Chapter 13
13.2 Similarities in structure define the intermediate filament family
Review
Steinert, P. M., and Parry, D. A., 1985. Intermediate filaments: conformity and diversity
of expression and structure. Annu. Rev. Cell Biol. v. 1 p. 41–65.
Research
Sun, T. T., Eichner, R., Nelson, W. G., Tseng, S. C., Weiss, R. A., Jarvinen, M., and
Woodcock-Mitchell, J., 1983. Keratin classes: molecular markers for different
types of epithelial differentiation. J. Invest. Dermatol. v. 81 p. 109s–115s.
Moll, R., Franke, W. W., Schiller, D. L., Geiger, B., and Krepler, R., 1982. The catalogue
of human cytokeratin polypeptides: Patterns of expression of specific cytokeratins
in normal epithelia, tumors and cultured cells. Cell v. 31 p. 11–24.
Hatzfeld, M., and Weber, K., 1990. The coiled coil of in vitro assembled keratin
filaments is a heterodimer of type I and II keratins: Use of site–specific
mutagenesis and recombinant protein expression. J. Cell Biol. v. 110 p. 1199–
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Lu, X., and Lane, E. B., 1990. Retrovirus–mediated transgenic keratin expression in
cultured fibroblasts: Specific domain functions in keratin stabilization and
filament formation. Cell v. 62 p. 681–696.
Rogers, M. A., Winter, H., Langbein, L., Bleiler, R., and Schweizer, J., 2004. The human
type I keratin gene family: Characterization of new hair follicle specific members
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527–540.
Rogers, M. A., Edler, L., Winter, H., Langbein, L., Beckmann, I., and Schweizer, J.,
2005. Characterization of new members of the human type II keratin gene family
and a general evaluation of the keratin gene domain on chromosome 12q13.13. J.
Invest.
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13.3 Intermediate filament subunits assemble with high affinity into strain–resistant
structures
Review
Fuchs, E., and Cleveland, D. W., 1998. A structural scaffolding of intermediate filaments
in health and disease. Science v. 279 p. 514–519.
Herrmann, H., Hesse, M., Reichenzeller, M., Aebi, U., and Magin, T. M., 2003.
Functional complexity of intermediate filament cytoskeletons: from structure to
assembly to gene ablation. Int. Rev. Cytol. v. 223 p. 83–175.
Research
Crick, F. H. C., 1952. Is alpha–keratin a coiled coil? Nature v. 170 p. 882–883.
Janmey, P. A., Euteneuer, U., Traub, P., and Schliwa, M.,1991. Viscoelastic properties of
vimentin compared with other filamentous biopolymer networks. J. Cell Biol. v.
113 p. 155–160.
Ma, L., Xu, J., Coulombe, P. A., and Wirtz, D., 1999. Keratin filament suspensions show
unique micromechanical properties. J. Biol. Chem. v. 274 p. 19145–19151.
13.4 Two-thirds of all intermediate filament proteins are keratins
Review
Coulombe, P. A., and Omary, M. B., 2002. ‘Hard’ and ‘soft’ principles defining the
structure, function and regulation of keratin intermediate filaments. Curr. Opin.
Cell Biol. v. 14 p. 110–122.
Lane, E. B., and Alexander, C. M., 1990. Use of keratin antibodies in tumor diagnosis.
Semin. Cancer Biol. v. 1 p. 165–179.
Research
Sun, T. T., Eichner, R., Nelson, W. G., Tseng, S. C., Weiss, R. A., Jarvinen, M., and
Woodcock–Mitchell, J., 1983. Keratin classes: molecular markers for different
types of epithelial differentiation. J. Invest. Dermatol. v. 81 p. 109s–115s.
Moll, R., Franke, W. W., Schiller, D. L., Geiger, B., and Krepler, R., 1982. The catologue
of human cytokeratin polypeptides: Patterns of expression of specific cytokeratins
in normal epithelia, tumors and cultured cells. Cell v. 31 p. 11–24.
