The Structure, Complexity, and Evolution of Intermediate Filament Genes
The foregoing chapters in this book have directly or indirectly posed many fundamental questions pertaining to the mechanisms by which the expression of intermediate filament (IF) genes is regulated during development and differentiation. A consensual hypothesis established repeatedly in this book suggests that the morphological similarity of IF resides in the highly conserved secondary structure of the rod domains of all IF chains. The end domains, which vary widely in size and amino acid sequence among IF chains (Table I), are thought to occupy peripheral positions on intact IF where they are intimately involved in the functions of the IF in cells (Steinert et. al., 1985a; Steinert and Roop, 1988). Accordingly, the fundamental role of IF gene expression is to generate a particular set of exposed end domains, coupled to specific rod domains, that admit the functions of the IF required by the cell in which they occur.
KeywordsIntermediate Filament Heptad Repeat Keratin Gene Wool Keratin Peptide Repeat
Unable to display preview. Download preview PDF.
- Bowden, P. E., Blanchard, A., and Steinert, P. M., 1987, Linkage of epidermal keratin genes isolated on large cosmid clones, J. Invest. Dermatol. 88: 478.Google Scholar
- Ferrari, S., Cannizzaro, L. A., Battini, R., Huebner, K., and Baserga, R., 1987, The gene encoding human vimentin is located on the short arm of chromosome 10, Am. J. Human Genet. 41: 616–626.Google Scholar
- Romano, V., Bosco, P., Costa, G., Leube, R., Franke, W. W., Rochi, M., and Romeo, G., 1987, Chromosome assignment of cytokeratin genes, Cytogenet. Cell Genet. 46: 683.Google Scholar
- Savtchenko, E. S., Freedberg, I. M., and Blumenberg, M., 1987, Human keratin genes are linked, J. Invest. Dermatol. 88: 516.Google Scholar
- Steinert, P. M., Parry, D. A. D., Racoosin, E. L., Idler, W. W., Steven, A. C., Trus, B. L., and Roop, D. R., 1984, The complete cDNA and deduced amino acid sequence of a type II mouse epidermal keratin of 60,000 molecular weight: Analysis of sequence differences between type I and type II keratins, Proc. Natl. Acad. Sci. USA 81: 5709–5713.PubMedCrossRefGoogle Scholar
- Steinert, P. M., Parry, D. A. D., Idler, W. W., Johnson, L. D., Steven, A. C., and Roop, D. R., 1985b, Amino acid sequences of mouse and human epidermal type II keratins of Mr 67,000 provide a systematic basis for the structural and functional diversity of the end domains of keratin intermediate filament subunits, J. Biol. Chem. 260: 7442–7449.Google Scholar
- Sun, T.-T., Eichner, R., Schermer, A., Cooper, D., Nelson, W. G., and Weiss, R. A., 1984, Classification, expression and possible mechanisms of evolution of mammalian epithelial keratins: A unifying model, in: Cancer Cells 1: The Transformed Phenotype, Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y., pp. 169–176.Google Scholar
- Weber, K., and Geisler, N., 1984, Intermediate filaments—from wool α-keratin to neurofilaments: A structural overview, in: Cancer Cells 1: The Transformed Phenotype, Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y., pp. 153–159.Google Scholar