메뉴 건너뛰기




Volumn 282, Issue 3, 1998, Pages 601-617

Assembly and architecture of invertebrate cytoplasmic intermediate filaments reconcile features of vertebrate cytoplasmic and nuclear lamin-type intermediate filaments

Author keywords

Filament assembly; Intermediate filaments (IFs); Nuclear lamins; Protostomic invertebrate IFs; Structural biology

Indexed keywords

AMINO ACID; INTERMEDIATE FILAMENT PROTEIN; LAMIN;

EID: 0032566613     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1995     Document Type: Article
Times cited : (51)

References (40)
  • 1
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi, U., Cohn, J., Buhle, L. & Gerace, L. (1986). The nuclear lamina is a meshwork of intermediate-type filaments. Nature, 323, 560-564.
    • (1986) Nature , vol.323 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, L.3    Gerace, L.4
  • 2
    • 0022760931 scopus 로고
    • Amino acid sequence and gene organization of cytokeratin no. 19, an exceptional tailless intermediate filament protein: Change in protein conformation corresponds to presence of a landmark intron
    • Bader, B. L., Magin, T. M., Hatzfeld, M. & Franke, W. W. (1986). Amino acid sequence and gene organization of cytokeratin no. 19, an exceptional tailless intermediate filament protein: change in protein conformation corresponds to presence of a landmark intron. EMBO J. 5, 1865-1875.
    • (1986) EMBO J. , vol.5 , pp. 1865-1875
    • Bader, B.L.1    Magin, T.M.2    Hatzfeld, M.3    Franke, W.W.4
  • 3
    • 0022415540 scopus 로고
    • Intermediate filaments in non-neuronal cells of invertebrates: Isolation and biochemical characterisation of intermediate filaments from the esophageal epithelium of the mollusc Helix pomatia
    • Bartnik, E., Osborn, M. & Weber, K. (1985). Intermediate filaments in non-neuronal cells of invertebrates: isolation and biochemical characterisation of intermediate filaments from the esophageal epithelium of the mollusc Helix pomatia. J. Cell. Biol. 101, 427-440.
    • (1985) J. Cell. Biol. , vol.101 , pp. 427-440
    • Bartnik, E.1    Osborn, M.2    Weber, K.3
  • 4
    • 0022451872 scopus 로고
    • Intermediate filaments in muscle and epithelial cells of nematodes
    • Bartnik, E., Osborn, M. & Weber, K. (1986). Intermediate filaments in muscle and epithelial cells of nematodes. J. Cell. Biol. 102, 2033-2041.
    • (1986) J. Cell. Biol. , vol.102 , pp. 2033-2041
    • Bartnik, E.1    Osborn, M.2    Weber, K.3
  • 5
    • 0028360872 scopus 로고
    • Structural elements of the amino-terminal head domain of vimentin essential for intermediate filament formation in vivo and in vitro. Expt
    • Beuttenmüller, M., Chen, M. Janetzko, A., Kühn, S. & Traub, P. (1994). Structural elements of the amino-terminal head domain of vimentin essential for intermediate filament formation in vivo and in vitro. Expt. Cell Res. 213, 128-142.
    • (1994) Cell Res. , vol.213 , pp. 128-142
    • Beuttenmüller, M.1    Chen, M.2    Janetzko, A.3    Kühn, S.4    Traub, P.5
  • 6
    • 0028910930 scopus 로고
    • The structure of a cytoplasmic intermediate filament (IF) protein from the annelid Lumbricus terrestris emphasizes a distinctive feature of protostomic if proteins
    • Bovenschulte, M., Riemer, D. & Weber, K. (1995). The structure of a cytoplasmic intermediate filament (IF) protein from the annelid Lumbricus terrestris emphasizes a distinctive feature of protostomic IF proteins. FEBS Letters, 360, 223-226.
