메뉴 건너뛰기




Volumn 134, Issue 6, 1996, Pages 1455-1467

Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; VIMENTIN;

EID: 10144233447     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.134.6.1455     Document Type: Article
Times cited : (153)

References (38)
  • 1
    • 0028968743 scopus 로고
    • The importance of importin
    • Adam, S.A. 1995. The importance of importin. Trends Cell Biol. 5:189-191.
    • (1995) Trends Cell Biol. , vol.5 , pp. 189-191
    • Adam, S.A.1
  • 2
    • 0019856909 scopus 로고
    • Visualization of the 10-nm filament vimentin rings in vascular endothelial cells in situ
    • Blose, S.H., and D.I. Meltzer. 1981. Visualization of the 10-nm filament vimentin rings in vascular endothelial cells in situ. Exp. Cell Res. 135:299-309.
    • (1981) Exp. Cell Res. , vol.135 , pp. 299-309
    • Blose, S.H.1    Meltzer, D.I.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0024411243 scopus 로고
    • Sequence requirements for synthetic peptide-mediated translocation to the nucleus
    • Chelsky, D., R. Ralph, and G. Jonak. 1989. Sequence requirements for synthetic peptide-mediated translocation to the nucleus. Mol. Cell. Biol. 9:2487-2492.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2487-2492
    • Chelsky, D.1    Ralph, R.2    Jonak, G.3
  • 5
    • 0019858082 scopus 로고
    • Pathology of cytoskeleton of liver cells: Demonstration of Mallory bodies (alcoholic hyalin) in murine and human hepatocytes by immunofluorescence microscopy using antibodies to cytokeratin polypeptides from hepatocytes
    • Denk, H., W.W. Franke, B. Dragosics, and I. Zeiler. 1981. Pathology of cytoskeleton of liver cells: demonstration of Mallory bodies (alcoholic hyalin) in murine and human hepatocytes by immunofluorescence microscopy using antibodies to cytokeratin polypeptides from hepatocytes. Hepatology. 1:9ff.
    • (1981) Hepatology , vol.1
    • Denk, H.1    Franke, W.W.2    Dragosics, B.3    Zeiler, I.4
  • 6
    • 0028326917 scopus 로고
    • The distribution of plectin, an intermediate filament associated protein, in the adult rat central nervous system
    • Errante, L.D., G. Wiche, and G. Shaw. 1994. The distribution of plectin, an intermediate filament associated protein, in the adult rat central nervous system. J. Neurosci. Res. 37:515-528.
    • (1994) J. Neurosci. Res. , vol.37 , pp. 515-528
    • Errante, L.D.1    Wiche, G.2    Shaw, G.3
  • 7
    • 0023645941 scopus 로고
    • Structure and hydrodynamic properties of plectin molecules
    • Foisner, R., and G. Wiche. 1987. Structure and hydrodynamic properties of plectin molecules. J. Mol. Biol. 198:515-531.
    • (1987) J. Mol. Biol. , vol.198 , pp. 515-531
    • Foisner, R.1    Wiche, G.2
  • 8
    • 0023840076 scopus 로고
    • Cytoskeleton-associated plectin: In situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins
    • Foisner, R., F.E. Leichtfried, H. Herrmann, J.V. Small, D. Lawson, and O. Wiche. 1988. Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins. J. Cell Biol. 106:723-733.
