Intermediate filaments: A historical perspective

Experimental Cell Research

Volumn 313, Issue 10, 2007, Pages 1981-1994

  Oshima, Robert G ^a  

^a BURNHAM INSTITUTE   (United States)

Author keywords

desmin; gfap; Intermediate filament; Keratin; Neurofilament; Vimentin

Indexed keywords

AMINO ACID SEQUENCE; AUSTRALIA; BODY FAT DISTRIBUTION; BRAIN DISEASE; CELL DEATH; CYTOSKELETON; ELECTRON MICROSCOPY; GENETIC ANALYSIS; HEART DISEASE; HUMAN; INTERMEDIATE FILAMENT; LIVER DISEASE; MICROSCOPY; MOLECULE; MULTIGENE FAMILY; NONHUMAN; POLYMERIZATION; PREMATURE AGING; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN STRUCTURE; REVIEW; SHEEP; SKIN DISEASE; STEM CELL; X RAY ANALYSIS;

EID: 34249680307     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2007.04.007     Document Type: Review

References (201)

1. Hesse M., Magin T.M., and Weber K. Genes for intermediate filament proteins and the draft sequence of the human genome: novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18. J. Cell Sci. 114 (2001) 2569-2575
2. Schweizer J., Bowden P.E., Coulombe P.A., Langbein L., Lane E.B., Magin T.M., Maltais L., Omary M.B., Parry D.A., Rogers M.A., and Wright M.W. New consensus nomenclature for mammalian keratins. J. Cell Biol. 174 (2006) 169-174
3. Franke W.W., Schmid E., Winter S., Osborn M., and Weber K. Widespread occurrence of intermediate-sized filaments of the vimentin-type in cultured cells from diverse vertebrates. Exp. Cell Res. 123 (1979) 25-46
4. Lazarides E., and Hubbard B.D. Immunological characterization of the subunit of the 100 A filaments from muscle cells. Proc. Natl. Acad. Sci. U. S. A. 73 (1976) 4344-4348
5. Bignami A., Eng L.F., Dahl D., and Uyeda C.T. Localization of the glial fibrillary acidic protein in astrocytes by immunofluorescence. Brain Res. 43 (1972) 429-435
6. Portier M.M., de Nechaud B., and Gros F. Peripherin, a new member of the intermediate filament protein family. Dev. Neurosci. 6 (1983) 335-344
7. Hoffman P.N., and Lasek R.J. The slow component of axonal transport. Identification of major structural polypeptides of the axon and their generality among mammalian neurons. J. Cell Biol. 66 (1975) 351-366
8. Lendahl U., Zimmerman L.B., and McKay R.D.G. CNS stem cells express a new class of intermediate filament protein. Cell 60 (1990) 585-595
9. Kaplan M.P., Chin S.S., Fliegner K.H., and Liem R.K. Alpha-internexin, a novel neuronal intermediate filament protein, precedes the low molecular weight neurofilament protein (NF-L) in the developing rat brain. J. Neurosci. 10 (1990) 2735-2748
10. Newey S.E., Howman E.V., Ponting C.P., Benson M.A., Nawrotzki R., Loh N.Y., Davies K.E., and Blake D.J. Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle. J. Biol. Chem. 276 (2001) 6645-6655
11. Bellin R.M., Sernett S.W., Becker B., Ip W., Huiatt T.W., and Robson R.M. Molecular characteristics and interactions of the intermediate filament protein synemin. Interactions with alpha-actinin may anchor synemin-containing heterofilaments. J. Biol. Chem. 274 (1999) 29493-29499
12. Lazarides E. Intermediate filaments: a chemically heterogeneous, developmentally regulated class of proteins. Ann. Rev. Biochem. 51 (1982) 219-250
13. Fuchs E., and Weber K. Intermediate filaments: structure, dynamics, function, and disease. Ann. Rev. Biochem. 63 (1994) 345-382
14. Steinert P.M., and Roop D.R. Molecular and cellular biology of intermediate filaments. Ann. Rev. Biochem. 57 (1988) 593-625
15. Fuchs E., and Cleveland D.W. A structural scaffolding of intermediate filaments in health and disease. Science 279 (1998) 514-519
16. Omary M.B., Coulombe P.A., and McLean W.H. Intermediate filament proteins and their associated diseases. N. Engl. J. Med. 351 (2004) 2087-2100
17. Helfand B.T., Chang L., and Goldman R.D. The dynamic and motile properties of intermediate filaments. Annu. Rev. Cell Dev. Biol. 19 (2003) 445-467
18. Coulombe P.A., and Wong P. Cytoplasmic intermediate filaments revealed as dynamic and multipurpose scaffolds. Nat. Cell Biol. 6 (2004) 699-706
19. Lariviere R.C., and Julien J.P. Functions of intermediate filaments in neuronal development and disease. J. Neurobiol. 58 (2004) 131-148
20. Porter R.M., and Lane E.B. Phenotypes, genotypes and their contribution to understanding keratin function. Trends Genet. 19 (2003) 278-285
21. Coulombe P.A., and Omary M.B. 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments. Curr. Opin. Cell Biol. 14 (2002) 110-122
22. Herrmann H., Hesse M., Reichenzeller M., Aebi U., and Magin T.M. Functional complexity of intermediate filament cytoskeletons: from structure to assembly to gene ablation. Int. Rev. Cyt. 223 (2003) 83-175
23. Herrmann H., and Aebi U. Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Ann. Rev. Biochem. 73 (2004) 749-789
24. Capell B.C., and Collins F.S. Human laminopathies: nuclei gone genetically awry. Nat. Rev., Genet. 7 (2006) 940-952
