The Engine of Microtubule Dynamics Comes into Focus | Zendy

Timothy J. Mitchison | Zendy

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The Engine of Microtubule Dynamics Comes into Focus

Author(s) -

Timothy J. Mitchison

Publication year - 2014

Publication title -

cell

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 26.304

H-Index - 776

eISSN - 1097-4172

pISSN - 0092-8674

DOI - 10.1016/j.cell.2014.05.001

Subject(s) - microtubule , biophysics , gtp' , mitosis , cytoskeleton , gtpase , tubulin , biology , motor protein , depolymerization , guanosine diphosphate , atp hydrolysis , microbiology and biotechnology , guanosine triphosphate , chemistry , cell , biochemistry , atpase , organic chemistry , enzyme

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.

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