## Actin plays several essential roles in cdluiarprocesses and is a vital component in the contractile apparatus. To accomplish its many cellular tasks, actin must interact with a wide range of other proteins in addition to self-assembling into $laments. Characterization of these functional domains
Structural and functional domains of tubulin
โ Scribed by Ricardo B. Maccioni; Luis Serrano; Jesus Avila
- Book ID
- 102758285
- Publisher
- John Wiley and Sons
- Year
- 1985
- Tongue
- English
- Weight
- 667 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0265-9247
No coin nor oath required. For personal study only.
โฆ Synopsis
The molecular aspects of the microtubule system is a research area that has developed very rapidly during the past decade. Research on the assembly mechanisms and chemistry of tubulin and the molecular biology of microtubules have advanced our understanding of microtubule formation and its regulation. The emerging view of tubulin is of a macromolecule containing spatially discrete sequences that constitute functionally different domains with respect to sewassociation, interactions with microtubule associated proteins (MAPS) and specijic ligands. Recent studiespoint to the role of the carboxyl-terminal moiety of tubulin subunits in regulating its assembly into microtubules. These investigations combined with further studies on the spatial relationships between tubulin domains should provide new insights into the detailed structural basis of microtubule assembly.
๐ SIMILAR VOLUMES
The microtubule cytoskeleton has lagged nearly a decade behind the actin cytoskeleton with respect to structural information on the basic polymer subunit. This structural inferiority complex has finally been lifted by two recent papers describing the structures of the โฃโค tubulin dimer (1) and FtsZ,