    • (1995) FEBS Letters , vol.360 , pp. 223-226
    • Bovenschulte, M.1    Riemer, D.2    Weber, K.3
  • 7
    • 0025013610 scopus 로고
    • Structure of an invertebrate gene encoding cytoplasmic intermediate filament (IF) proteins: Implications for the origin and the diversification of if proteins
    • Dodemont, H., Riemer, D. & Weber, K. (1990). Structure of an invertebrate gene encoding cytoplasmic intermediate filament (IF) proteins: implications for the origin and the diversification of IF proteins. EMBO J. 9, 4083-4094.
    • (1990) EMBO J. , vol.9 , pp. 4083-4094
    • Dodemont, H.1    Riemer, D.2    Weber, K.3
  • 8
    • 0021968193 scopus 로고
    • Polymorphism of reconstituted human epidermal keratin filaments: Determination of their mass-per-length and width by scanning transmission electron microscopy (STEM)
    • Engel, A., Eichner, R. & Aebi, U. (1985). Polymorphism of reconstituted human epidermal keratin filaments: determination of their mass-per-length and width by scanning transmission electron microscopy (STEM). J. Ultrastruct. Res. 90, 323-335.
    • (1985) J. Ultrastruct. Res. , vol.90 , pp. 323-335
    • Engel, A.1    Eichner, R.2    Aebi, U.3
  • 9
    • 0023032014 scopus 로고
    • cDNA sequencing of nuclear lamins a and C reveals primary and secondary structural homology to intermediate filament proteins
    • Fisher, D. Z., Chaudhary, N. & Blobel, G. (1986). cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc. Natl Acad. Sci. USA, 83, 6450-6454.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 6450-6454
    • Fisher, D.Z.1    Chaudhary, N.2    Blobel, G.3
  • 10
    • 0020960602 scopus 로고
    • Preparation of single molecules and supramolecular complexes for high resolution metal shadowing
    • Fowler, W. & Aebi, U. (1983). Preparation of single molecules and supramolecular complexes for high resolution metal shadowing. J. Ultrastruct. Res. 83, 319-334.
    • (1983) J. Ultrastruct. Res. , vol.83 , pp. 319-334
    • Fowler, W.1    Aebi, U.2
  • 11
    • 0019133440 scopus 로고
    • Purification of smooth muscle desmin and a protein-chemical comparison of desmins from chicken gizzard and hog stomach
    • Geisler, N. & Weber, K. (1980). Purification of smooth muscle desmin and a protein-chemical comparison of desmins from chicken gizzard and hog stomach. Eur. J. Biochem. 111, 425-433.
    • (1980) Eur. J. Biochem. , vol.111 , pp. 425-433
    • Geisler, N.1    Weber, K.2
  • 12
    • 0026664314 scopus 로고
    • Chemical crosslinking indicates a staggered and antiparallel protofilament of desmin intermediate filaments and characterizes one higher level complex between protofilaments
    • Geisler, N., Schuenemann, J. & Weber, K. (1992). Chemical crosslinking indicates a staggered and antiparallel protofilament of desmin intermediate filaments and characterizes one higher level complex between protofilaments. Eur. J. Biochem. 206, 841-852.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 841-852
    • Geisler, N.1    Schuenemann, J.2    Weber, K.3
  • 13
    • 0012426291 scopus 로고    scopus 로고
    • Glycerol spraying/low angle rotary metal shadowing
    • (Celis, J. E., ed.), 2nd edit., Academic Press, Inc., San Diego, CA
    • Häner, M., Bremer, A. & Aebi, U. (1997). Glycerol spraying/low angle rotary metal shadowing. In Cell Biology: A Laboratory Handbook (Celis, J. E., ed.), 2nd edit., vol. 3, pp. 292-298, Academic Press, Inc., San Diego, CA.