25. Goldman R.D. Worms reveal essential functions for intermediate filaments. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 7659-7661
26. Pallari H.M., and Eriksson J.E. Intermediate filaments as signaling platforms. Sci. STKE 2006 (2006) pe53
27. Lazarides E. Intermediate filaments as mechanical integrators of cellular space. Nature 283 (1980) 249-256
28. Astbury W.T., and Street A. X-ray studies of the structure of hair, wool, and related fibres. Philos. Trans. R. Soc. Lond. 230 (1932) 75-101
29. Crick F.H. Is alpha-keratin a coiled coil?. Nature 170 (1952) 882-883
30. Crick F.H. The packing of a-helices: simple coiled-coils. Acta Crystallogr. 6 (1953) 689-697
31. Steinert P.M., Idler W.W., and Zimmerman S.B. Self-assembly of bovine keratin filaments in vitro. J. Mol. Biol. 108 (1976) 547-567
32. Strelkov S.V., Herrmann H., Geisler N., Wedig T., Zimbelmann R., Aebi U., and Burkhard P. Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. EMBO J. 21 (2002) 1255-1266
33. Herrmann H., Strelkov S.V., Feja B., Rogers K.R., Brettel M., Lustig A., Haner M., Parry D.A., Steinert P.M., Burkhard P., and Aebi U. The intermediate filament protein consensus motif of helix 2B: its atomic structure and contribution to assembly. J. Mol. Biol. 298 (2000) 817-832
34. Strelkov S.V., Schumacher J., Burkhard P., Aebi U., and Herrmann H. Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins. J. Mol. Biol. 343 (2004) 1067-1080
35. Ishikawa H., Bischoff R., and Holtzer H. Mitosis and intermediate-sized filaments in developing skeletal muscle. J. Cell Biol. 38 (1968) 538-555
36. Huneeus F.C., and Davison P.F. Fibrillar proteins from squid axons. I. Neurofilament protein. J. Mol. Biol. 52 (1970) 415-428
37. Julien J.P., Meyer D., Flavell D., Hurst J., and Grosveld F. Cloning and developmental expression of the murine neurofilament gene family. Brain Res. 387 (1986) 243-250
38. Garcia M.L., Lobsiger C.S., Shah S.B., Deerinck T.J., Crum J., Young D., Ward C.M., Crawford T.O., Gotow T., Uchiyama Y., Ellisman M.H., Calcutt N.A., and Cleveland D.W. NF-M is an essential target for the myelin-directed "outside-in" signaling cascade that mediates radial axonal growth. J. Cell Biol. 163 (2003) 1011-1020
39. Jacomy H., Zhu Q., Couillard-Despres S., Beaulieu J.M., and Julien J.P. Disruption of type IV intermediate filament network in mice lacking the neurofilament medium and heavy subunits. J. Neurochem. 73 (1999) 972-984
40. Zhu Q., Lindenbaum M., Levavasseur F., Jacomy H., and Julien J.P. Disruption of the NF-H gene increases axonal microtubule content and velocity of neurofilament transport: relief of axonopathy resulting from the toxin beta,beta′-iminodipropionitrile. J. Cell Biol. 143 (1998) 183-193
41. Rao M.V., Houseweart M.K., Williamson T.L., Crawford T.O., Folmer J., and Cleveland D.W. Neurofilament-dependent radial growth of motor axons and axonal organization of neurofilaments does not require the neurofilament heavy subunit (NF-H) or its phosphorylation. J. Cell Biol. 143 (1998) 171-181
42. Hirokawa N., and Takeda S. Gene targeting studies begin to reveal the function of neurofilament proteins. J. Cell Biol. 143 (1998) 1-4
43. Eyer J., and Peterson A. Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilament-beta-galactosidase fusion protein. Neuron 12 (1994) 389-405
44. Xu Z., Cork L.C., Griffin J.W., and Cleveland D.W. Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease. Cell 73 (1993) 23-33
45. Cote F., Collard J.-F., and Julien J.-P. Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: a mouse model of Amyotrophic Lateral Sclerosis. Cell 73 (1993) 35-46
46. Mersiyanova I.V., Perepelov A.V., Polyakov A.V., Sitnikov V.F., Dadali E.L., Oparin R.B., Petrin A.N., and Evgrafov O.V. A new variant of Charcot-Marie-Tooth disease type 2 is probably the result of a mutation in the neurofilament-light gene. Am. J. Hum. Genet. 67 (2000) 37-46
47. Garcia M.L., Singleton A.B., Hernandez D., Ward C.M., Evey C., Sapp P.A., Hardy J., Brown Jr. R.H., and Cleveland D.W. Mutations in neurofilament genes are not a significant primary cause of non-SOD1-mediated amyotrophic lateral sclerosis. Neurobiol. Dis. 21 (2006) 102-109
48. Doetsch F., Caille I., Lim D.A., Garcia-Verdugo J.M., and Alvarez-Buylla A. Subventricular zone astrocytes are neural stem cells in the adult mammalian brain. Cell 97 (1999) 703-716
49. Lazarides E., and Weber K. Actin antibody: the specific visualization of actin filaments in non-muscle cells. Proc. Natl. Acad. Sci. U. S. A. 71 (1974) 2268-2272
50. Hynes R.O., and Destree A.T. 10 nm filaments in normal and transformed cells. Cell 13 (1978) 151-163
51. Franke W.W., Schmid E., Osborn M., and Weber K. Different intermediate-sized filaments distinguished by immunofluorescence microscopy. Proc. Natl. Acad. Sci. U. S. A. 75 (1978) 5034-5038
52. Liem R.K., Yen S.H., Salomon G.D., and Shelanski M.L. Intermediate filaments in nervous tissues. J. Cell Biol. 79 (1978) 637-645