Purkis, P. E., Steel, J. B., Mackenzie, I. C., Nathrath, W. B., Leigh, I. M., and Lane,
E. B., 1990. Antibody markers of basal cells in complex epithelia. J. Cell Sci. v.
97 p. 39–50.
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., 2006.
New consensus nomenclature for mammalian keratins. J. Cell Biol. v. 174 p. 169–
174.
13.5 Mutations in keratins cause epithelial fragility
Review
Fuchs, E., and Cleveland, D. W., 1998. A structural scaffolding of intermediate filaments
in health and disease. Science v. 279 p. 514–519.
Owens, D. W., and Lane, E. B., 2004. Keratin mutations and intestinal pathology. J.
Pathol. v. 204 p. 377–385.
Irvine, A. D., and McLean, W. H. I., 1999. Human keratin diseases: The increasing
spectrum of disease and subtlety of the phenotype–genotype correlation. Br. J.
Dermatol. v. 140 p. 815–828.
Omary, M. B., Coulombe, P. A., and McLean, W. H. (2004). Intermediate filament
proteins and their associated diseases. N. Engl. J. Med. v. 351 p. 2087–2100.
Research
Bonifas, J. M., Rothman, A. L., and Epstein, E. H., Jr., 1991. Epidermolysis bullosa
simplex: Evidence in two families for keratin gene abnormalities. Science v. 254
p. 1202–1205.
Coulombe, P. A., Hutton, M. E., Letai, A., Hebert, A., Paller, A. S., and Fuchs, E., 1991.
Point mutations in human keratin 14 genes of epidermolysis bullosa simplex
patients: Genetic and functional analyses. Cell v. 66 p. 1301–1311.
Lane, E. B., Rugg, E. L., Navsaria, H., Leigh, I. M., Heagerty, A. H., Ishida–Yamamoto,
A., and Eady, R. A., 1992. A mutation in the conserved helix termination peptide
of keratin 5 in hereditary skin blistering. Nature v. 356 p. 244–246.
Owens, D. W., Wilson, N. J., Hill, A. J., Rugg, E. L., Porter, R. M., Hutcheson, A. M.,
Quinlan, R. A., van Heel, D., Parkes, M., Jewell, D. P., et al., 2004. Human
keratin 8 mutations that disturb filament assembly observed in inflammatory
bowel disease patients. J. Cell Sci. v. 117 p. 1989–1999.
Ku, N. O., Gish, R., Wright, T. L., and Omary, M. B., 2001. Keratin 8 mutations in
patients with cryptogenic liver disease. N. Engl. J. Med. v. 344 p. 1580–1587.
13.6 Intermediate filaments of nerve, muscle, and connective tissue often show
overlapping expression
Review
Magin, T. M., Reichelt, J., and Hatzfeld, M., 2004. Emerging functions: Diseases and
animal models reshape our view of the cytoskeleton. Exp. Cell Res. v. 301
p. 91–102.
Al–Chalabi, A., and Miller, C. C., 2003. Neurofilaments and neurological disease.
Bioessays v. 25 p. 346–355.
Cairns, N. J., Lee, V. M., and Trojanowski, J. Q., 2004. The cytoskeleton in
neurodegenerative diseases. J. Pathol. v. 204 p. 438–449.
Lane, E. B., and Pekny, M. (2004). Stress models for the study of intermediate filament
function. Methods Cell Biol. v. 78 p. 229–264.
Research
Hesse, M., Magin, T. M., and Weber, K., 2001. 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. v. 114 p. 2569–2575.
Balogh, J., Merisckay, M., Li, Z., Paulin, D., and Arner, A., 2002. Hearts from mice
lacking desmin have a myopathy with impaired active force generation and
unaltered wall compliance. Cardiovasc. Res. v. 53 p. 439–450.
Weisleder, N., Taffet, G. E., and Capetanaki, Y., 2004. Bcl–2 overexpression corrects
mitochondrial defects and ameliorates inherited desmin null cardiomyopathy.