    • (1988) J. Cell Biol. , vol.106 , pp. 723-733
    • Foisner, R.1    Leichtfried, F.E.2    Herrmann, H.3    Small, J.V.4    Lawson, D.5    Wiche, O.6
  • 9
    • 0025797361 scopus 로고
    • Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin
    • Foisner, R., P. Traub, and G. Wiche. 1991. Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin. Proc. Natl. Acad. Sci. USA. 88:3812-3816.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3812-3816
    • Foisner, R.1    Traub, P.2    Wiche, G.3
  • 10
    • 0030020359 scopus 로고    scopus 로고
    • M-phase specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase
    • Foisner, R., N. Malecz, N. Dressel, C. Stadler, and G. Wiche. 1996. M-phase specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase. Mol. Biol. Cell. 7: 273-288.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 273-288
    • Foisner, R.1    Malecz, N.2    Dressel, N.3    Stadler, C.4    Wiche, G.5
  • 13
    • 0022571840 scopus 로고
    • Induction of vimentin synthesis in mouse mycloma cells MPC-11 by 12-0-tetradecanoylphorbol-13-acetate
    • Giese, G., and P. Traub. 1986. Induction of vimentin synthesis in mouse mycloma cells MPC-11 by 12-0-tetradecanoylphorbol-13-acetate. Eur. J. Cell Biol. 40:266-274.
    • (1986) Eur. J. Cell Biol. , vol.40 , pp. 266-274
    • Giese, G.1    Traub, P.2
  • 14
    • 0015847039 scopus 로고
    • A new technique for the assay of infectivity of human adenovirus 5 DNA
    • Graham, F.L., and E. van der Eb. 1973. A new technique for the assay of infectivity of human adenovirus 5 DNA. Virology 52:456-467.
    • (1973) Virology , vol.52 , pp. 456-467
    • Graham, F.L.1    Van Der Eb, E.2
  • 16
    • 0026755162 scopus 로고
    • A comparative structural analysis of desmoplakin, bullous pemphigoid antigen and plectin: Members of a new gene family involved in organization of intermediate filaments
    • Green, K.J., M.L.A. Virata, G.W. Elgart, J.R. Stanley, and D.A.D. Parry. 1992. A comparative structural analysis of desmoplakin, bullous pemphigoid antigen and plectin: members of a new gene family involved in organization of intermediate filaments. Int. J. Biol. Macromol. 14:145-153.
    • (1992) Int. J. Biol. Macromol. , vol.14 , pp. 145-153
    • Green, K.J.1    Virata, M.L.A.2    Elgart, G.W.3    Stanley, J.R.4    Parry, D.A.D.5
  • 17
    • 0023126564 scopus 로고
    • Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin
    • Herrmann, H., and G. Wiche. 1987. Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin. J. Biol. Chem. 262:1320-1325.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1320-1325
    • Herrmann, H.1    Wiche, G.2
  • 18
    • 0021053192 scopus 로고
    • Specific in situ phosphorylation of plectin in detergent-resistant cytoskeletons from cultured chinese hamster ovary cells
    • Herrmann, H., and G. Wiche. 1983. Specific in situ phosphorylation of plectin in detergent-resistant cytoskeletons from cultured chinese hamster ovary cells. J. Biol. Chem. 258:14610-14618.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14610-14618
    • Herrmann, H.1    Wiche, G.2
  • 19
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton, R.M., H.D. Hunt, S.N. Ho, J.K. Pullen, and L.R. Pease. 1989. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene (Amst.). 77:61-68.
    • (1989) Gene (Amst.) , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 20
    • 0029961661 scopus 로고    scopus 로고
    • Human plectin: Organization of the gene, sequence analysis, and chromosome localization (8q24)
    • Liu, C.-g., C. Maercker, M.J. Castañón, R. Hauptmann, and G. Wiche. 1996. Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24). Proc. Natl. Acad. Sci. USA. 93:4278-4283.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4278-4283
    • Liu, C.-G.1    Maercker, C.2    Castañón, M.J.3    Hauptmann, R.4    Wiche, G.5
  • 21
    • 0027715286 scopus 로고
    • Regulated docking of nuclear membrane vesicles to vimentin filaments during mitosis
    • Maison, C., H. Horstmann, and S.D. Georgatos. 1993. Regulated docking of nuclear membrane vesicles to vimentin filaments during mitosis. J. Cell Biol. 123:1491-1505.
