The engine of microtubule dynamics comes into focus.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 24855939.
- Also identified by DOI 10.1016/j.cell.2014.05.001.
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Abstract
In this issue, Alushin et al. report high-resolution structures of three states of the microtubule lattice: GTP-bound, which is stable to depolymerization; unstable GDP-bound; and stable Taxol and GDP-bound. By comparing these structures at near-atomic resolution, they are able to propose a detailed model for how GTP hydrolysis destabilizes the microtubule and thus powers dynamic instability and chromosome movement. Destabilization of cytoskeleton filaments by nucleotide hydrolysis is an important general principle in cell dynamics, and this work represents a major step forward on a problem with a long history.
Medical subject headings
- Guanosine Triphosphate
- Microtubules
- Tubulin