Characterization of distinct early assembly units of different intermediate filament proteins

Journal of Molecular Biology

Volumn 286, Issue 5, 1999, Pages 1403-1420

  Herrmann, Harald ^a   Häner, Markus ^b   Brettel, Monika ^a   Ku, Nam On ^c   Aebi, Ueli ^b  

^a GERMAN CANCER RESEARCH CENTER DKFZ   (Germany)

^b UNIVERSITY OF BASEL   (Switzerland)

^c STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Cytokeratins; Desmin; Filament assembly; Neurofilament protein; Vimentin

Indexed keywords

CYTOKERATIN; DESMIN; INTERMEDIATE FILAMENT PROTEIN; NEUROFILAMENT PROTEIN; VIMENTIN;

ARTICLE; IONIC STRENGTH; NEUROFILAMENT; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY;

EID: 0344096498     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2528     Document Type: Article

References (72)

1. Aebi U., Fowler W. E., Rew P., Sun T.-T. The fibrillar substructure of keratin filaments unravelled. J. Cell Biol. 97:1983;1131-1143.
2. Aebi U., Häner M., Troncoso J., Eichner R., Engel A. Unifying principles in intermediate filament (IF) structure and assembly. Protoplasma. 145:1988;73-81.
3. Cerdà J., Conrad M., Markl J., Brand M., Herrmann H. Zebrafish vimentin: molecular characterization, assembly properties and developmental expression. Eur. J. Cell Biol. 77:1998;175-187.
4. Chew M. K., Squire J. M. Packing of α-helical coiled-coil myosin rods in vertebrate muscle thick filaments. J. Struct. Biol. 115:1995;233-249.
5. Chou R.-G., Stromer M. H., Robson R. M., Huiatt T. W. Determination of the critical concentration required for desmin assembly. Biochem. J. 272:1990;139-145.
6. Coulombe P. A., Fuchs E. Elucidating the early stages of keratin filament assembly. J. Cell Biol. 111:1990;153-169.
7. Coulombe P. A., Chan Y., Albers K., Fuchs E. Deletions in epidermal keratins leading to alterations in filament organization in vivo and in intermediate filament assembly in vitro. J. Cell Biol. 111:1990;3049-3064.
8. Dodemont H., Riemer D., Ledger N., Weber K. Eight genes and alternative RNA processing pathways generate an unexpectedly large diversity of cytoplasmic intermediate filament proteins in the nematode, Caenorhabditis elegans. EMBO J. 12:1994;2625-2638.
9. Eckelt A., Herrmann H., Franke W. W. Assembly of a tail-less mutant of the intermediate filament protein, vimentin, in vitro and in vivo. Eur. J. Cell Biol. 58:1992;319-330.
10. Eichner R., Rew P., Engel A., Aebi U. Human epidermal keratin filaments: studies on their structure and assembly. Ann. NY Acad. Sci. 455:1985;381-402.
11. Engel A., Reichelt R. Scanned and fixed beam microscopy of cytoskeletal components. Aebi U., Engel J. Cytoskeletal and Extracellular Proteins. Structure, Interactions and Assembly. 1989;187-202 Springer-Verlag, Berlin, Heidelberg.
12. Engel A., Eichner R., Aebi U. Polymorphism of reconstituted human epidermal keratin filaments: determination of their mass-per-length and width by scanning transmission electron microscopy (STEM). J. Ultrastructure Res. 90:1985;323-335.
13. Franke W. W., Kartenbeck J. Cytokeratins. Kreis T., Vale R. Guidebook to the Cytoskeletal and Motor Proteins. 1993;145-148 Oxford University Press, Oxford.
14. 2cells. II. Structure and composition of isolated filaments. Cytobiologie. 17:1978;392-411.
15. Franke W. W., Schiller D. L., Grund C. Protofilamentous and annular structures as intermediates during reconstitution of cytokeratin filaments in vitro. Biol. Cell. 46:1982;257-268.
16. Fuchs E., Weber K. Intermediate filaments structure, dynamics, function, and disease. Annu. Rev. Biochem. 63:1994;345-382.
