Catalysis of the microtubule on-rate is the major parameter regulating the depolymerase activity of MCAK
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The kinesin-13, MCAK, is a critical regulator of microtubule dynamics in eukaryotic cells. We have functionally dissected the structural features responsible for MCAK's potent microtubule depolymerization activity. MCAK's positively charged neck enhances its delivery to microtubule ends not by tethering the molecule to microtubules during diffusion, as commonly thought, but by catalyzing the association of MCAK to microtubules. On the other hand, this same positively charged neck slightly diminishes MCAK's ability to remove tubulin subunits once at the microtubule end. Conversely, dimerization reduces MCAK delivery but improves MCAK's ability to remove tubulin subunits. The reported kinetics for these events predicts a nonspecific binding mechanism that may represent a paradigm for the diffusive interaction of many microtubule-binding proteins.
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The diffusion coefficient of GFP-MCAK on dynamic microtubules is comparable to that previously observed for the same GFP-MCAK preparation on Taxol-stabilized microtubules.
“the diffusion coefficient of GFP-MCAK on dynamic MTs ( w 0.05 m m 2 3 s 2 1 ) was comparable to the one previously observed for the same GFP-MCAK preparation on Taxol-stabilized MTs ( w 0.08 m m 2 3 s 2 1 ) [11]”
From In vitro reconstitution of the functional interplay between MCAK and EB3 at microtubule plus ends (2010) · cites this paper as [11]
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References 32 · Cited by 95
- Authors
- Cooper, J. R., Wagenbach, M., Asbury, C. L., & Wordeman, L.
- Affiliations
- University of Washington (US)
- Corresponding author
- Wordeman, Linda
- Venue
- Nature Structural & Molecular Biology
- Published
- 2009-12-06
- Volume
- 17
- Issue
- 1
- Pages
- 77-82
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC2909650
- OpenAlex
- W2093088276
- Cited by
- 95
- References
- 32
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 4 · 2023: 6 · 2022: 4 · 2021: 1 · 2020: 2 · 2019: 2 · 2018: 6 · 2017: 9 · 2016: 12 · 2015: 10 · 2014: 9 · 2013: 5 · 2012: 3
- FWCI
- 2.52
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (GM069429, R01GM079373, R01GM069429)
- 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 › Biophysics › Advanced Fluorescence Microscopy Techniques
- Keywords
- MCAK, kinesin-13, microtubule depolymerization, microtubule dynamics, mitotic kinesin, protein dimerization, non-specific binding, microtubule-binding protein, single-molecule kinetics
- MeSH terms
- Animals, Catalysis, Cricetulus, Cricetinae, Image Processing, Computer-Assisted, Kinetics, Microscopy, Fluorescence, Microtubules, Mutation, Protein Binding, Tubulin, Kinesins, Protein Structure, Tertiary, Dimerization, Photobleaching
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