53. Sun T.-T., and Green H. Immunofluorescent staining of keratin fibers in cultured cells. Cell 14 (1978) 469-476
54. Fuchs E., and Green H. The expression of keratin genes in epidermis and cultured epidermal cells. Cell 15 (1978) 887-897
55. Fuchs E., and Green H. Multiple keratins of cultured human epidermal cells are translated from different mRNA molecules. Cell 17 (1979) 573-582
56. Fuchs E., and Green H. Changes in keratin gene expression during terminal differentiation of the keratinocyte. Cell 19 (1980) 1033-1042
57. Fuchs E.V., Coppock S.M., Green H., and Cleveland D.W. Two distinct classes of keratin genes and their evolutionary significance. Cell 27 (1981) 75-84
58. Hanukoglu I., and Fuchs E. The cDNA sequence of a human epidermal keratin: divergence of sequence but conservation of structure among intermediate filament proteins. Cell 31 (1982) 243-252
59. Coulombe P.A., Hutton M.E., Letai A., Hebert A., Paller A.S., and Fuchs E. Point mutations in human keratin 14 genes of epidermolysis bullosa simplex patients: genetic and functional analyses. Cell 66 (1991) 1301-1311
60. Franke W.W., Weber K., Osborn M., Schmid E., and Freudenstein C. Antibody to prekeratin: decoration of tonofilament-like arrays in various cells of epithelial character. Exp. Cell Res. 116 (1978) 429-445
61. Moll R., Franke W.W., Schiller D.L., Geiger B., and Krepler R. The catalog of human cytokeratins: patterns of expression in normal epithelia, tumors and cultured cells. Cell 31 (1982) 11-24
62. Hatzfeld M., and Franke W.W. Pair formation and promiscuity of cytokeratins: formation in vitro of heterotypic complexes and intermediate-sized filaments by homologous and heterologous recombinations of purified polypeptides. J. Cell Biol. 101 (1985) 1826-1841
63. Kim K.H., Rheinwald J.G., and Fuchs E.V. Tissue specificity of epithelial keratins: differential expression of mRNAs from two multigene families. Mol. Cell. Biol. 3 (1983) 495-502
64. Geisler N., and Weber K. The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins. EMBO J. 1 (1982) 1649-1656
65. Brulet P., Babinet C., Kemler R., and Jacob F. Monoclonal antibodies against trophectoderm-specific markers during mouse blastocyst formation. Proc. Natl. Acad. Sci. U. S. A. 77 (1980) 4113-4117
66. Kemler R., Brulet P., Schnebelen M.T., Gaillard J., and Jacob F. Reactivity of monoclonal antibodies against intermediate filament proteins during embryonic development. J. Embryol. Exp. Morphol. 64 (1981) 45-60
67. Oshima R.G. Identification and immunoprecipitation of cytoskeletal proteins from murine extra-embryonic endodermal cells. J. Biol. Chem. 256 (1981) 8124-8133
68. Oshima R.G. Developmental expression of murine extra-embryonic endodermal cytoskeletal proteins. J. Biol. Chem. 257 (1982) 3414-3421
69. Jackson B.W., Grund C., Schmid E., Burke K., Franke W., and Illmensee K. Formation of cytoskeletal elements during mouse embryogenesis intermediate filaments of the cytokeratin type and desmosomes in preimplantation embryos. Differentiation 17 (1980) 161-179
70. Paulin D., Jakob H., Jacob J., Weber K., and Osborn M. In vitro differentiation of mouse teratocarcinoma cells monitored by intermediate filament expression. Differentiation 22 (1982) 90-99
71. Oshima R.G., Howe W.E., Klier F.G., Adamson E.D., and Shevinsky L.H. Intermediate filament protein synthesis in preimplantation murine embryos. Dev. Biol. 99 (1983) 447-455
72. Franke W.W., Grund C., Kuhn C., Jackson B.W., and Illmensee K. Formation of cytoskeletal elements during mouse embryogenesis: III. Primary mesenchymal cells and the first appearance of vimentin filaments. Differentiation 23 (1982) 43-59
73. Jackson B.W., Grund C., Winter S., Franke W.W., and Illmensee K. Formation of cytoskeletal elements during mouse embryogenesis: epithelial differentiation and intermediate-sized filaments in early postimplantation embryos. Differentiation 20 (1981) 203-216
74. Trevor K., and Oshima R.G. Preimplantation mouse embryos and liver express the same type I keratin gene product. J. Biol. Chem. 260 (1985) 15885-15891
75. Singer P.A., Trevor K., and Oshima R.G. Molecular cloning and characterization of the Endo B cytokeratin expressed in preimplantation mouse embryos. J. Biol. Chem. 261 (1986) 538-547
76. Vasseur M., Duprey P., Brulet P., and Jacob F. One gene and one pseudogene for the cytokeratin endo A. Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 1155-1159
77. Duprey P., Morello D., Vasseur M., Babinet C., Condamine H., Brulet P., and Jacob F. Expression of the cytokeratin endo A gene during early mouse embryogenesis. Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 8535-8539
78. Ichinose Y., Morita T., Zhang F., Srimahasongcram S., Tondella M.L.C., Matsumoto M., Nozaki M., and Matsushiro A. Nucleotide sequence and structure of the mouse cytokeratin endoB gene. Gene 70 (1988) 85-95