17. Geiger B., Kreis T. E., Gigi O., Schmid E., Mittnacht S., Jorcano J. L., von Bassewitz D. B., Franke W. W. Dynamic rearrangements of cytokeratins in living cells. Levine A. J., Vande Woude G. F., Topp W. C., Watson J. D. Cancer Cells 1, The Transformed Phenotype. 1984;201-215 Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
18. Geisler N., Weber K. Purification of smooth-muscle desmin and a protein-chemical comparison of desmins from chicken gizzard and hog stomach. Eur. J. Biochem. 111:1980;425-433.
19. Geisler N., Weber K. Self-assembly in vitro of the 68,000 molecular weight component of the mammalian neurofilament triplet proteins into intermediate-sized filaments. J. Mol. Biol. 151:1981;565-571.
20. Geisler N., Weber K. Structural aspects of intermediate filaments. Shay J. W. Cell and Molecular Biology of the Cytoskeleton. 1986;41-68 Plenum Press, New York, London.
21. Geisler N., Schünemann J., Weber K., Häner M., Aebi U. Assembly and architecture of invertebrate cytoplasmic intermediate filaments reconcile features of vertebrate cytoplasmic and nuclear lamin-type intermediate filaments. J. Mol. Biol. 282:1998;601-617.
22. Georgatos S. D., Gounari F., Goulielmos G., Aebi U. To bead or not to bead? Lens-specific intermediate filaments revisited. J. Cell Sci. 110:1997;2629-2634.
23. Gill S. R., Wong P. C., Monteiro M. J., Cleveland D. W. Assembly properties of dominant and recessive mutations in the small mouse neurofilament (NF-L) subunit. J. Cell Biol. 111:1990;2005-2019.
24. Goulielmos G., Gounari F., Remington S., Müller S., Häner M., Aebi U., Georgatos S. D. Filensin and phakinin form a novel type of beaded intermediate filaments and coassemble de novo in cultured cells. J. Cell Biol. 132:1996;643-655.
25. Heins S., Aebi U. Making heads and tails of intermediate filament assembly, dynamics and networks. Curr. Opin. Cell Biol. 6:1994;25-33.
26. Heins S., Wong P. C., Müller S., Goldie K., Cleveland D. W., Aebi U. The rod domain of NF-L determines neurofilament architecture, whereas the end domains specify filament assembly and network formation. J. Cell Biol. 123:1993;1517-1533.
27. Hemken P. M., Bellin R. M., Sernett S. W., Becker B., Huiatt T. W., Robson R. M. Molecular characteristics of the novel intermediate filament protein paranemin. J. Biol. Chem. 272:1997;32489-32499.
28. Henderson D., Geisler N., Weber K. A periodic ultrastructure in intermediate filaments. J. Mol. Biol. 155:1982;173-176.
29. Herrmann, H. 1995, Strukturbildende und topogene Domänen von Intermediärfilamentproteinen. Habilitationsschrift, 1, 68, University of Heidelberg.
30. Herrmann H., Aebi U. Intermediate filament assembly: fibrillogenesis is driven by decisive dimer-dimer interactions. Curr. Opin. Struct. Biol. 8:1998a;177-185.
31. Herrmann H., Aebi U. Structure, assembly and dynamics of intermediate filaments. Herrmann H., Harris J. R. Intermediate Filaments. Subcellular Biochemistry. 1998b;319-362 Plenum Press, New York.
32. Herrmann H., Fouquet B., Franke W. W. Expression of intermediate filament proteins during development of Xenopus laevis. I. cDNA clones encoding different forms of vimentin. Development. 105:1989a;279-298.
33. Herrmann H., Fouquet B., Franke W. W. Expression of intermediate filament proteins during development of Xenopus laevis. II. Identification and molecular characterization of desmin. Development. 105:1989b;299-307.
34. Herrmann H., Hofmann I., Franke W. W. Identification of a nonapeptide motif in the vimentin head domain involved in intermediate filament assembly. J. Mol. Biol. 223:1992;637-650.
