ArticlePloS one2013
A second tubulin binding site on the kinesin-13 motor head domain is important during mitosis.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- A kinesin-13 family kinesin in Trypanosoma brucei regulates cytokinesis and cytoskeleton morphogenesis by promoting microtubule bundling.PLoS pathogens · 2024Article
- The minus-end depolymerase KIF2A drives flux-like treadmilling of γTuRC-uncapped microtubules.The Journal of cell biology · 2023Article
- Structural insights into the mechanism of GTP initiation of microtubule assembly.Nature communications · 2023Article
- Flexible microtubule anchoring modulates the bi-directional motility of the kinesin-5 Cin8.Cellular and molecular life sciences : CMLS · 2021Article
- Parts list for a microtubule depolymerising kinesin.Biochemical Society transactions · 2018Review
- Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s.Nature communications · 2018Article
- Microtubule Tip Tracking by the Spindle and Kinetochore Protein Ska1 Requires Diverse Tubulin-Interacting Surfaces.Current biology : CB · 2017Article
- Review
- Article
- Distinct Interaction Modes of the Kinesin-13 Motor Domain with the Microtubule.Biophysical journal · 2016Article
- HX-MS2 for high performance conformational analysis of complex protein states.Protein science : a publication of the Protein Society · 2015Article
- Article
- Mass spec studio for integrative structural biology.Structure (London, England : 1993) · 2014Article
- Nucleotide exchange in dimeric MCAK induces longitudinal and lateral stress at microtubule ends to support depolymerization.Structure (London, England : 1993) · 2014Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Kinesin-13s are microtubule (MT) depolymerases different from most other kinesins that move along MTs. Like other kinesins, they have a motor or head domain (HD) containing a tubulin and an ATP binding site. Interestingly, kinesin-13s have an additional binding site (Kin-Tub-2) on the opposite side of the HD that contains several family conserved positively charged residues. The role of this site in kinesin-13 function is not clear. To address this issue, we investigated the in-vitro and in-vivo effects of mutating Kin-Tub-2 family conserved residues on the Drosophila melanogaster kinesin-13, KLP10A. We show that the Kin-Tub-2 site enhances tubulin cross-linking and MT bundling properties of KLP10A in-vitro. Disruption of the Kin-Tub-2 site, despite not having a deleterious effect on MT depolymerization, results in abnormal mitotic spindles and lagging chromosomes during mitosis in Drosophila S2 cells. The results suggest that the additional Kin-Tub-2 tubulin biding site plays a direct MT attachment role in-vivo.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.