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Microtubule structure and dynamics

1997; Elsevier BV; Volume: 9; Issue: 1 Linguagem: Inglês

10.1016/s0955-0674(97)80146-9

1879-0410

Richard H. Wade,

14-3-3 protein interactions

The study of microtubules always manages to surprise and fascinate us, and it has done so yet again over the past year as significant progress has been made in the areas of microtubule nucleation, growth and structural polarity. Microtubule nucleation has been the subject of publications that show the involvement of γ-tubulin-containing complexes as nucleating templates in the microtubule-organizing centre. It is unclear how this nucleation is compatible with microtubule growth, which appears to take place by an unusual, and perhaps unique, process involving sheet-like extensions that continuously close into tubes as growth proceeds. The related, and longstanding, problem is that of the relationship between tubulin dimer structure and microtubule polarity. This problem appears to be solved. A number of approaches have converged to suggest that the tubulin dimer is organized with β-tubulin pointing towards the microtubule fast-growing plus end and with α-tubulin towards the minus end. Specific decoration with kinesin monomers shows that all microtubules examined to date are basically organized as B-lattices.