79. Oshima R.G., Abrams L., and Kulesh D. Activation of an intron enhancer within the keratin 18 gene by expression of c-fos and c-jun in undifferentiated F9 embryonal carcinoma cells. Genes Dev. 4 (1990) 835-848
80. Fujimura Y., Yamamoto H., Hamazato F., and Nozaki M. One of two ets-binding sites in the cytokeratin EndoA enhancer is essential for enhancer activity and binds to ets-2 related proteins. Nucleic Acids Res. 22 (1994) 613-618
81. Takemoto Y., Fujimura Y., Matsumoto M., Tamai Y., Morita T., Matsushiro A., and Nozaki M. The promoter of the endo A cytokeratin gene is activated by a 3′ downstream enhancer. Nucleic Acids Res. 19 (1991) 2761-2765
82. Seth A., Robinson L., Panayiotakis A., Thompson D.M., Hodge D.R., Zhang X.K., Watson D.K., Ozato K., and Papas T.S. The EndoA enhancer contains multiple ETS binding site repeats and is regulated by ETS proteins. Oncogene 9 (1994) 469-477
83. Oshima R.G., Baribault H., and Caulin C. Oncogenic regulation and function of keratin 8 and 18. Cancer Metastasis Rev. 15 (1996) 445-471
84. Cecena G., Wen F., Cardiff R.D., and Oshima R.G. Differential sensitivity of mouse epithelial tissues to the polyomavirus middle T oncogene. Am. J. Pathol. 168 (2006) 310-320
85. Lersch R., Stellmach V., Stocks C., Giudice G., and Fuchs E. Isolation, sequence, and expression of a human keratin K5 gene: transcriptional regulation of keratins and insights into pairwise control. Mol. Cell. Biol. 9 (1989) 3685-3697
86. Vasioukhin V., Degenstein L., Wise B., and Fuchs E. The magical touch: genome targeting in epidermal stem cells induced by tamoxifen application to mouse skin. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 8551-8556
87. Vassar R., and Fuchs E. Transgenic mice provide new insights into the role of TGF-alpha during epidermal development and differentiation. Genes Dev. 5 (1991) 714-727
88. Lu B., Rothnagel J.A., Longley M.A., Tsai S.Y., and Roop D.R. Differentiation-specific expression of human keratin 1 is mediated by a composite AP-1/steroid hormone element. J. Biol. Chem. 269 (1994) 7443-7449
89. Brenner M., Kisseberth W.C., Su Y., Besnard F., and Messing A. GFAP promoter directs astrocyte-specific expression in transgenic mice. J. Neurosci. 14 (1994) 1030-1037
90. Kuisk I.R., Li H., Tran D., and Capetanaki Y. A single MEF2 site governs desmin transcription in both heart and skeletal muscle during mouse embryogenesis. Dev. Biol. 174 (1996) 1-13
91. Frisen J., Johansson C.B., Torok C., Risling M., and Lendahl U. Rapid, widespread, and longlasting induction of nestin contributes to the generation of glial scar tissue after CNS injury. J. Cell Biol. 131 (1995) 453-464
92. Zimmerman L., Parr B., Lendahl U., Cunningham M., McKay R., Gavin B., Mann J., Vassileva G., and McMahon A. Independent regulatory elements in the nestin gene direct transgene expression to neural stem cells or muscle precursors. Neuron 12 (1994) 11-24
93. Sahlgren C.M., Pallari H.M., He T., Chou Y.H., Goldman R.D., and Eriksson J.E. A nestin scaffold links Cdk5/p35 signaling to oxidant-induced cell death. EMBO J. 25 (2006) 4808-4819
94. Denk H., Franke W.W., Eckerstorfer R., Schmid E., and Kerjaschki D. Formation and involution of Mallory bodies ("alcoholic hyalin") in murine and human liver revealed by immunofluorescence microscopy with antibodies to prekeratin. Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 4112-4116
95. Bannasch P., Zerban H., Schmid E., and Franke W.W. Liver tumors distinguished by immunofluorescence microscopy with antibodies to proteins of intermediate-sized filaments. Proc. Natl. Acad. Sci. U. S. A. 77 (1980) 4948-4952
96. Osborn M., and Weber K. Tumor diagnosis by intermediate filament typing: a novel tool for surgical pathology. Lab. Invest. 48 (1983) 372-394
97. Debus E., Weber K., and Osborn M. Monoclonal cytokeratin antibodies that distinguish simple from stratified squamous epithelia: characterization on human tissues. EMBO J. 1 (1982) 1641-1647
98. Lane E.B., and Klymkowsky M.W. Epithelial tonofilaments: investigating their form and function using monoclonal antibodies. Cold Spring Harbor Symp. Quant. Biol. (1982) 387-402
99. Lane E.B. Monoclonal antibodies provide specific intramolecular markers for the study of epithelial tonofilament organization. J. Cell Biol. 92 (1982) 665-673
100. Ramaekers F., Huysmans A., Moesker O., Kant A., Jap P., Herman C., and Vooijs P. Monoclonal antibody to keratin filaments, specific for glandular epithelia and their tumors. Lab. Invest. 49 (1983) 353-361
101. Tseng C.G., Jarvinen M.J., Nelson W.G., Huang J.W., Woodcock-Mitchell J., and Sun T.T. Correlation of specific keratins with different types of epithelial differentiation: monoclonal antibody studies. Cell 30 (1982) 361-372
102. Franke W.W., Schmid E., Weber K., and Osborn M. HeLa cells contain intermediate-sized filaments of the prekeratin type. Exp. Cell Res. 118 (1979) 95-109
103. Weber K., Osborn M., Moll R., Wiklund B., and Luning B. Tissue polypeptide antigen (TPA) is related to the non-epidermal keratins 8, 18 and 19 typical of simple and non-squamous epithelia: re-evaluation of a human tumor marker. EMBO J. 3 (1984) 2707-2714