Proc. Natl. Acad. Sci. U.S.A. v. 101 p. 769–774.
Pekny, M., Johansson, C. B., Eliasson, C., Stakeberg, J., Wallen, A., Perlmann, T.,
Lendahl, U., Betsholtz, C., Berthold, C. H., and Frisen, J. 1999. Abnormal
reaction to central nervous system injury in mice lacking glial fibrillary acidic
protein and vimentin. J. Cell Biol. v. 145 p. 503–514.
13.7 Lamin intermediate filaments reinforce the nuclear envelope
Review
Mattout, A., Dechat, T., Adam, S. A., Goldman, R. D., Gruenbaum, Y., 2006. Nuclear
lamins, diseases and aging. Curr. Opin. Cell Biol. v. 18 p. 335–341.
Burke, B., and Stewart, C. L., 2006. The laminopathies: the functional architecture of the
nucleus and its contribution to disease. Ann. Rev. Genom. Hum. Genet. v. 7 p.
369-405.
Smith, E. D., Kudlow, B. A., Frock, R. L., and Kennedy, B. K., 2005. A–type nuclear
lamins, progerias and other degenerative disorders. Mech. Ageing Dev. v. 126
p. 447–460.
Broers, J. L., Ramaekers, F. C., Bonne, G., Yaou, R. B., and Hutchison, C. J., 2006.
Nuclear lamins: Laminopathies and their role in premature ageing. Physiol. Rev.
v. 86 p. 967–1008.
Broers, J. L., Hutchison, C. J., and Ramaekers, F. C., 2004. Laminopathies. J. Pathol. v.
204 p. 478–488.
Zastrow, M. S., Vlcek, S., and Wilson, K. L., 2004. Proteins that bind A–type lamins:
Integrating isolated clues. J. Cell Sci. v. 117 p. 979–987.
Research
Erber, A., Riemer, D., Bovenschulte, M., and Weber, K., 1998. Molecular phylogeny of
metazoan intermediate filament proteins. J. Mol. Evol. v. 47 p. 751–762.
Sullivan, T., Escalante-Alcalde, D., Bhatt, H., Anver, M., Bhat, N., Nagashima, K.,
Stewart, C. L., and Burke, B., 1999. Loss of A–type lamin expression
compromises nuclear envelope integrity leading to muscular dystrophy. J. Cell
Biol. v. 147 p. 913–920.
Vergnes, L., Peterfy, M., Bergo, M. O., Young, S. G., Reue, K., 2004. Lamin B1 is
required for mouse development and nuclear integrity. Proc. Natl. Acad. Sci.
U.S.A. v. 101 p. 10428–10433.
13.8 Even the divergent lens filament proteins are conserved in evolution
Review
Perng, M. D., Sandilands, A., Kuszak, J., Dahm, R., Wegener, A., Prescott, A. R., and
Quinlan, R. A., 2004. The intermediate filament systems in the eye lens. Methods
Cell Biol. v. 78 p. 597–624.
Research
Zimek, A., Stick, R., and Weber, K. (2003). Genes coding for intermediate filament
proteins: Common features and unexpected differences in the genomes of humans
and the teleost fish Fugu rubripes. J. Cell Sci. 116, 2295–2302.
Conley, Y. P., Erturk, D., Keverline, A., Mah, T. S., Keravala, A., Barnes, L. R.,
Bruchis, A., Hess, J. F., FitzGerald, P. G., Weeks, D. E., Ferrell, R. E., and Gorin,
M. B., 2000. A juvenile-onset, progressive cataract locus on chromosome 3q2122 is associated with a missense mutations in the beaded filament structural
protein-2. Am. J. Hum. Genet. v. 66 p. 1426–1431.
