Polymorphic Assemblies of Tubulin

Paul R. Burton
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Paul R. Burton: University of Kansas, Department of Physiology and Cell Biology

Chapter 8 in Cell and Muscle Motility, 1981, pp 289-333 from Springer

Abstract: Abstract This chapter does not deal directly with cell motility as such; rather, it focuses on various structural manifestations of tubulin, the constituent protein of microtubules. Microtubules are important components of the cytoskeleton of cells, and only recently have we begun to perceive the associations between microtubules and other components of the cytoskeleton, such as actin (Griffith and Pollard, 1978; Fujii and Tanaka, 1979). There are several reasons that polymorphic assemblies of tubulin are of interest. First, determining how such structures are formed (e.g., under what conditions) and into what they might be transformed would provide information on the assembly potential of the tubulin dimer, either with or without the associated proteins that copurify with tubulin. Second, by studying the arrangement of dimers in tubulin polymorphs, information can be obtained on the various kinds of binding interactions between dimers and possible conformational states of the molecule. The kinds of structures that can be formed, and their stability, can provide clues to the tubulin polymorphs that may exist in vivo in normal and diseased or aged cells, even though there is always uncertainty associated with the degree to which the behavior of tubulin in vitro can be extrapolated to its behavior in vivo in the cytoplasmic milieu of the living cell.

Keywords: Vinca Alkaloid; Microtubule Assembly; Tubulin Dimer; Ribbon Structure; Tubulin Assembly (search for similar items in EconPapers)
Date: 1981
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DOI: 10.1007/978-1-4684-8196-9_8

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