H.1    Goto, H.2    Yanagida, M.3
  • 46
    • 0035942501 scopus 로고    scopus 로고
    • Protein kinases required for segregation of vimentin filaments in mitotic process
    • Yasui Y, Goto H, Matsui S et al. Protein kinases required for segregation of vimentin filaments in mitotic process. Oncogene 2001; 20: 2868-76.
    • (2001) Oncogene , vol.20 , pp. 2868-2876
    • Yasui, Y.1    Goto, H.2    Matsui, S.3
  • 47
  • 48
    • 11144354860 scopus 로고    scopus 로고
    • Autophosphorylation of a newly identified site of Aurora-B is indispensable for cytokinesis
    • Yasui Y, Urano T, Kawajiri A et al. Autophosphorylation of a newly identified site of Aurora-B is indispensable for cytokinesis. J Biol Chem 2004; 279: 12 997-3003.
    • (2004) J Biol Chem , vol.279 , Issue.12 , pp. 997-3003
    • Yasui, Y.1    Urano, T.2    Kawajiri, A.3
  • 49
    • 25844475838 scopus 로고    scopus 로고
    • On the road to cancer: Aneuploidy and the mitotic checkpoint
    • Kops GJPL, Weaver BAA, Cleveland DW. On the road to cancer: Aneuploidy and the mitotic checkpoint. Nat Rev Cancer 2005; 5: 773-85.
    • (2005) Nat Rev Cancer , vol.5 , pp. 773-785
    • Kops, G.J.P.L.1    Weaver, B.A.A.2    Cleveland, D.W.3
  • 50
    • 0347762556 scopus 로고    scopus 로고
    • From polyploidy to aneuploidy, genome instability and cancer
    • Storchova Z, Pellman D. From polyploidy to aneuploidy, genome instability and cancer. Nat Rev Mol Cell Biol 2004; 5: 45-54.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 45-54
    • Storchova, Z.1    Pellman, D.2
  • 51
    • 0036468732 scopus 로고    scopus 로고
    • 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments
    • Coulombe PA, Omary MB. 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments. Curr Opin Cell Biol 2002; 14: 110-22.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 110-122
    • Coulombe, P.A.1    Omary, M.B.2
  • 52
    • 0031663054 scopus 로고    scopus 로고
    • Role of plectin in cytoskeleton organization and dynamics
    • Wiche G. Role of plectin in cytoskeleton organization and dynamics. J Cell Sci 1998; 111: 2477-86.
    • (1998) J Cell Sci , vol.111 , pp. 2477-2486
    • Wiche, G.1
  • 53
    • 0034568948 scopus 로고    scopus 로고
    • Are desmosomes more than tethers for intermediate filaments?
    • Green KJ, Gaudry CA. Are desmosomes more than tethers for intermediate filaments? Nat Rev Mol Cell Biol 2000; 1: 208-16.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 208-216
    • Green, K.J.1    Gaudry, C.A.2
  • 54
  • 55
    • 0027227464 scopus 로고
    • Mid-gestational lethality in mice lacking keratin 8
    • Baribault H, Price J, Miyai K, Oshima RG. Mid-gestational lethality in mice lacking keratin 8. Genes Dev 1993; 7: 1191-202.
    • (1993) Genes Dev , vol.7 , pp. 1191-1202
    • Baribault, H.1    Price, J.2    Miyai, K.3    Oshima, R.G.4
  • 56
    • 0028607055 scopus 로고
    • Colorectal hyperplasia and inflammation in keratin 8-deficient FVB/N mice
    • Baribault H, Penner J, Iozzo RV, Wilson-Heiner M. Colorectal hyperplasia and inflammation in keratin 8-deficient FVB/N mice. Genes Dev 1994; 8: 2964-73.
    • (1994) Genes Dev , vol.8 , pp. 2964-2973
    • Baribault, H.1    Penner, J.2    Iozzo, R.V.3    Wilson-Heiner, M.4
  • 57
    • 0033843879 scopus 로고    scopus 로고
    • Cytokeratin 8 protects from hepatotoxicity, and its ratio to cytokeratin 18 determines the ability of hepatocytes to form Mallory bodies
    • Zatloukal K, Stumptner C, Lehner M et al. Cytokeratin 8 protects from hepatotoxicity, and its ratio to cytokeratin 18 determines the ability of hepatocytes to form Mallory bodies. Am J Pathol 2000; 156: 1263-74.
    • (2000) Am J Pathol , vol.156 , pp. 1263-1274
    • Zatloukal, K.1    Stumptner, C.2    Lehner, M.3
  • 58
    • 2642684550 scopus 로고    scopus 로고
    • Lessons from keratin 18 knockout mice: Formation of novel keratin filaments, secondary loss of keratin 7 and accumulation of liver-specific keratin 8-positive aggregates
    • Magin TM, Schröder R, Leitgeb S et al. Lessons from keratin 18 knockout mice: Formation of novel keratin filaments, secondary loss of keratin 7 and accumulation of liver-specific keratin 8-positive aggregates. J Cell Biol 1998; 140: 1441-51.
    • (1998) J Cell Biol , vol.140 , pp. 1441-1451
    • Magin, T.M.1    Schröder, R.2    Leitgeb, S.3
  • 59
    • 0042090843 scopus 로고    scopus 로고
    • The quest for the function of simple epithelial keratins
    • Owens DW, Lane EB. The quest for the function of simple epithelial keratins. Bioessays 2003; 25: 748-58.