35. Herrmann H., Eckelt A., Brettel M., Grund C., Franke W. W. Temperature-sensitive intermediate filament assembly: alternative structures of Xenopus laevis vimentin in vitro and in vivo. J. Mol. Biol. 234:1993;99-113.
36. Herrmann H., Münick M. D., Brettel M., Fouquet B., Markl J. Vimentin in a cold-water fish, the rainbow trout: Highly conserved primary structure but unique assembly properties. J. Cell Sci. 109:1996a;569-578.
37. Herrmann H., Häner M., Brettel M., Müller S. A., Goldie K. N., Fedtke B., Lustig A., Franke W. W., Aebi U. Structure and assembly properties of the intermediate filament protein vimentin: the role of its head, rod and tail domains. J. Mol. Biol. 264:1996b;933-953.
38. Hisanaga S.-I., Hirokawa N. Molecular architecture of the neurofilament. II. Reassembly process of neurofilament L protein in vitro. J. Mol. Biol. 211:1990;871-882.
39. Hisanaga S.-I., Ikai A., Hirokawa N. Molecular architecture of the neurofilament. I. Subunit arrangement of neurofilament L protein in the intermediate-sized filament. J. Mol. Biol. 211:1990;857-869.
40. Hofmann I., Franke W. W. Heterotypic interactions and filament assembly of type I and type II cytokeratins in vitro: viscometry and determinations of relative affinities. Eur. J. Cell Biol. 72:1997;122-132.
41. Hofmann I., Herrmann H., Franke W. W. Assembly and structure of calcium-induced thick vimentin filaments. Eur. J. Cell Biol. 56:1991;328-341.
42. Hynes R. O., Destree A. T. 10 nm filaments in normal and transformed cells. Cell. 13:1978;151-163.
43. Ip W., Hartzer M. K., Pang Y.-Y. S., Robson R. M. Assembly of vimentin in vitro and its implications concerning the structure of intermediate filaments. J. Mol. Biol. 183:1985;365-375.
44. Ishikawa H., Bischoff R., Holtzer H. Mitosis and intermediate-sized filaments in developing skeletal muscle. J. Cell Biol. 38:1968;538-555.
45. Janmey P., Shah J. V., Janssen K.-P. Viscoelasticity of intermediate filament networks. Herrmann H., Harris J. R. Intermediate Filaments. Subcellular Biochemistry. 1998;381-397 Plenum Press, New York.
46. Kooijman M., Bloemendal M., Traub P., van Grondelle R., van Amerongen R. Transient electric birefringence study of intermediate filament formation from vimentin and glial fibrillary acidic protein. J. Biol. Chem. 272:1997;22548-22555.
47. Ku N.-O., Omary B. Phosphorylation of human keration 8 invivo at conserved head domain serine 23 and at epidermal growth factor-stimulated tail domain serine 431. J. Biol. Chem. 272:1997;7556-7564.
48. Lawson D. Epinemin: a new protein associated with vimentin filaments in non-neuronal cells. J. Cell Biol. 97:1983;1891-1905.
49. Lazarides E. Intermediate filaments: a chemically heterogeneous, developmentally regulated class of proteins. Annu. Rev. Biochem. 51:1982;219-250.
50. Leung C. L., Flores R. L., Liem R. K. H. The complexity of intermediate filaments in the nervous system. Herrmann H., Harris J. R. Intermediate Filaments. Subcellular Biochemistry. 1998;497-526 Plenum Press, New York.
51. Müller S. A., Goldie K. N., Bürki R., Häring R., Engel A. Factors influencing the precision of quantitative scanning transmission electron microscopy. Ultramicroscopy. 46:1992;317-334.
52. Ngai J., Coleman T. R., Lazarides E. Localization of newly synthesized vimentin subunits reveals a novel mechanism of intermediate filament assembly. Cell. 60:1990;415-427.
53. Offer G. Myosin filaments. Squire J. M., Vibert P. J. Fibrous Protein Structure. 1987;307-356 Academic Press.
54. Parry D. A. D., Steinert P. M. Intermediate Filament Structure. 1995;Springer-Verlag, New York Berlin Heidelberg. p. 1-183.
