ArticleThe EMBO journal2011
The kinesin-13 MCAK has an unconventional ATPase cycle adapted for microtubule depolymerization.
Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 88 citations in OpenAlex.
- Article
- Factors Determining Kinesin Motors in a Predominant One-Head-Bound or Two-Heads-Bound State During Its Stepping Cycle.Biomolecules · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Modeling study of kinesin-13 MCAK microtubule depolymerase.European biophysics journal : EBJ · 2024Article
- CSPP1 stabilizes microtubules by capping both plus and minus ends.Journal of molecular cell biology · 2024Article
- Competition between physical search and a weak-to-strong transition rate-limits kinesin binding times.PLoS computational biology · 2024Article
- ADP release can explain spatially-dependent kinesin binding times.bioRxiv : the preprint server for biology · 2023Article
- A synthetic ancestral kinesin-13 depolymerizes microtubules faster than any natural depolymerizing kinesin.Open biology · 2022Article
- Kinetics of ATP/ADP binding to the gp16 ATPase.Biophysical journal · 2022Article
- The molecular biology of tubulinopathies: Understanding the impact of variants on tubulin structure and microtubule regulation.Frontiers in cellular neuroscience · 2022Review
- Impact of the 'tubulin economy' on the formation and function of the microtubule cytoskeleton.Current opinion in cell biology · 2021Review
- How Kinesin-1 Utilize the Energy of Nucleotide: The Conformational Changes and Mechanochemical Coupling in the Unidirectional Motion of Kinesin-1.International journal of molecular sciences · 2020Review
- These motors were made for walking.Protein science : a publication of the Protein Society · 2020Review
- Functional characterization of MCAK/Kif2C cancer mutations using high-throughput microscopic analysis.Molecular biology of the cell · 2020Article
- Kinesin-5 Promotes Microtubule Nucleation and Assembly by Stabilizing a Lattice-Competent Conformation of Tubulin.Current biology : CB · 2019Article
- Identification of key residues that regulate the interaction of kinesins with microtubule ends.Cytoskeleton (Hoboken, N.J.) · 2019Article
- Interplay between the Kinesin and Tubulin Mechanochemical Cycles Underlies Microtubule Tip Tracking by the Non-motile Ciliary Kinesin Kif7.Developmental cell · 2019Article
- Co-expression network analysis identified KIF2C in association with progression and prognosis in lung adenocarcinoma.Cancer biomarkers : section A of Disease markers · 2019Article
- Parts list for a microtubule depolymerising kinesin.Biochemical Society transactions · 2018Review
- Ternary complex of Kif2A-bound tandem tubulin heterodimers represents a kinesin-13-mediated microtubule depolymerization reaction intermediate.Nature communications · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Unlike other kinesins, members of the kinesin-13 subfamily do not move directionally along microtubules but, instead, depolymerize them. To understand how kinesins with structurally similar motor domains can have such dissimilar functions, we elucidated the ATP turnover cycle of the kinesin-13, MCAK. In contrast to translocating kinesins, ATP cleavage, rather than product release, is the rate-limiting step for ATP turnover by MCAK; unpolymerized tubulin and microtubules accelerate this step. Further, microtubule ends fully activate the ATPase by accelerating the exchange of ADP for ATP. This tuning of the cycle adapts MCAK for its depolymerization activity: lattice-stimulated ATP cleavage drives MCAK into a weakly bound nucleotide state that reaches microtubule ends by diffusion, and end-specific acceleration of nucleotide exchange drives MCAK into a strongly bound state that promotes depolymerization. This altered cycle accounts well for the different mechanical behaviour of this kinesin, which depolymerizes microtubules from their ends, compared to translocating kinesins that walk along microtubules. Thus, the kinesin motor domain is a nucleotide-dependent engine that can be differentially tuned for transport or depolymerization functions.
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