Lazarides, E. Intermediate filaments as mechanical integrators of cellular space. Nature 283, 249–256 (1980).

Article  CAS  Google Scholar 

Fuchs, E. & Cleveland, D.W. A structural scaffolding of intermediate filaments in health and disease. Science 279, 514–519 (1998).

Article  CAS  Google Scholar 

Osborn, M. & Weber, K. Tumor diagnosis by intermediate filament typing: a novel tool for surgical pathology. Lab. Invest. 48, 372–394 (1983).

CAS  PubMed  Google Scholar 

Omary, M.B., Coulombe, P.A. & McLean, W.H.I. Intermediate filament proteins and their associated diseases. N. Engl. J. Med. 351, 2087–2100 (2004).

Article  CAS  Google Scholar 

Szeverenyi, I. et al. The Human Intermediate Filament Database: comprehensive information on a gene family involved in many human diseases. Hum. Mutat. 29, 351–360 (2008).

Article  CAS  Google Scholar 

Kim, S. & Coulombe, P.A. Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm. Genes Dev. 21, 1581–1597 (2007).

Article  CAS  Google Scholar 

Hanukoglu, I. & Fuchs, E. The cDNA sequence of a Type II cytoskeletal keratin reveals constant and variable structural domains among keratins. Cell 33, 915–924 (1983).

Article  CAS  Google Scholar 

Kim, S., Wong, P. & Coulombe, P.A. A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth. Nature 441, 362–365 (2006).

Article  CAS  Google Scholar 

Hatzfeld, M. & Weber, K. 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. 110, 1199–1210 (1990).

Article  CAS  Google Scholar 

Strelkov, S.V. et al. Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. EMBO J. 21, 1255–1266 (2002).

Article  CAS  Google Scholar 

Steinert, P.M., Marekov, L.N., Fraser, R.D. & Parry, D.A. Keratin intermediate filament structure. Crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly. J. Mol. Biol. 230, 436–452 (1993).

Article  CAS  Google Scholar 

Bernot, K.M., Lee, C.H. & Coulombe, P.A. A small surface hydrophobic stripe in the coiled-coil domain of type I keratins mediates tetramer stability. J. Cell Biol. 168, 965–974 (2005).

Article  CAS  Google Scholar 

Franke, W.W. et al. Monoclonal cytokeratin antibody recognizing a heterotypic complex: immunological probing of conformational states of cytoskeletal proteins in filaments and in solution. Exp. Cell Res. 173, 17–37 (1987).

Article  CAS  Google Scholar 

Aebi, U., Haner, M., Troncoso, J., Eichner, R. & Engel, A. Unifying principles in intermediate filament assembly. Protoplasma 145, 73–81 (1988).

Article  Google Scholar 

Sokolova, A.V. et al. Monitoring intermediate filament assembly by small-angle x-ray scattering reveals the molecular architecture of assembly intermediates. Proc. Natl. Acad. Sci. USA 103, 16206–16211 (2006).

Article  CAS  Google Scholar 

Goldie, K.N. et al. Dissecting the 3-D structure of vimentin intermediate filaments by cryo-electron tomography. J. Struct. Biol. 158, 378–385 (2007).

Article  CAS  Google Scholar 

Strelkov, S.V. et al. Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments. J. Mol. Biol. 306, 773–781 (2001).

Article  CAS  Google Scholar 

Strelkov, S.V., Schumacher, J., Burkhard, P., Aebi, U. & 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, 1067–1080 (2004).

Article  CAS  Google Scholar 

Krimm, I. et al. The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy. Structure 10, 811–823 (2002).

Article  CAS  Google Scholar 

Dhe-Paganon, S., Werner, E.D., Chi, Y.I. & Shoelson, S.E. Structure of the globular tail of nuclear lamin. J. Biol. Chem. 277, 17381–17384 (2002).

Article  CAS  Google Scholar 

Meier, M. et al. Vimentin coil 1A-A molecular switch involved in the initiation of filament elongation. J. Mol. Biol. 390, 245–261 (2009).