55. Riemer D., Karabinos A., Weber K. Analysis of eight cDNAs and six genes for intermediate filament (IF) proteins in the cephalochordateBranchiostoma reveals differences in the IF multigene families of lower chordates and the vertebrates. Gene. 211:1998;361-373.
56. Sandilands A., Masaki S., Quinlan R. A. Lens intermediate filament proteins. Herrmann H., Harris J. R. Intermediate Filaments. Subcellular Biochemistry. 1998;291-318 Plenum Press, New York.
57. Sauk J. J., Krumweide M., Cocking-Johnson D., White J. G. Reconstitution of cytokeratin filaments in vitro: further evidence for the role of nonhelical peptides in filament assembly. J. Cell Biol. 99:1984;1590-1597.
58. Schliwa M. The Cytoskeleton. Cell Biology Monographs. 1986;Springer-Verlag, Wien New York. p. 1-326.
59. Starger J., Brown W. E., Goldmann A. E., Goldman R. D. Biochemical and immunological analysis of rapidly purified 10 nm filaments from baby hamster kidney (BHK-21) cells. J. Cell Biol. 78:1978;93-109.
60. Steinert P., Idler W., Aynardi-Whitman M., Zackroff R., Goldman R. D. Heterogeneity of intermediate filaments assembled in vitro. Cold Spring Harbor Symp. Quant. Biol. 46:1982;465-474.
61. Steinert P. M., North A. C. T., Parry D. A. D. Structural features of keratin intermediate filaments. J. Invest. Dermatol. 103:1994;19S-24S.
62. Steven A. C., Wall J., Hainfeld J., Steinert P. M. Structure of fibroblastic intermediate filaments: analysis by scanning transmission electron microscopy. Proc. Natl Acad. Sci. USA. 79:1982;3101-3105.
63. Steven A. C., Hainfeld J. F., Trus B. L., Wall J. S., Steinert P. M. The distribution of mass in heteropolymer intermediate filaments assembled in vitro. J. Biol. Chem. 258:1983a;8323-8329.
64. Steven A. C., Hainfeld J. F., Trus B. L., Wall J. S., Steinert P. M. Epidermal keratin filaments assembled in vitro have masses-per-unit-length that scalle according to average subunit mass: structural basis for homologous packing of subunits in intermediate filaments. J. Cell Biol. 97:1983b;1939-1944.
65. Steven A. C., Trus B. L., Hainfeld J. F., Wall J. S., Steinert P. M. Conformity and diversity in the structures of intermediate filaments. Ann. NY Acad. Sci. 455:1985;371-380.
66. Stromer M. H., Huiatt T. W., Richardson F. L., Robson R. M. Disassembly of synthetic 10-nm desmin filaments from smooth muscle into protofilaments. Eur. J. Cell Biol. 25:1981;136-143.
67. Stromer M. H., Ritter M. A., Pang Y.-Y. S., Robson R. M. Effect of cations and temperature on kinetics of desmin assembly. Biochem. J. 246:1987;75-81.
68. Stuurman N., Heins S., Aebi U. Nuclear lamins: their structure, assembly, and interactions. J. Struct. Biol. 122:1998;42-66.
69. Troncoso J. C., Häner M., March J. L., Reichelt R., Engel A., Aebi U. Structure and assembly of neurofilaments (NF): analysis of native NF and of specific NF subunit combinations. Aebi U., Engel J. Cytoskeletal and Extracellular Proteins. 1989;33-38 Springer-Verlag, Berlin.
70. Wiche G., Herrmann H., Leichtfried F., Pytela R. Plectin: a high-molecular weight cytoskeletal polypeptide component that copurifies with intermediate filaments of the vimentin type. Cold Spring Harbor Symp. Quant. Biol. 46:1982;475-482.
71. Winter H., Hofmann I., Langbein L., Rogers M. A., Schweizer J. A splice site mutation in the gene of the human type I hair keratin hHa1 results in the expression of a tailless keratin isoform. J. Biol. Chem. 272:1997;32345-32352.
72. Zackroff R. V., Goldman R. D. In vitro assembly of intermediate filaments from baby hamster kidney (BHK-21) cells. Proc. Natl Acad. Sci. USA. 76:1979;6226-6230.