Sandilands, A., Prescott, A. R., Wegener, A., Zoltoski, R. K., Hutcheson, A. M., Masaki,
S.,
Kuszak, J. R., and Quinlan, R. A., 2003. Knockout of the intermediate filament
proteins CP49 destabilises the lens fibre cell cytoskeleton and decreases lens
optical quality, but does not induce cataract. Exp. Eye Res. v. 76 p. 385–391.
13.9 Post-translational modifications regulate and remodel intermediate filament
networks
Review
Coulombe, P. A., and Omary, M. B., 2002. ‘Hard’ and ‘soft’ principles defining the
structure, function and regulation of keratin intermediate filaments. Curr. Opin.
Cell
Biol. v. 14 p. 110–122.
Omary, M. B., Ku, N. O., Liao, J., and Price, D., 1998. Keratin modifications and
solubility properties in epithelial cells and in vitro. Subcell. Biochem. v. 31 p.
105–140.
Omary, M. B., Ku, N. -O., Tao, G. Z., Toivola, D. M., Liao, J., 2006. ‘Heads and tails’ of
intermediate filament phosphorylation: Multiple sites and functional insights.
Trends Biochem. Sci. v. 31 p. 383–394.
Research
Inagaki, M., Gonda, Y., Matsuyama, M., Nishizawa, K., Nishi, Y., and Sato, C., 1988.
Intermediate filament reconstitution in vitro. The role of phosphorylation on the
assembly–disassembly of desmin. J. Biol. Chem. v. 263 p. 5970–5978.
Ku, N.–O., Fu, H., and Omary, M. B., 2004. Raf–1 activation disrupts its binding to
keratins during cell stress. J. Cell Biol. v. 166 p. 479–485.
13.10 Interacting proteins facilitate secondary functions of intermediate filaments
Review
Rezniczek, G. A., Janda, L., and Wiche, G., 2004. Plectin. Methods Cell Biol. v. 78 p.
721–755.
Ruhrberg, C., and Watt, F. M., 1997. The plakin family: Versatile organizers of
cytoskeletal architecture. Curr. Opin. Genet. Dev. v. 7 p. 392–397.
Hudson, T. Y., Fontao, L., Godsel, L. M., Choi, H. J., Huen, A. C., Borradori, L., Weis,
W. I., and Green, K. J. (2004). In vitro methods for investigating desmoplakin–
intermediate filament interactions and their role in adhesive strength. Methods
Cell Biol. v. 78 p. 757–786.
Research
Janda, L., Damborsky, J., Rezniczek, G. A., Wiche, G., 2001. Plectin repeats and
modules: Strategic cysteines and their presumed impact on cytolinker functions.
Bioessays. v. 23 p. 1064–1069.
Smith, F. J., Irvine, A. D., Terron-Kwiatkowski, A., Sandilands, A., Campbell, L. E.,
Zhao, Y., Liao, H., Evans, A. T., Goudie, D. R., Lewis-Jones, S., Arseculeratne,
G., Munro, C. S., Sergeant, A., O‘Regan, G., Bale, S. J., Compton, J. G.,
DiGiovanna, J. J., Presland, R. B., Fleckman, P., McLean, W. H., 2006. Loss-offunction mutations in the gene encoding filaggrin cause ichthyosis vulgaris. Nat.
Genet. v. 38 p. 337–342.
13.11 Intermediate filament genes are represented through metazoan evolution
Research
Erber, A., Riemer, D., Bovenschulte, M., and Weber, K., 1998. Molecular phylogeny of
metazoan intermediate filament proteins. J. Mol. Evol. v. 47 p. 751–762.
Karabinos, A., Zimek, A., and Weber, K., 2004. The genome of the early chordate Ciona
intestinalis encodes only five cytoplasmic intermediate filament proteins
including a single type I and type II keratin and a unique IF–annexin fusion
protein. Gene v. 326 p. 123–129.
Zimek, A., Stick, R., and Weber, K., 2003. Genes coding for intermediate filament
proteins: Common features and unexpected differences in the genomes of humans
and the teleost fish Fugu rubripes. J. Cell Sci. 116, 2295–2302.