Structural diversity and dynamics of microtubules and polymorphic tubulin assemblies.
Tubulin, the main protein of microtubules (MTs), has the potency of forming a variety of other assembly products in vitro: rings, ring-crystals, C- and S-shaped ribbons, 10 nm fibres, hoops, sheets, heaped sheets, MT doublets, MT triplets, double-wall MTs, microtubules, curled ribbons, and paracrystals. The supramolecular subunits of all of them are the protofilaments which might be arranged either parallel to the axis (e.g., in MTs, ribbons) or curved (e.g., in hoops, microtubules). There is strong evidence that in the second case the protofilaments have an inside-out orientation compared to MTs. All assembly products mentioned are described structurally and their relevance to the in vivo situation is considered. Moreover, MTs and the other assemblies undergo permanent changes. These dynamics occurring in both individual assemblies and assembly populations are discussed from the structural point of view.
Unger
E
E
Academy of Sciences of the G.D.R., Central Institute of Microbiology and Experimental Therapy, Jena.
Böhm
K J
KJ
Vater
W
W
D000818:Animals; D006801:Humans; D008854:Microscopy, Electron; D008870:Microtubules / Q000502:physiology / Q000648:ultrastructure*; D014404:Tubulin / Q000502:physiology / Q000648:ultrastructure*
D014404:Tubulin