104. Stigbrand T., Andres C., Bellanger L., Omary M.B., Bodenmiiller H., Bonfrer H., Brundell J., Einarsson R., Erlandsson A., Johansson A., Leca J.F., Levi M., Meier T., Nap M., Nustad K., Seguin P., Sjodin A., Sundstrom B., van Dalen A., Wiebelhause E., Wiklund B., Arlestig L., and Hilgers J. Epitope specificity of 30 monoclonal antibodies against cytokeratin antigens: the ISOBM TD5-1 workshop. Tumor Biol. 19 (1998) 132-152
105. Rao L., Perez D., and White E. Lamin proteolysis facilitates nuclear events during apoptosis. J. Cell Biol. 135 (1996) 1441-1455
106. Takahashi A., Alnemri E.S., Lazebnik Y.A., Fernandes-Alnemri T., Litwack G., and Moir R.D. Cleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 8395-8400
107. Caulin C., Salvesen G.S., and Oshima R.G. Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial apoptosis. J. Cell Biol. 138 (1997) 1379-1394
108. Ku N.-O., Liao J., and Omary M.B. Apoptosis generates stable fragments of human type I keratins. J. Biol. Chem. 272 (1997) 33197-33203
109. Leers M.P., Kolgen W., Bjorklund V., Bergman T., Tribbick G., Persson B., Bjorklund P., Ramaekers F.C., Bjorklund B., Nap M., Jornvall H., and Schutte B. Immunocytochemical detection and mapping of a cytokeratin 18 neo-epitope exposed during early apoptosis. J. Pathol. 187 (1999) 567-572
110. Chen F., Chang R., Trivedi M., Capetanaki Y., and Cryns V.L. Caspase proteolysis of desmin produces a dominant-negative inhibitor of intermediate filaments and promotes apoptosis. J. Biol. Chem. 278 (2003) 6848-6853
111. Byun Y., Chen F., Chang R., Trived M., Green K.J., and Cryns V.L. Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis. Cell Death Differ. 8 (2001) 443-450
112. Stegh A.H., Herrmann H., Lampel S., Weisenberger D., Andra K., Seper M., Wiche G., Krammer P.H., and Peter M.E. Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis. Mol. Cell. Biol. 20 (2000) 5665-5679
113. Lee J.C., Schickling O., Stegh A.H., Oshima R.G., Dinsdale D., Cohen G.M., and Peter M.E. DEDD regulates degradation of intermediate filaments during apoptosis. J. Cell Biol. 158 (2002) 1051-1066
114. Pruss R.M., Mirsky R., and Raff M.C. All classes of intermediate filaments share a common antigenic determinant defined by a monoclonal antibody. Cell 27 (1981) 419-428
115. McKeon F.D., Kirschner M.W., and Caput D. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319 (1986) 463-468
116. Weber K., Plessmann U., and Ulrich W. 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 (1989) 3221-3227
117. Karabinos A., Schmidt H., Harborth J., Schnabel R., and Weber K. Essential roles for four cytoplasmic intermediate filament proteins in Caenorhabditis elegans development. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 7863-7868
118. Aebi U., Cohn J., Buhle L., and Gerace L. The nuclear lamina is a meshwork of intermediate-type filaments. Nature 323 (1986) 560-564
119. Klymkowsky M.W. Intermediate filaments in 3T3 cells collapse after intracellular injection of a monoclonal anti-intermediate filament antibody. Nature 291 (1981) 249-251
120. Klymkowsky M.W., Miller R.H., and Lane E.B. Morphology, behavior, and interaction of cultured epithelial cells after the antibody-induced disruption of keratin filament organization. J. Cell Biol. 96 (1983) 494-509
121. Emerson J.A. Disruption of the cytokeratin filament network in the preimplantation mouse embryo. Development 104 (1988) 219-234
122. Yamasaki H., Itakura C., and Mizutani M. Hereditary hypotrophic axonopathy with neurofilament deficiency in a mutant strain of the Japanese quail. Acta Neuropathol. (Berl) 82 (1991) 427-434
123. Ohara O., Gahara Y., Miyake T., Teraoka H., and Kitamura T. Neurofilament deficiency in quail caused by nonsense mutation in neurofilament-L gene. J. Cell Biol. 121 (1993) 387-395
124. Baribault H., and Oshima R.G. Polarized and functional epithelia can form after the targeted inactivation of both mouse keratin 8 alleles. J. Cell Biol. 115 (1991) 1675-1684
125. Kulesh D.A., Cecena G., Darmon Y.M., Vasseur M., and Oshima R.G. Post-translational regulation of keratins: degradation of unpolymerized mouse and human keratins 18 and 8. Mol. Cell. Biol. 9 (1989) 1553-1565
126. Baribault H., Price J., Miyai K., and Oshima R.G. Mid-gestational lethality in mice lacking keratin 8. Genes Dev. 7 (1993) 1191-1202
127. Rossant J., and Cross J.C. Placental development: lessons from mouse mutants. Nat. Rev., Genet. 2 (2001) 538-548
128. Jaquemar D., Kupriyanov S., Wankell M., Avis J., Benirschke K., Baribault H., and Oshima R.G. Keratin 8 protection of placental barrier function. J. Cell Biol. 161 (2003) 749-756
129. Hesse M., Franz T., Tamai Y., Taketo M.M., and Magin T.M. Targeted deletion of keratins 18 and 19 leads to trophoblast fragility and early embryonic lethality. EMBO J. 19 (2000) 5060-5070
