Abstract
Intermediate filament (IF) proteins, actin, and tubulin are the troika of the eukaryotic cytoskeleton, in that fibrous polymers of these three classes of protein abound in virtually all kinds of cells. However, as our knowledge of their molecular properties grows, it is becoming increasingly apparent that IF proteins (Steinert & Roop, 1988) differ in many respects from actin (Pollard & Cooper, 1986) and tubulin (Kirschner & Mitchison, 1986), but have much in common with another important and long-studied component of the cytoskeleton, albeit one that is somewhat less ubiquitous - myosin (Harrington & Rodgers, 1984; Warrick & Spudich, 1987). It is the purpose of this contribution to summarize some recent lines of evidence emerging from biophysical and molecular biological experiments concerning both static and dynamic properties of IF proteins; to examine how far their resemblance to myosin extends; and to explore its implications for the functions - still rather vaguely defined - that are exercised by IF in cells.
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Steven, A.C., Mack, J.W., Trus, B.L., Bisher, M.E., Steinert, P.M. (1989). Structure and Assembly of Intermediate Filaments: Multi- Faceted, Myosin-like (But Non-Motile) Cytoskeletal Polymers. In: Aebi, U., Engel, J. (eds) Cytoskeletal and Extracellular Proteins. Springer Series in Biophysics, vol 3. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-73925-5_3
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DOI: https://doi.org/10.1007/978-3-642-73925-5_3
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