    • (2003) Bioessays , vol.25 , pp. 748-758
    • Owens, D.W.1    Lane, E.B.2
  • 60
    • 0034599872 scopus 로고    scopus 로고
    • Keratin-dependent, epithelial resistance to tumor necrosis factor-induced apoptosis
    • Caulin C, Ware CF, Magin TM, Oshima RG. Keratin-dependent, epithelial resistance to tumor necrosis factor-induced apoptosis. J Cell Biol 2000; 149: 17-22.
    • (2000) J Cell Biol , vol.149 , pp. 17-22
    • Caulin, C.1    Ware, C.F.2    Magin, T.M.3    Oshima, R.G.4
  • 61
    • 0036097410 scopus 로고    scopus 로고
    • Apoptosis and keratin intermediate filaments
    • Oshima RG. Apoptosis and keratin intermediate filaments. Cell Death Differ 2002; 9: 486-92.
    • (2002) Cell Death Differ , vol.9 , pp. 486-492
    • Oshima, R.G.1
  • 62
    • 0035851916 scopus 로고    scopus 로고
    • Keratin attenuates tumor necrosis factor-induced cytotoxicity through association with TRADD
    • Inada H, Izawa I, Nishizawa M et al. Keratin attenuates tumor necrosis factor-induced cytotoxicity through association with TRADD. J Cell Biol 2001; 155: 415-25.
    • (2001) J Cell Biol , vol.155 , pp. 415-425
    • Inada, H.1    Izawa, I.2    Nishizawa, M.3
  • 63
    • 1342346544 scopus 로고    scopus 로고
    • An autocrine/paracrine loop linking keratin 14 aggregates to tumor necrosis factor α-mediated cytotoxicity in a keratinocyte model of epidermolysis bullosa simplex
    • Yoneda K, Furukawa T, Zheng YJ et al. An autocrine/paracrine loop linking keratin 14 aggregates to tumor necrosis factor α-mediated cytotoxicity in a keratinocyte model of epidermolysis bullosa simplex. J Biol Chem 2004; 279: 7296-303.
    • (2004) J Biol Chem , vol.279 , pp. 7296-7303
    • Yoneda, K.1    Furukawa, T.2    Zheng, Y.J.3
  • 64
    • 0035921430 scopus 로고    scopus 로고
    • Simple epithelium keratins 8 and 18 provide resistance to Fas-mediated apoptosis The protection occurs through a receptor-targeting modulation
    • Gilbert S, Loranger A, Daigle N, Marceau N. Simple epithelium keratins 8 and 18 provide resistance to Fas-mediated apoptosis. The protection occurs through a receptor-targeting modulation. J Cell Biol 2001; 154: 763-73.
    • (2001) J Cell Biol , vol.154 , pp. 763-773
    • Gilbert, S.1    Loranger, A.2    Daigle, N.3    Marceau, N.4
  • 65
    • 0037119943 scopus 로고    scopus 로고
    • DEDD regulates degradation of intermediate filaments during apoptosis
    • Lee JC, Schickling O, Stegh AH et al. DEDD regulates degradation of intermediate filaments during apoptosis. J Cell Biol 2002; 158: 1051-66.
    • (2002) J Cell Biol , vol.158 , pp. 1051-1066
    • Lee, J.C.1    Schickling, O.2    Stegh, A.H.3
  • 66
    • 1542289716 scopus 로고    scopus 로고
    • Intermediate filaments control the intracellular distribution of caspases during apoptosis
    • Dinsdale D, Lee JC, Dewson G, Cohen GM, Peter ME. Intermediate filaments control the intracellular distribution of caspases during apoptosis. Am J Pathol 2004; 164: 395-407.
    • (2004) Am J Pathol , vol.164 , pp. 395-407
    • Dinsdale, D.1    Lee, J.C.2    Dewson, G.3    Cohen, G.M.4    Peter, M.E.5
  • 67
    • 3543009577 scopus 로고    scopus 로고
    • Keratins modulate c-FLIP/extracellular signal-regulated kinase 1 and 2 antiapoptotic signaling in simple epithelial cells
    • Gilbert S, Loranger A, Marceau N. Keratins modulate c-FLIP/extracellular signal-regulated kinase 1 and 2 antiapoptotic signaling in simple epithelial cells. Mol Cell Biol 2004; 24: 7072-81.
    • (2004) Mol Cell Biol , vol.24 , pp. 7072-7081
    • Gilbert, S.1    Loranger, A.2    Marceau, N.3
  • 68
    • 0034602272 scopus 로고    scopus 로고
    • Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein
    • Izawa I, Nishizawa M, Ohtakara K, Ohtsuka K, Inada H, Inagaki M. Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein. J Biol Chem 2000; 275: 34 521-7.
    • (2000) J Biol Chem , vol.275 , Issue.34 , pp. 521-527
    • Izawa, I.1    Nishizawa, M.2    Ohtakara, K.3    Ohtsuka, K.4    Inada, H.5    Inagaki, M.6
  • 69
    • 16844380974 scopus 로고    scopus 로고
    • Identification of trichoplein, a novel keratin filament-binding protein
    • Nishizawa M, Izawa I, Inoko A et al. Identification of trichoplein, a novel keratin filament-binding protein. J Cell Sci 2005; 118: 1081 - 90. 1081-90.
    • (2005) J Cell Sci , vol.118 , pp. 1081-1090
    • Nishizawa, M.1    Izawa, I.2    Inoko, A.3


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