Characterization of disulfide crosslink formation of human vimentin at the dimer, tetramer, and intermediate filament levels

Journal of Structural Biology

Volumn 117, Issue 1, 1996, Pages 55-69

  Rogers, Kevin R ^a,b   Herrmann, Harald ^b   Franke, Werner W ^b  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

^b GERMAN CANCER RESEARCH CENTER DKFZ   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

VIMENTIN;

ARTICLE; DISULFIDE BOND; HUMAN; INTERMEDIATE FILAMENT; MICROFILAMENT; PRIORITY JOURNAL; STRUCTURE ANALYSIS; ULTRASTRUCTURE;

EID: 0030198631     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1996.0069     Document Type: Article

References (53)

1. Aebi, U., Häner, M., Troncoso, J., Eichner, R., and Engel, A. (1988) Unifying principles in intermediate filament (IF) structure and assembly, Protoplasma 145, 73-81.
2. Ahmadi, B., and Speakman, P. T. (1978) Subimidate crosslinking shows rod-shaped, low cysteine, high helix protein prepared by limited proteolysis of reduced wool has four protein chains, FEBS Lett. 94, 365-367.
3. Ahmadi, B., Boston, N. M., Dobb, M. G., and Speakman, P. T. (1980) Possible four-chain repeating unit in the microfibril of wool, in Parry, D. A. D., and Creaner, L. K. (Eds.), Fibrous Proteins: Scientific, Industrial and Medical Aspects, Vol. 2, pp. 161-166, Academic Press, London.
4. Albers, K., and Fuchs, E. (1989) Expression of mutant epidermal keratin cDNAs transfected in simple epithelial and squamous cell carcinoma lines, J. Cell Biol. 105, 791-806.
5. Coulombe, P. A., and Fuchs, E. (1990) Elucidating the early stages of keratin filament assembly, J. Cell Biol. 111, 153-169.
6. Creighton, T. E. (1983) Proteins. Structure and Molecular Properties, pp. 289-291, Freeman, New York.
7. Fraser, R. D. B., MacRae, T. P., Suzuki, E., and Parry, D. A. D. (1985) Intermediate filament structure: Molecular interactions in the filament, Int. J. Biol. Macromol. 7, 285-274.
8. Fuchs, E., and Weber, K. (1994) Intermediate filaments: Structure, dynamics, function, and disease, Annu. Rev. Biochem. 63, 345-382.
9. Geisler, N., and Weber, K. (1982) The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins, EMBO J. 12, 1649-1656.
10. Geisler, N., Kaufmann, E., and Weber, K. (1985) Antiparallel orientation of two double-stranded coiled-coils in the tetrameric protofilament unit in intermediate filaments, J. Mol. Biol. 182, 173-177.
11. Geisler, N., Schünemann, J., and Weber, K. (1992) Chemical cross-linking indicates a staggered and antiparallel protofilament of desmin intermediate filaments and characterizes a higher-level complex between protofilaments, Eur. J. Biochem. 206, 841-852.
12. Gruen, L. C., and Woods, E. F. (1983) Structural studies on the microfibrillar protein of wool. Interaction between α-helical segments and reassembly of a four-chain structure, Biochem. J. 209, 587-598.
13. Hatzfeld, M., and Weber, K. (1990) The coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and type II keratins: Use of site-specific mutagenesis and recombinant protein expression, J. Cell Biol. 110, 1199-1210.
14. Heins, S., and Aebi, U. (1994) Making heads and tails of intermediate filament assembly, dynamics and networks, Curr. Opin. Cell Biol. 6, 25-33.
15. Herrmann, H., Fouquet, B., and Franke, W. W. (1989a) Expression of intermediate filament proteins during development of Xenopus laevis. I. cDNA clones encoding different forms of vimentin, Development 223, 637-650.
