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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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| Main Authors: | , , , , , , |
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| 格式: | Artigo |
| 語言: | Inglês |
| 出版: |
American Society for Biochemistry and Molecular Biology
2012
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| 主題: | |
| 在線閱讀: | 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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