    • (1997) Cell Biology: A Laboratory Handbook , vol.3 , pp. 292-298
    • Häner, M.1    Bremer, A.2    Aebi, U.3
  • 14
    • 0028290358 scopus 로고
    • Function of type I and type II keratin head domains: Their role in dimer, tetramer and filament formation
    • Hatzfeld, M. & Burba, M. (1994). Function of type I and type II keratin head domains: their role in dimer, tetramer and filament formation. J. Cell Sci. 107, 1959-1972.
    • (1994) J. Cell Sci. , vol.107 , pp. 1959-1972
    • Hatzfeld, M.1    Burba, M.2
  • 15
    • 0025107377 scopus 로고
    • Tailless keratins assemble into regular intermediate filaments in vitro
    • Hatzfeld, M. & Weber, K. (1990). Tailless keratins assemble into regular intermediate filaments in vitro. J. Cell Sci. 97, 317-324.
    • (1990) J. Cell Sci. , vol.97 , pp. 317-324
    • Hatzfeld, M.1    Weber, K.2
  • 16
    • 0028091403 scopus 로고
    • Making heads and tails of intermediate filament assembly, dynamics and networks
    • Heins, S. & Aebi, U. (1994). Making heads and tails of intermediate filament assembly, dynamics and networks. Curr. Opin. Cell Biol. 6, 25-33.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 25-33
    • Heins, S.1    Aebi, U.2
  • 17
    • 0027763184 scopus 로고
    • The rod domain of NF-L determines neurofilament architecture, whereas the end domains specify filament assembly and network formation
    • Heins, S., Wong, P. C., Müller, S., Goldie, K., Cleveland, D. & Aebi, U. (1993). The rod domain of NF-L determines neurofilament architecture, whereas the end domains specify filament assembly and network formation. J. Cell Biol. 123, 1517-1533.
    • (1993) J. Cell Biol. , vol.123 , pp. 1517-1533
    • Heins, S.1    Wong, P.C.2    Müller, S.3    Goldie, K.4    Cleveland, D.5    Aebi, U.6
  • 20
    • 0020051333 scopus 로고
    • A periodic ultrastructure in intermediate filaments
    • Henderson, D., Geisler, N. & Weber, K. (1982). A periodic ultrastructure in intermediate filaments. J. Mol. Biol. 155, 173-176.
    • (1982) J. Mol. Biol. , vol.155 , pp. 173-176
    • Henderson, D.1    Geisler, N.2    Weber, K.3
  • 21
    • 0032053588 scopus 로고    scopus 로고
    • Intermediate filament assembly: Fibrillogenesis is driven by decisive dimer-dimer interactions
    • Herrmann, H. & Aebi, U. (1998). Intermediate filament assembly: fibrillogenesis is driven by decisive dimer-dimer interactions. Curr. Opin. Struct. Biol. 8, 177-185.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 177-185
    • Herrmann, H.1    Aebi, U.2
  • 22
    • 0030596170 scopus 로고    scopus 로고
    • Structure and assembly properties of the intermediate filament protein vimentin: The role of its head, rod and tail domains
    • Herrmann, H., Häner, M., Brettel, M., Müller, S. A., Goldie, K. N., Fedtke, B., Lustig, A., Franke, W. W. & Aebi, U. (1996). Structure and assembly properties of the intermediate filament protein vimentin: the role of its head, rod and tail domains. J. Mol. Biol. 264, 933-953.
    • (1996) J. Mol. Biol. , vol.264 , pp. 933-953
    • Herrmann, H.1    Häner, M.2    Brettel, M.3    Müller, S.A.4    Goldie, K.N.5    Fedtke, B.6    Lustig, A.7    Franke, W.W.8    Aebi, U.9
  • 23
    • 0022339650 scopus 로고
    • Intermediate filament forming ability of desmin derivatives lacking either amino-terminal 67 or the carboxy-terminal 27 residues
    • Kaufmann, E., Weber, K. & Geisler, N. (1985). Intermediate filament forming ability of desmin derivatives lacking either amino-terminal 67 or the carboxy-terminal 27 residues. J. Mol. Biol. 185, 733-742.
