Lucky 13-microtubule depolymerisation by kinesin-13 motors
Abstract
The kinesin-13 class of motors catalyses microtubule depolymerisation by bending tubulins at microtubule ends. Depolymerisation activity is intrinsic to the kinesin-13 motor core but the activity of the core alone is very low compared with that of constructs that also contain a conserved neck sequence. The full-length dimeric motor is an efficient depolymeriser and also diffuses along the microtubule lattice, which helps it to find microtubule ends. Current evidence supports the idea of a generic mechanism for kinesin-13-catalysed depolymerisation. However, the activity of kinesin-13 motors is precisely localised and regulated in vivo to enable a wide range of cellular roles. The proteins are involved in global control of microtubule dynamics. They also localise to mitotic and meiotic spindles, where they contribute to formation and maintenance of spindle bipolarity, chromosomal congression, attachment correction and chromatid separation. In interphase cells, intricate and subtle mechanisms appear to allow kinesin-13 motors to act on specific populations of microtubules. Such carefully controlled localisation and regulation makes these kinesins efficient, multi-tasking molecular motors.
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MCAK is a potent microtubule depolymerase.
“The kinesin-13 family member mitotic centromere-associated kinesin (MCAK) is a potent microtubule depolymerase [1-4].”
From In vitro reconstitution of the functional interplay between MCAK and EB3 at microtubule plus ends (2010) · cites this paper as [4]
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References 77 · Cited by 92
- Authors
- Moores, C. A., & Milligan, R. A.
- Affiliations
- Birkbeck, University of London (GB)
- Scripps Research Institute (US)
- ORCID
- Moores, Carolyn A.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2006-10-01
- Volume
- 119
- Issue
- 19
- Pages
- 3905-3913
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2013110453
- Cited by
- 92
- References
- 77
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 1 · 2023: 5 · 2022: 3 · 2021: 4 · 2020: 3 · 2019: 6 · 2018: 4 · 2017: 4 · 2016: 2 · 2015: 5 · 2014: 5 · 2013: 5 · 2012: 4
- FWCI
- 0.58
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- BIROn (Birkbeck, University of London) (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (GM 52468)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Keywords
- kinesin-13, microtubule depolymerization, microtubule dynamics, microtubule ends, mitotic spindle, meiotic spindle, spindle bipolarity, molecular motors
- MeSH terms
- Amino Acid Sequence, Animals, Cell Division, Humans, Interphase, Microtubules, Models, Biological, Models, Molecular, Molecular Sequence Data, Polymers, Protein Binding, Tubulin, Kinesins, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Dimerization
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