Article  CAS  Google Scholar 

Nicolet, S., Herrmann, H., Aebi, U. & Strelkov, S.V. Atomic structure of vimentin coil 2. J. Struct. Biol. 170, 369–376 (2010).

Article  CAS  Google Scholar 

Fuchs, E. Keratins and the skin. Annu. Rev. Cell Dev. Biol. 11, 123–153 (1995).

Article  CAS  Google Scholar 

Moll, R., Franke, W.W., Schiller, D.L., Geiger, B. & Krepler, R. The catalog of human cytokeratins: patterns of expression in normal epithelia, tumors and cultured cells. Cell 31, 11–24 (1982).

Article  CAS  Google Scholar 

Coulombe, P.A. & Fuchs, E. Elucidating the early stages of keratin filament assembly. J. Cell Biol. 111, 153–169 (1990).

Article  CAS  Google Scholar 

Lee, C.H. & Coulombe, P.A. Self-organization of keratin intermediate filaments into cross-linked networks. J. Cell Biol. 186, 409–421 (2009).

Article  CAS  Google Scholar 

Coulombe, P.A. et al. Point mutations in human keratin 14 genes of epidermolysis bullosa simplex patients: genetic and functional analyses. Cell 66, 1301–1311 (1991).

Article  CAS  Google Scholar 

Coulombe, P.A., Kerns, M.L. & Fuchs, E. Epidermolysis bullosa simplex: a paradigm for disorders of tissue fragility. J. Clin. Invest. 119, 1784–1793 (2009).

Article  CAS  Google Scholar 

Herrmann, H. & Aebi, U. Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular Scaffolds. Annu. Rev. Biochem. 73, 749–789 (2004).

Article  CAS  Google Scholar 

Parry, D.A., Fraser, R.D. & Squire, J.M. Fifty years of coiled-coils and alpha-helical bundles: a close relationship between sequence and structure. J. Struct. Biol. 163, 258–269 (2008).

Article  CAS  Google Scholar 

Vinson, C., Acharya, A. & Taparowsky, E.J. Deciphering B-ZIP transcription factor interactions in vitro and in vivo. Biochim. Biophys. Acta 1759, 4–12 (2006).

Article  CAS  Google Scholar 

Wu, K.C. et al. Coiled-coil trigger motifs in the 1B and 2B rod domain segments are required for the stability of keratin intermediate filaments. Mol. Biol. Cell 11, 3539–3558 (2000).

Article  CAS  Google Scholar 

Yasukawa, K., Sawamura, D., McMillan, J.R., Nakamura, H. & Shimizu, H. Dominant and recessive compound heterozygous mutations in epidermolysis bullosa simplex demonstrate the role of the stutter region in keratin intermediate filament assembly. J. Biol. Chem. 277, 23670–23674 (2002).

Article  CAS  Google Scholar 

Wilson, A.K., Coulombe, P.A. & Fuchs, E. The roles of K5 and K14 head, tail, and R/K L L E G E domains in keratin filament assembly in vitro. J. Cell Biol. 119, 401–414 (1992).

Article  CAS  Google Scholar 

Arslan, M., Qin, Z. & Buehler, M.J. Coiled-coil intermediate filament stutter instability and molecular unfolding. Comput. Methods Biomech. Biomed. Engin. 14, 483–489 (2011).

Article  Google Scholar 

Sun, T.T. & Green, H. Keratin filaments of cultured human epidermal cells. Formation of intermolecular disulfide bonds during terminal differentiation. J. Biol. Chem. 253, 2053–2060 (1978).

CAS  PubMed  Google Scholar 

Hennings, H. & Holbrook, K.A. Calcium regulation of cell-cell contact and differentiation of epidermal cells in culture. Exp. Cell Res. 143, 127–142 (1983).

Article  CAS  Google Scholar 

Feige, M.J. & Hendershot, L.M. Disulfide bonds in ER protein folding and homeostasis. Curr. Opin. Cell Biol. 23, 167–175 (2011).

Article  CAS  Google Scholar 

Chung, B.M., Murray, C.I., Van Eyk, J.E. & Coulombe, P.A. Identification of a novel interaction between Annexin A2 and Keratin 17: Evidence for reciprocal regulation. J. Biol. Chem. 287, 7573–7581 (2012).