    • (1985) J. Mol. Biol. , vol.185 , pp. 733-742
    • Kaufmann, E.1    Weber, K.2    Geisler, N.3
  • 24
    • 0025881180 scopus 로고
    • A potential role for the COOH-terminal domain in the lateral packing of type III intermediate filaments
    • Kouklis, P. D., Papamarcaki, T., Merdes, A. & Georgatos, S. D. (1991). A potential role for the COOH-terminal domain in the lateral packing of type III intermediate filaments. J. Cell. Biol. 114, 773-786.
    • (1991) J. Cell. Biol. , vol.114 , pp. 773-786
    • Kouklis, P.D.1    Papamarcaki, T.2    Merdes, A.3    Georgatos, S.D.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 277, 680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0024042469 scopus 로고
    • The structure and organization of human heavy neurofilament subunit (NF-H) and the gene encoding it
    • Lees, J. F., Schneidman, P. S., Skuntz, S. F., Carden, M. J. & Lazzarini, R. A. (1988). The structure and organization of human heavy neurofilament subunit (NF-H) and the gene encoding it. EMBO J. 7, 1947-1955.
    • (1988) EMBO J. , vol.7 , pp. 1947-1955
    • Lees, J.F.1    Schneidman, P.S.2    Skuntz, S.F.3    Carden, M.J.4    Lazzarini, R.A.5
  • 27
    • 0022648101 scopus 로고
    • Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins
    • McKeon, F. D., Kirschner, M. W. & Caput, D. (1986). Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature, 319, 463-468.
    • (1986) Nature , vol.319 , pp. 463-468
    • McKeon, F.D.1    Kirschner, M.W.2    Caput, D.3
  • 28
    • 0020383751 scopus 로고
    • Visualization of a 21-nm axial periodicity in shadowed keratin filaments and neurofilaments
    • Milam, L. & Erickson, H. P. (1982). Visualization of a 21-nm axial periodicity in shadowed keratin filaments and neurofilaments. J. Cell. Biol. 94, 592-596.
    • (1982) J. Cell. Biol. , vol.94 , pp. 592-596
    • Milam, L.1    Erickson, H.P.2
  • 29
    • 0026499526 scopus 로고
    • Factors influencing the precision of quantitative scanning electron microscopy
    • Müller, S. A., Goldie, K. N., Bürki, R., Häring, R. & Engel, A. (1992). Factors influencing the precision of quantitative scanning electron microscopy. Ultramicroscopy, 46, 317-334.
    • (1992) Ultramicroscopy , vol.46 , pp. 317-334
    • Müller, S.A.1    Goldie, K.N.2    Bürki, R.3    Häring, R.4    Engel, A.5
  • 30
    • 0022546016 scopus 로고
    • Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins
    • Parry, D. A. D., Conway, J. F. & Steinert, P. M. (1986). Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins. Biochem. J. 238, 305-308.
    • (1986) Biochem. J. , vol.238 , pp. 305-308
    • Parry, D.A.D.1    Conway, J.F.2    Steinert, P.M.3
  • 31
    • 0025736038 scopus 로고
    • Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase
    • Peter, M., Heitlinger, E., Häner, M., Aebi, U. & Nigg, E. A. (1991). Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase. EMBO J. 10, 1535-1544.
    • (1991) EMBO J. , vol.10 , pp. 1535-1544
    • Peter, M.1    Heitlinger, E.2    Häner, M.3    Aebi, U.4    Nigg, E.A.5
  • 32
    • 0026778228 scopus 로고
    • Analysis of the cDNA and gene encoding a cytoplasmic intermediate filament (IF) protein from the cephalochordate Branchiostoma lanceolatum; implications for the evolution of the if protein family
    • Riemer, D., Dodemont, H. & Weber, K. (1992). Analysis of the cDNA and gene encoding a cytoplasmic intermediate filament (IF) protein from the cephalochordate Branchiostoma lanceolatum; implications for the evolution of the IF protein family. Eur. J. Cell Biol. 58, 128-135.