16. Herrmann, H., Fouquet, B., and Franke, W. W. (1989b) Expression of intermediate filament proteins during development of Xenopus laevis. II. Identification and molecular characterization of desmin, Development 105, 299-307.
17. Herrmann, H., Hofmann, I., and Franke, W. W. (1992) Identification of a nonapeptide motif in the vimentin head domain involved in intermediate filament assembly, J. Mol. Biol. 223, 637-650.
18. Herrmann, H., Eckelt, A., Brettel, M., Grund, C., and Franke, W. W. (1993) Temperature-sensitive intermediate filament assembly. Alternative structures of Xenopus laevis vimentin in vitro and in vivo, J. Mol. Biol. 234, 99-113.
19. Herrmann, H., Münick, M. D., Brettel, M., Fouquet, B., and Markl, J. (1996) Vimentin in a cold-water fish, the rainbow trout: Highly conserved primary structure but unique assembly properties. J. Cell Sci. 109, 569-578.
20. Hofmann, I., Herrmann, H., and Franke, W. W. (1991) Assembly and structure of calcium-induced thick vimentin filaments, Eur. J. Cell Biol. 56, 328-341.
21. Ip, W., Hartzer, M. K., Pang, Y. Y. S., and Robson, R. M. (1985) Assembly of vimentin and its implications concerning the structure of intermediate filaments, J. Mol. Biol. 183, 365-375.
22. Laemmli, U. K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4, Nature 227, 680-685.
23. Lehrer, S. S., Qian, Y., and Hvidt, S. (1989) Assembly of the native heterodimer of Rana esculenta tropomyosin by chain exchange, Science 246, 926-928.
24. Li, H., Choudhary, S. K., Milner, D. J., Munir, M. I., Kuisk, I. R., and Capetanaki, Y (1994) Inhibition of desmin expression blocks myoblast fusion and interferes with the myogenic regulators myoD and myogenin, J. Cell Biol. 124, 827-841.
25. Liem, R. K. H. (1993) Molecular biology of neuronal intermediate filaments, Curr. Opin. Cell Biol. 5, 12-16.
26. McLachlan, A. D., and Stewart, M. (1982) Periodic charge distribution in the intermediate filament proteins desmin and vimentin, J. Mol. Biol. 162, 693-698.
27. Parry, D. A. D., and Fraser, R. D. B. (1985) Intermediate filament structure: Molecular interactions in the filament, Int. J. Biol. Macromol. 7, 203-213.
28. Parry, D. A. D., and Steinert, P. M. (1992) Intermediate filament structure, Curr. Opin. Cell Biol. 4, 94-98.
29. Parry, D. A. D., and Steinert, P. M. (1995) Intermediate Filament Structure, pp. 1-183, Springer-Verlag, New York/Berlin/ Heidelberg.
30. Parry, D. A. D., Steven, A. C., and Steinert, P. M. (1985) The coiled-coil molecules of intermediate filaments consist of two parallel chains in exact axial register, Biochem. Biophys. Res. Commun. 127, 1012-1018.
31. Quax-Jeuken, Y. E. F. M., Quax, W. J., and Bloemendal, H. (1983) Primary and secondary structure of hamster vimentin predicted from the nucleotide sequence, Proc. Natl. Acad. Sci. USA 80, 3548-3552.
32. Quinlan, R. A., and Franke, W. W. (1982) Heteropolymer filaments of vimentin and desmin in vascular smooth muscle tissue and cultured baby hamster kidney cells demonstrated by chemical crosslinking. Proc. Natl. Acad. Sci. USA 79, 3452-3456.
33. Quinlan, R. A., and Franke, W. W. (1983) Molecular interactions of intermediate filament-sized filaments revealed by chemical crosslinking. Heteropolymers of vimentin and glial filament protein in cultured human glioma cells, Eur. J. Biochem. 132, 477-484.
34. 2) complexes of non-epidermal keratins isolated from the cytoskeletons of rat hepatocytes and hepatoma cells, J. Mol. Biol. 178, 365-388.
35. Quinlan, R. A., Hatzfeld, M., Franke, W. W., Lustig, A., Schulthess, T., and Engel, J. (1986) Characterization of dimer subunits of intermediate filament proteins, J. Mol. Biol. 192, 337-349.