130. Caulin C., Ware C.F., Magin T.M., and Oshima R.G. Keratin-dependent, epithelial resistance to tumor necrosis factor-induced apoptosis. J. Cell Biol. 149 (2000) 17-22
131. Ku N.O., Soetikno R.M., and Omary M.B. Keratin mutation in transgenic mice predisposes to Fas but not TNF-induced apoptosis and massive liver injury. Hepatology 37 (2003) 1006-1014
132. Inada H., Izawa I., Nishizawa M., Fujita E., Kiyono T., Takahashi T., Momoi T., and Inagaki M. Keratin attenuates tumor necrosis factor-induced cytotoxicity through association with TRADD. J. Cell Biol. 155 (2001) 415-426
133. Tong X., and Coulombe P.A. Keratin 17 modulates hair follicle cycling in a TNFalpha-dependent fashion. Genes Dev. 20 (2006) 1353-1364
134. Gilbert S., Loranger A., and Marceau N. Keratins modulate c-Flip/extracellular signal-regulated kinase 1 and 2 antiapoptotic signaling in simple epithelial cells. Mol. Cell. Biol. 24 (2004) 7072-7081
135. Ku N.O., and Omary M.B. A disease- and phosphorylation-related nonmechanical function for keratin 8. J. Cell Biol. 174 (2006) 115-125
136. Zatloukal K., Stumptner C., Lehner M., Denk H., Baribault H., Eshkind L.G., and Franke W.W. Cytokeratin 8 protects from hepatotoxicity, and its ratio to cytokeratin 18 determines the ability of hepatocytes to form Mallory bodies. Am. J. Pathol. 156 (2000) 1263-1274
137. Ku N.O., Darling J.M., Krams S.M., Esquivel C.O., Keeffe E.B., Sibley R.K., Lee Y.M., Wright T.L., and Omary M.B. Keratin 8 and 18 mutations are risk factors for developing liver disease of multiple etiologies. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 6063-6068
138. Loranger A., Duclos S., Grenier A., Price J., Wilson-Heiner M., Baribault H., and Marceau N. Simple epithelium keratins are required for maintenance of hepatocyte integrity. Am. J. Pathol. 151 (1997) 1673-1683
139. Ku N.-O., Michie S., Oshima R.G., and Omary M.B. Chronic hepatitis, hepatocyte fragility, and increased soluble phosphoglycokeratins in transgenic mice expressing a keratin 18 conserved arginine mutant. J. Cell Biol. 131 (1995) 1303-1314
140. Baribault H., Penner J., Iozzo R.V., and Wilson-Heiner M. Colorectal hyperplasia and inflammation in keratin 8-deficient FVB/N mice. Genes Dev. 8 (1994) 2964-2973
141. Habtezion A., Toivola D.M., Butcher E.C., and Omary M.B. Keratin-8-deficient mice develop chronic spontaneous Th2 colitis amenable to antibiotic treatment. J. Cell Sci. 118 (2005) 1971-1980
142. Ameen N.A., Figueroa Y., and Salas P.J. Anomalous apical plasma membrane phenotype in CK8-deficient mice indicates a novel role for intermediate filaments in the polarization of simple epithelia. J. Cell Sci. 114 (2001) 563-575
143. Toivola D.M., Krishnan S., Binder H.J., Singh S.K., and Omary M.B. Keratins modulate colonocyte electrolyte transport via protein mistargeting. J. Cell Biol. 164 (2004) 911-921
144. Colucci-Guyon E., Portier M.-M., Dunia I., Paulin D., Pournin S., and Babinet C. Mice lacking vimentin develop and reproduce without an obvious phenotype. Cell 79 (1994) 679-694
145. Milner D.J., Weitzer G., Tran D., Bradley A., and Capetanaki Y. Disruption of muscle architecture and myocardial degeneration in mice lacking desmin. J. Cell Biol. 134 (1996) 1255-1270
146. Li Z., Colucci-Guyon E., Pincon-Raymond M., Mericskay M., Pournin S., Paulin D., and Babinet C. Cardiovascular lesions and skeletal myopathy in mice lacking desmin. Dev. Biol. 175 (1996) 362-366
147. Liedtke W., Edelmann W., Bieri P.L., Chiu F.C., Cowan N.J., Kucherlapati R., and Raine C.S. GFAP is necessary for the integrity of CNS white matter architecture and long-term maintenance of myelination. Neuron 17 (1996) 607-615
148. Tamai Y., Ishikawa T.-O., Bosl M.R., Mori M., Nozaki M., Baribault H., Oshima R.G., and Taketo M.M. Cytokeratins 8 and 19 in the mouse placental development. J. Cell Biol. 151 (2000) 563-572
149. Zhu Q., Couillard-Despres S., and Julien J.P. Delayed maturation of regenerating myelinated axons in mice lacking neurofilaments. Exp. Neurol. 148 (1997) 299-316
150. Elder G.A., Friedrich Jr. V.L., Bosco P., Kang C., Gourov A., Tu P.H., Lee V.M., and Lazzarini R.A. Absence of the mid-sized neurofilament subunit decreases axonal calibers, levels of light neurofilament (NF-L), and neurofilament content. J. Cell Biol. 141 (1998) 727-739
151. Elder G.A., Friedrich Jr. V.L., Kang C., Bosco P., Gourov A., Tu P.H., Zhang B., Lee V.M., and Lazzarini R.A. Requirement of heavy neurofilament subunit in the development of axons with large calibers. J. Cell Biol. 143 (1998) 195-205
152. Li Z., Mericskay M., Agbulut O., Butler-Browne G., Carlsson L., Thornell L.E., Babinet C., and Paulin D. Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle. J. Cell Biol. 139 (1997) 129-144
153. Dalakas M.C., Park K.Y., Semino-Mora C., Lee H.S., Sivakumar K., and Goldfarb L.G. Desmin myopathy, a skeletal myopathy with cardiomyopathy caused by mutations in the desmin gene. N. Engl. J. Med. 342 (2000) 770-780
