Kif2C Minimal Functional Domain Has Unusual Nucleotide Binding Properties That Are Adapted to Microtubule Depolymerization

The kinesin-13 Kif2C hydrolyzes ATP and uses the energy released to disassemble microtubules. The mechanism by which this is achieved remains elusive. Here we show that Kif2C-(sN+M), a monomeric construct consisting of the motor domain with the proximal part of the N-terminal Neck extension but devo...

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Bibliografiska uppgifter
Huvudupphovsmän: Wang, Weiyi, Jiang, Qiyang, Argentini, Manuela, Cornu, David, Gigant, Benoît, Knossow, Marcel, Wang, Chunguang
Materialtyp: Artigo
Språk:Inglês
Publicerad: American Society for Biochemistry and Molecular Biology 2012
Ämnen:
Enzymology
Länkar:https://ncbi.nlm.nih.gov/pmc/articles/PMC3340219/
https://ncbi.nlm.nih.gov/pubmed/22403406
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.317859
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