36. Rogers, K. R., Morris, C. J., and Blake, B. R. (1989) Cytoskeletal rearrangement by oxidative stress, Int. J. Tissue React. 11, 309-314.
37. Rogers, K. R., Morris, C. J., and Blake, B. R. (1991) Oxidation of thiol in the vimentin cytoskeleton, Biochem. J. 275, 789-791.
38. Soellner, P., Quinlan, R. A., and Franke, W. W. (1985) Identification of a distinct soluble subunit of an intermediate filament protein: Tetrameric vimentin from living cells, Proc. Natl. Acad. Sci. USA 82, 7929-7933.
39. Steinert, P. M. (1990) The two-chain coiled-coil molecule of native epidermal keratin intermediate filaments is a type I-type-II heterodimer, J. Biol. Chem. 265, 8766-8774.
40. Steinert, P. M. (1991) Analysis of the mechanism of assembly of mouse keratin 1/keratin 10 intermediate filaments in vitro suggests that intermediate filaments are built from multiple oligomer units rather than a unique tetrameric building block, J. Struct. Biol. 107, 175-188.
41. Steinert, P. M., and Parry, D. A. (1993) The conserved HI domain of the type II keratin 1 chain plays an essential role in the alignment of nearest neighbor molecules in mouse and human keratin 1/keratin 10 intermediate filaments at the two-to four-molecule level of structure, J. Biol. Chem. 268, 2878-2887.
42. Steinert, P. M., and Roop, D. R. (1988) Molecular and cellular biology of intermediate filaments, Annu. Rev. Biochem. 57, 593-625.
43. Steinert, P. M., Rice, R. H., Roop, D. R., Trus, B. L., and Stevens, A. C. (1983) Complete amino acid sequence of a mouse epidermal keratin subunit and implications for the structure of intermediate filaments, Nature 301, 794-800.
44. Steinert, P. M., Stevens, A. C., and Roop, D. R. (1985) The molecular biology of intermediate filaments, Cell 42, 411-419.
45. Steinert, P. M., Marekov, L. N., Fraser, R. D., and Parry, D. A. (1993a) Keratin intermediate filament structure. Crosslinking studies yield quantitative information on molecular dimensions and mechanisms of assembly, J. Mol. Biol. 230, 436-452.
46. Steinert, P. M., Marekov, L. N., and Parry, D. A. (1993b) 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.
47. Stewart, M. (1993) Intermediate filament structure and assembly, Curr. Opin. Cell Biol. 5, 3-11.
48. Stewart, M., Quinlan, R. A., and Moir, R. D. (1989) Molecular interactions in paracrystals of a fragment corresponding to the 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.
49. Traub, P., Perides, G., Schimmel, H., and Scherbarth, A. (1986) Interaction in vitro of nonepithelial intermediate filament proteins with total cellular lipids, individual phospholipids, and a phospholipid mixture, J. Biol. Chem. 261, 10558-10568.
50. Traub, P., Kühn, S., and Grub, S. (1993) Separation and characterization of homo and hetero-oligomers of the intermediate filament proteins desmin and vimentin, J. Mol. Biol. 230, 837-856.
51. van de Hundert, F. A. J. M., Raats, J. M. H., and Bloemendal, H. (1993) Intermediate filaments: Regulation of gene expression and assembly, Eur. J. Biochem. 214, 351-366.
52. Weber, K., and Geisler, N. (1984) Intermediate filaments - from wool α-keratins to neurofilaments: A structural overview, in Levine, A. J., Vande Woude, G. F., Topp, W. C., and Watson, J. D. (Eds.), Cancer Cells, The Transformed Phenotype, Vol. 1, pp. 153-159, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
53. Woods, E. F., and Gruen, L. C. (1981) Structural studies on the microfibrillar proteins of wool: Characterization of the α-helicalrich particule produced by chymotryptic digest, Aust. J. Biol. Sci. 34, 515-526.