154. Eckes B., Colucci-Guyon E., Smola H., Nodder S., Babinet C., Krieg T., and Martin P. Impaired wound healing in embryonic and adult mice lacking vimentin. J. Cell Sci. 113 (2000) 2455-2462
155. Nieminen M., Henttinen T., Merinen M., Marttila-Ichihara F., Eriksson J.E., and Jalkanen S. Vimentin function in lymphocyte adhesion and transcellular migration. Nat. Cell Biol. 8 (2006) 156-162
156. Pekny M., Johansson C.B., Eliasson C., Stakeberg J., Wallen A., Perlmann T., Lendahl U., Betsholtz C., Berthold C.H., and Frisen J. Abnormal reaction to central nervous system injury in mice lacking glial fibrillary acidic protein and vimentin. J. Cell Biol. 145 (1999) 503-514
157. Magin T.M., Schroder R., Leitgeb S., Wanninger F., Zatloukal K., Grund C., and Melton D.W. 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. 140 (1998) 1441-1451
158. Kim S., Wong P., and Coulombe P.A. A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth. Nature 441 (2006) 362-365
159. Hutton E., Paladini R.D., Yu Q.-C., Yen M., Coulombe P.A., and Fuchs E. Functional differences between keratins of stratified and simple epithelia. J. Cell Biol. 143 (1998) 487-499
160. Kirfel J., Peters B., Grund C., Reifenberg K., and Magin T.M. Ectopic expression of desmin in the epidermis of transgenic mice permits development of a normal epidermis. Differentiation 70 (2002) 56-68
161. Harborth J., Elbashir S.M., Bechert K., Tuschl T., and Weber K. Identification of essential genes in cultured mammalian cells using small interfering RNAs. J. Cell Sci. 114 (2001) 4557-4565
162. Goldman R.D., Shumaker D.K., Erdos M.R., Eriksson M., Goldman A.E., Gordon L.B., Gruenbaum Y., Khuon S., Mendez M., Varga R., and Collins F.S. Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson-Gilford progeria syndrome. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 8963-8968
163. Sullivan T., Escalante-Alcalde D., Bhatt H., Anver M., Bhat N., Nagashima K., Stewart C.L., and Burke B. Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy. J. Cell Biol. 147 (1999) 913-920
164. Lammerding J., Schulze P.C., Takahashi T., Kozlov S., Sullivan T., Kamm R.D., Stewart C.L., and Lee R.T. Lamin A/C deficiency causes defective nuclear mechanics and mechanotransduction. J. Clin. Invest. 113 (2004) 370-378
165. Mounkes L., Kozlov S., Burke B., and Stewart C.L. The laminopathies: nuclear structure meets disease. Curr. Opin. Genet. Dev. 13 (2003) 223-230
166. Spann T.P., Goldman A.E., Wang C., Huang S., and Goldman R.D. Alteration of nuclear lamin organization inhibits RNA polymerase II-dependent transcription. J. Cell Biol. 156 (2002) 603-608
167. Shumaker D.K., Lopez-Soler R.I., Adam S.A., Herrmann H., Moir R.D., Spann T.P., and Goldman R.D. Functions and dysfunctions of the nuclear lamin Ig-fold domain in nuclear assembly, growth, and Emery-Dreifuss muscular dystrophy. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 15494-15499
168. Andrulis E.D., Neiman A.M., Zappulla D.C., and Sternglanz R. Perinuclear localization of chromatin facilitates transcriptional silencing. Nature 394 (1998) 592-595
169. He T., Stepulak A., Holmstrom T.H., Omary M.B., and Eriksson J.E. The intermediate filament protein keratin 8 is a novel cytoplasmic substrate for c-Jun N-terminal kinase. J. Biol. Chem. 277 (2002) 10767-10774
170. Liao J., and Omary M.B. 14-3-3 proteins associate with phosphorylated simple epithelial keratins during cell cycle progression and act as a solubility cofactor. J. Cell Biol. 133 (1996) 345-357
171. Ku N.-O., Liao J., and Omary M.B. Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteins. EMBO J. 17 (1998) 1892-1906
172. Lane E.B., Rugg E.L., Navsaria H., Leigh I.M., Heagerty A.H.M., Ishida-Yamamoto A., and Eady R.A.J. A mutation in the conserved helix termination peptide of keratin 5 in hereditary skin blistering. Nature 356 (1992) 236-244
173. Vassar R., Coulombe P.A., Degenstein L., Albers K., and Fuchs E. Mutant keratin expression in transgenic mice causes marked abnormalities resembling a human genetic skin disease. Cell 64 (1991) 365-380
174. Vassar R., Rosenberg M., Ross S., Tyner A., and Fuchs E. Tissue-specific and differentiation-specific expression of a human K14 keratin gene in transgenic mice. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 1563-1567
175. Chan Y., Anton-Lamprecht I., Yu Q., Jackel A., Zabel B., Ernst J., and Fuchs E. A human keratin 14 "knockout": the absence of K14 leads to severe epidermolysis bullosa simplex and a function for an intermediate filament protein. Genes Dev. 8 (1994) 2574-2587
176. Rothnagel J.A., Dominey A.M., Dempsey L.D., Longley M.A., Greenhalgh D.A., Gagne T.A., Huber M., Frenk E., Hohl D., and Roop D.R. Mutations in the rod domains of keratins 1 and 10 in epidermolytic hyperkeratosis. Science 257 (1992) 1128-1130
177. Cheng J., Syder A.J., Yu Q.C., Letai A., Paller A.S., and Fuchs E. The genetic basis of epidermolytic hyperkeratosis: a disorder of differentiation-specific epidermal keratin genes. Cell 70 (1992) 811-819