    • (1992) Eur. J. Cell Biol. , vol.58 , pp. 128-135
    • Riemer, D.1    Dodemont, H.2    Weber, K.3
  • 34
    • 0027435278 scopus 로고
    • Diversity of intermediate filament structure: Evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments
    • Steinert, P. M., Marekov, L. N. & Parry, D. A. D. (1993a). Diversity of intermediate filament structure: evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments. J. Biol. Chem. 268, 24916-24925.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24916-24925
    • Steinert, P.M.1    Marekov, L.N.2    Parry, D.A.D.3
  • 35
    • 0027160195 scopus 로고
    • Keratin intermediate filament structure. Crosslinking studies yield quantitative information on molecular dimensions and mechanisms of assembly
    • Steinert, P. M., Marekov, L. N., Fraser, R. D. & Steinert, P. M. (1993b). Keratin intermediate filament structure. Crosslinking studies yield quantitative information on molecular dimensions and mechanisms of assembly. J. Mol. Biol. 230, 436-452.
    • (1993) J. Mol. Biol. , vol.230 , pp. 436-452
    • Steinert, P.M.1    Marekov, L.N.2    Fraser, R.D.3    Steinert, P.M.4
  • 36
    • 0024380346 scopus 로고
    • Molecular interactions in paracrystals of a fragment corresponding to the α-helical coiled coil rod portion of glial fibrillary acidic protein: Evidence for an antiparallel packing of molecules and polymorphism related to intermediate filament structure
    • Stewart, M., Quinlan, R. A. & Moir, R. D. (1989). Molecular interactions in paracrystals of a fragment corresponding to the α-helical coiled coil rod portion of glial fibrillary acidic protein: evidence for an antiparallel packing of molecules and polymorphism related to intermediate filament structure. J. Cell Biol. 109, 225-234.
    • (1989) J. Cell Biol. , vol.109 , pp. 225-234
    • Stewart, M.1    Quinlan, R.A.2    Moir, R.D.3
  • 38
    • 0020825122 scopus 로고
    • Involvement of the N-terminal polypeptide of vimentin in the formation of intermediate filaments
    • Traub, P. & Vorgias, C. E. (1983). Involvement of the N-terminal polypeptide of vimentin in the formation of intermediate filaments. J. Cell. Sci. 63, 43-67.
    • (1983) J. Cell. Sci. , vol.63 , pp. 43-67
    • Traub, P.1    Vorgias, C.E.2
  • 39
    • 0024447881 scopus 로고
    • Cytoplasmic intermediate filament proteins of invertebrates are closer to nuclear lamins than are vertebrate intermediate filament proteins; sequence characterization of two muscle proteins of a nematode
    • Weber, K., Plessmann, U. & Ulrich, W. (1989). Cytoplasmic intermediate filament proteins of invertebrates are closer to nuclear lamins than are vertebrate intermediate filament proteins; sequence characterization of two muscle proteins of a nematode. EMBO J. 8, 3221-3227.
    • (1989) EMBO J. , vol.8 , pp. 3221-3227
    • Weber, K.1    Plessmann, U.2    Ulrich, W.3
  • 40
    • 0024094057 scopus 로고
    • Amino acid sequences and homopolymer-forming ability of intermediate filament proteins from an invertebrate epithelium
    • Weber, K., Plessmann, U., Dodemont, H. & Kossmagk-Stephan, K. (1988). Amino acid sequences and homopolymer-forming ability of intermediate filament proteins from an invertebrate epithelium. EMBO J. 7, 2995-3001.
    • (1988) EMBO J. , vol.7 , pp. 2995-3001
    • Weber, K.1    Plessmann, U.2    Dodemont, H.3    Kossmagk-Stephan, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.