Article  CAS  Google Scholar 

Crick, F.H. Is alpha-keratin a coiled coil? Nature 170, 882–883 (1952).

Article  CAS  Google Scholar 

O'Shea, E.K., Klemm, J.D., Kim, P.S. & Alber, T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254, 539–544 (1991).

Article  CAS  Google Scholar 

Herrmann, H., Häner, M., Brettel, M., Ku, N.O. & Aebi, U. Characterization of distinct early assembly units of different intermediate filament proteins. J. Mol. Biol. 286, 1403–1420 (1999).

Article  CAS  Google Scholar 

Norlen, L. & Al-Amoudi, A. Stratum corneum keratin structure, function, and formation: the cubic rod-packing and membrane templating model. J. Invest. Dermatol. 123, 715–732 (2004).

Article  CAS  Google Scholar 

Hashimoto, Y. et al. Immunohistochemical localization of sulfhydryl oxidase correlates with disulfide crosslinking in the upper epidermis of rat skin. Arch. Dermatol. Res. 292, 570–572 (2000).

Article  CAS  Google Scholar 

Lyle, S. et al. The C8/144B monoclonal antibody recognizes cytokeratin 15 and defines the location of human hair follicle stem cells. J. Cell Sci. 111, 3179–3188 (1998).

CAS  PubMed  Google Scholar 

Troy, T.C. & Turksen, K. In vitro characteristics of early epidermal progenitors isolated from keratin 14 (K14)-deficient mice: insights into the role of keratin 17 in mouse keratinocytes. J. Cell. Physiol. 180, 409–421 (1999).

Article  CAS  Google Scholar 

Dupin, I., Sakamoto, Y. & Etienne-Manneville, S. Cytoplasmic intermediate filaments mediate actin-driven positioning of the nucleus. J. Cell Sci. 124, 865–872 (2011).

Article  CAS  Google Scholar 

Arnesano, F. et al. The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status. J. Biol. Chem. 279, 47998–48003 (2004).

Article  CAS  Google Scholar 

Meister, A. & Anderson, M.E. Glutathione. Annu. Rev. Biochem. 52, 711–760 (1983).

Article  CAS  Google Scholar 

Ostergaard, H., Tachibana, C. & Winther, J.R. Monitoring disulfide bond formation in the eukaryotic cytosol. J. Cell Biol. 166, 337–345 (2004).

Article  CAS  Google Scholar 

Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. in Methods in Enzymology, Macromolecular Crystallography Part A Vol. 276 (eds., Carter, C.W. Jr. & Sweet, R.M.) 307–326 (Academic Press, New York, 1997).

Terwilliger, T.C. SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol. 374, 22–37 (2003).

Article  CAS  Google Scholar 

Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126–2132 (2004).

Article  Google Scholar 

Adams, P.D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213–221 (2010).

Article  CAS  Google Scholar 

Davis, I.W. et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35, W375–W383 (2007).

Article  Google Scholar 

Wallace, A.C., Laskowski, R.A. & Thornton, J.M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127–134 (1995).

Article  CAS  Google Scholar 

Eswar, N. et al. Comparative Protein Structure Modeling with MODELLER. in Current Protocols in Bioinformatics (suppl. 15) 5.6.1–5.6.30 (John Wiley & Sons, Inc., 2006).

Baker, N.A., Sept, D., Joseph, S., Holst, M.J. & McCammon, J.A. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl. Acad. Sci. USA 98, 10037–10041 (2001).

Article  CAS  Google Scholar 

Pang, Y.Y., Schermer, A., Yu, J. & Sun, T.T. Suprabasal change and subsequent formation of disulfide-stabilized homo- and hetero-dimers of keratins during esophageal epithelial differentiation. J. Cell Sci. 104, 727–740 (1993).

PubMed  Google Scholar 

Lloyd, C. et al. The basal keratin network of stratified squamous epithelia: defining K15 function in the absence of K14. J. Cell Biol. 129, 1329–1344 (1995).

Article  CAS  Google Scholar