178. Chipev C.C., Korge B.P., Markova N., Bale S.J., DiGiovanna J.J., Compton J.G., and Steinert P.M. A leucine proline mutation in the H1 subdomain of keratin 1 causes epidermolytic hyperkeratosis. Cell 70 (1992) 821-828
179. Mattout A., Dechat T., Adam S.A., Goldman R.D., and Gruenbaum Y. Nuclear lamins, diseases and aging. Curr. Opin. Cell Biol. 18 (2006) 335-341
180. Fong L.G., Ng J.K., Lammerding J., Vickers T.A., Meta M., Cote N., Gavino B., Qiao X., Chang S.Y., Young S.R., Yang S.H., Stewart C.L., Lee R.T., Bennett C.F., Bergo M.O., and Young S.G. Prelamin A and lamin A appear to be dispensable in the nuclear lamina. J. Clin. Invest. 116 (2006) 743-752
181. Damjanov I., Clark R.K., and Andrews P.W. Expression of keratin polypeptides in human embryonal carcinoma cells, Intermediate Filaments. Ann. N.Y. Acad. Sci. 455 (1985) 732-733
182. Steinert P.M., Parry D.A.D., Racoosin E.L., Idler W.W., Steven A.C., Trus B.L., and Roop D.R. The complete cDNA and deduced amino acid sequence of a type II mouse epidermal keratin of 60,000 Da: analysis of sequence differences between type I and type II keratins. Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 5709-5713
183. Ichinose Y., Hashido K., Miyamoto H., Nagata T., Nozaki M., Morita T., and Matsushiro A. Molecular cloning and characterization of cDNA encoding mouse cytokeratin No. 19. Gene 80 (1989) 315-323
184. Langbein L., and Schweizer J. Keratins of the human hair follicle. Int. Rev. Cyt. 243 (2005) 1-78
185. Steinert P.M., Rice R.H., Roop D.R., Trus B.L., and Steven A.C. Complete amino acid sequence of a mouse epidermal keratin subunit and implications for the structure of intermediate filaments. Nature 302 (1983) 794-800
186. Jorcano J.L., Franz J.K., and Franke W.W. Amino acid sequence diversity between bovine epidermal cytokeratin polypeptides of the basic (type II) subfamily as determined from cDNA clones. Differentiation 28 (1984) 155-163
187. Winter H., Rogers M.A., Langbein L., Stevens H.P., Leigh I.M., Labreze C., Roul S., Taieb A., Krieg T., and Schweizer J. Mutations in the hair cortex keratin hHb6 cause the inherited hair disease monilethrix. Nat. Genet. 16 (1997) 372-374
188. Quax-Jeuken Y.E., Quax W.J., and Bloemendal H. Primary and secondary structure of hamster vimentin predicted from the nucleotide sequence. Proc. Natl. Acad. Sci. U. S. A. 80 (1983) 3548-3552
189. Lewis S.A., Balcarek J.M., Krek V., Shelanski M., and Cowan N.J. Sequence of a cDNA clone encoding mouse glial fibrillary acidic protein: structural conservation of intermediate filaments. Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 2743-2746
190. Julien J.P., Ramachandran K., and Grosveld F. Cloning of a cDNA encoding the smallest neurofilament protein from the rat. Biochim. Biophys. Acta 825 (1985) 398-404
191. Granger B.L., and Lazarides E. Synemin: a new high molecular weight protein associated with desmin and vimentin filaments in muscle. Cell 22 (1980) 727-738
192. Becker B., Bellin R.M., Sernett S.W., Huiatt T.W., and Robson R.M. Synemin contains the rod domain of intermediate filaments. Biochem. Biophys. Res. Commun. 213 (1995) 796-802
193. Pachter J.S., and Liem R.K. alpha-Internexin, a 66-kD intermediate filament-binding protein from mammalian central nervous tissues. J. Cell Biol. 101 (1985) 1316-1322
194. Fliegner K.H., Ching G.Y., and Liem R.K. The predicted amino acid sequence of alpha-internexin is that of a novel neuronal intermediate filament protein. EMBO J. 9 (1990) 749-755
195. Levavasseur F., Zhu Q., and Julien J.P. No requirement of alpha-internexin for nervous system development and for radial growth of axons. Brain Res. Mol. Brain Res. 69 (1999) 104-112
196. Gerace L., Blum A., and Blobel G. Immunocytochemical localization of the major polypeptides of the nuclear pore complex-lamina fraction. Interphase and mitotic distribution. J. Cell Biol. 79 (1978) 546-566
197. Wolin S.L., Krohne G., and Kirschner M.W. A new lamin in Xenopus somatic tissues displays strong homology to human lamin A. EMBO J. 6 (1987) 3809-3818
198. Hoger T.H., Krohne G., and Franke W.W. Amino acid sequence and molecular characterization of murine lamin B as deduced from cDNA clones. Eur. J. Cell Biol. 47 (1988) 283-290
199. Merdes A., Brunkener M., Horstmann H., and Georgatos S.D. Filensin: a new vimentin-binding, polymerization-competent, and membrane-associated protein of the lens fiber cell. J. Cell Biol. 115 (1991) 397-410
200. Alizadeh A., Clark J., Seeberger T., Hess J., Blankenship T., and FitzGerald P.G. Targeted deletion of the lens fiber cell-specific intermediate filament protein filensin. Invest. Ophthalmol. Visual Sci. 44 (2003) 5252-5258
201. Merdes A., Gounari F., and Georgatos S.D. The 47-kD lens-specific protein phakinin is a tailless intermediate filament protein and an assembly partner of filensin. J. Cell Biol. 123 (1993) 1507-1516