    • (1993) J. Cell Biol. , vol.123 , pp. 1491-1505
    • Maison, C.1    Horstmann, H.2    Georgatos, S.D.3
  • 23
    • 0026078249 scopus 로고
    • Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: Identification of a class of bipartite nuclear targeting sequence
    • Robbins, J., S.M. Dilworth, R.A. Laskey, and C. Dingwall. 1991. Two interdependent basic domains in nucleoplasmin nuclear targeting sequence: identification of a class of bipartite nuclear targeting sequence. Cell. 64:615-623.
    • (1991) Cell , vol.64 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 25
    • 0026052915 scopus 로고
    • Human bullous pemphigoid antigen (BPAG1)
    • Sawamura, D., K. Li, M.-L. Chou, and J. Uitto. 1991. Human bullous pemphigoid antigen (BPAG1). J. Biol. Chem. 266:17784-17790.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17784-17790
    • Sawamura, D.1    Li, K.2    Chou, M.-L.3    Uitto, J.4
  • 26
    • 0026442554 scopus 로고
    • Immunolocalization of the intermediate filament-associated protein plectin at focal contacts and actin stress fibers
    • Seifert, G., D. Lawson, and G. Wiche. 1992. Immunolocalization of the intermediate filament-associated protein plectin at focal contacts and actin stress fibers. Eur. J. Cell Biol. 59:138-147.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 138-147
    • Seifert, G.1    Lawson, D.2    Wiche, G.3
  • 27
    • 0000010409 scopus 로고
    • Time-resolved fluorescence of lanthanide probes and applications in biotechnology
    • Soini, E., and T. Lövgren. 1987. Time-resolved fluorescence of lanthanide probes and applications in biotechnology. CRC Crit. Rev. Anal. Chem. 18: 105-154.
    • (1987) CRC Crit. Rev. Anal. Chem. , vol.18 , pp. 105-154
    • Soini, E.1    Lövgren, T.2
  • 28
    • 0027428693 scopus 로고
    • Functional analysis of desmoplakin domains: Specification of the interaction with keratin versus vimentin intermediate filament networks
    • Stappenbeck, T.S., E.A. Bornslaeger, C.M. Corcoran, H.H. Luu, M.L.A. Virata, and K.J. Green. 1993. Functional analysis of desmoplakin domains: specification of the interaction with keratin versus vimentin intermediate filament networks. J. Cell Biol. 123:691-705.
    • (1993) J. Cell Biol. , vol.123 , pp. 691-705
    • Stappenbeck, T.S.1    Bornslaeger, E.A.2    Corcoran, C.M.3    Luu, H.H.4    Virata, M.L.A.5    Green, K.J.6
  • 29
    • 0018852410 scopus 로고
    • Rotary shadowing of extended molecules dried from glycerol
    • Tyler, J.M., and D. Branton. 1980. Rotary shadowing of extended molecules dried from glycerol. J. Ultrastruct. Res. 71:95-102.
    • (1980) J. Ultrastruct. Res. , vol.71 , pp. 95-102
    • Tyler, J.M.1    Branton, D.2
  • 30
    • 0023657934 scopus 로고
    • Plectin from bovine lenses: Chemical properties, structural analysis and initial identification of interaction partners
    • Weitzer, G., and G. Wiche. 1987. Plectin from bovine lenses: chemical properties, structural analysis and initial identification of interaction partners. Eur. J. Biochem. 169:41-52.
    • (1987) Eur. J. Biochem. , vol.169 , pp. 41-52
    • Weitzer, G.1    Wiche, G.2
  • 31
    • 0020329482 scopus 로고
    • Plectin: A high-molecular-weight cytoskeletal polypeptide component that copurifies with intermediate filaments of the vimentin type
    • Wiche, G., H. Herrmann, F. Leichtfried, and R. Pytela. 1982. Plectin: a high-molecular-weight cytoskeletal polypeptide component that copurifies with intermediate filaments of the vimentin type. Cold Spring Harbor Symp. Quant. Biol. 46:475-482.
