Review: postchaperonin tubulin folding cofactors and their role in microtubule dynamics.

摘要: The microtubule cytoskeleton consists of a highly organized network polymers bound to their accessory proteins: microtubule-associated proteins, molecular motors, and microtubule-organizing proteins. subunits are heterodimers composed one alpha-tubulin polypeptide beta-tubulin that should undergo complex folding processing before they achieve quaternary structure will allow incorporation into the polymer. Due extremely high protein concentration exists at cell cytoplasm, there alpha- interacting proteins prevent unwanted interaction these polypeptides with surrounding pool during folding, thus allowing dynamics. Several years ago, development nondenaturing electrophoretic technique made it possible identify different tubulin intermediate complexes biogenesis in vitro. By means, cytosolic chaperonin containing TCP-1 (CCT or TriC) prefoldin have been demonstrated intervene through actin folding. Various other cofactors also identified along postchaperonin route now known additional roles such as participating synthesis, transport, storage beta-tubulin. future characterization tubulin-binding sites perhaps still unknown help chemicals could interfere modulating In this paper, current knowledge above cofactors, which fact chaperones involved heterodimer achievement, be reviewed.