    • (1982) Cold Spring Harbor Symp. Quant. Biol. , vol.46 , pp. 475-482
    • Wiche, G.1    Herrmann, H.2    Leichtfried, F.3    Pytela, R.4
  • 32
  • 33
    • 0021749865 scopus 로고
    • Identification of plectin in different human cell types and immunolocalization at epithelial basal cell surface membranes
    • Wiche, G., R. Krepler, U. Artlieb, R. Pytela, and W. Aberer. 1984. Identification of plectin in different human cell types and immunolocalization at epithelial basal cell surface membranes. Exp. Cell Res. 155:43-49.
    • (1984) Exp. Cell Res. , vol.155 , pp. 43-49
    • Wiche, G.1    Krepler, R.2    Artlieb, U.3    Pytela, R.4    Aberer, W.5
  • 34
    • 0026014584 scopus 로고
    • Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central α-helical coiled coil
    • Wiche, G., B. Becker, K. Luber, G. Weitzer, M. J. Castañón, R. Hauptmann, C. Stratowa, and M. Stewart. 1991. Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central α-helical coiled coil. J. Cell Biol. 114:83-99.
    • (1991) J. Cell Biol. , vol.114 , pp. 83-99
    • Wiche, G.1    Becker, B.2    Luber, K.3    Weitzer, G.4    Castañón, M.J.5    Hauptmann, R.6    Stratowa, C.7    Stewart, M.8
  • 35
    • 0027159977 scopus 로고
    • Expression of plectin mutant cDNA in cultured cells indicates a role of C-terminal domain in intermediate filament association
    • Wiche, G., D. Gromov, A. Donovan, M. J. Castañón, and E. Fuchs. 1993. Expression of plectin mutant cDNA in cultured cells indicates a role of C-terminal domain in intermediate filament association. J. Cell Biol. 121:607-619.
    • (1993) J. Cell Biol. , vol.121 , pp. 607-619
    • Wiche, G.1    Gromov, D.2    Donovan, A.3    Castañón, M.J.4    Fuchs, E.5
  • 36
    • 0029982832 scopus 로고    scopus 로고
    • Perinuclear distribution of plectin characterizes visceral epithelial cells of rat glomeruli
    • Yaoita, E., G. Wiche, T. Yamamoto, K. Kawasaki, and I. Kihara. 1996. Perinuclear distribution of plectin characterizes visceral epithelial cells of rat glomeruli. Am. J. Pathol. 149:319-328.
    • (1996) Am. J. Pathol. , vol.149 , pp. 319-328
    • Yaoita, E.1    Wiche, G.2    Yamamoto, T.3    Kawasaki, K.4    Kihara, I.5
  • 37
    • 0019158157 scopus 로고
    • A survey of transformation markers in differentiating epidermal cell lines in culture
    • Yuspa, S. H., P. Hawley-Nelson, B. Koehler, and J.R. Stanley. 1980. A survey of transformation markers in differentiating epidermal cell lines in culture. Cancer Res. 40:4694-4703.
    • (1980) Cancer Res. , vol.40 , pp. 4694-4703
    • Yuspa, S.H.1    Hawley-Nelson, P.2    Koehler, B.3    Stanley, J.R.4
  • 38
    • 0021828068 scopus 로고
    • Morphological integrity of single adult cardiac myocytes isolated by collangenase treatment: Immunolocalization of tubulin, microtubule-associated proteins 1 and 2, plectin, vimentin, and vinculin
    • Zernig, G., and G. Wiche. 1985. Morphological integrity of single adult cardiac myocytes isolated by collangenase treatment: immunolocalization of tubulin, microtubule-associated proteins 1 and 2, plectin, vimentin, and vinculin. Eur. J. Cell Biol. 38:113-122.
    • (1985) Eur. J. Cell Biol. , vol.38 , pp. 113-122
    • Zernig, G.1    Wiche, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.