Microtubule interaction site of the kinesin motor
Open accessAbstract
Kinesin and myosin are motor proteins that share a common structural core and bind to microtubules and actin filaments, respectively. While the actomyosin interface has been well studied, the location of the microtubule-binding site on kinesin has not been identified. Using alanine-scanning mutagenesis, we have found that microtubule-interacting kinesin residues are located in three loops that cluster in a patch on the motor surface. The critical residues are primarily positively charged, which is consistent with a primarily electrostatic interaction with the negatively charged tubulin molecule. The core of the microtubule-binding interface resides in a highly conserved loop and helix (L12/alpha5) that corresponds topologically to the major actin-binding domain of myosin. Thus, kinesin and myosin have developed distinct polymer-binding domains in a similar region with respect to their common catalytic cores.
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KIF1C E170A was able to protect the Golgi ribbon.
“KIF1C E170A, mutated in a conserved kinesin microtubule binding site (Woehlke et al., 1997; Grant et al., 2011), was also able to protect the Golgi ribbon.”
From The Rab6-regulated KIF1C kinesin motor domain contributes to Golgi organization (2015) · cites this paper as Woehlke et al., 1997
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- Authors
- Woehlke, G., Ruby, A. K., Hart, C. L., Ly, B., Hom-Booher, N., & Vale, R. D.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Vale, Ronald D
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-07
- Volume
- 90
- Issue
- 2
- Pages
- 207-216
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2166088282
- Cited by
- 386
- References
- 57
- Citations by year
- 2026: 6 · 2025: 12 · 2024: 8 · 2023: 12 · 2022: 12 · 2021: 18 · 2020: 11 · 2019: 8 · 2018: 7 · 2017: 14 · 2016: 5 · 2015: 16 · 2014: 12 · 2013: 14 · 2012: 11
- FWCI
- 8.54
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR-42895, P01AR042895)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- kinesin, microtubule-binding site, motor proteins, myosin, actin-binding domain, tubulin, electrostatic interactions, protein-protein interaction, alanine scanning
- MeSH terms
- Adenosine Triphosphatases, Bacterial Proteins, Escherichia coli, Microtubules, Protein Binding, Mutagenesis, Site-Directed, Kinesins, Protein Structure, Tertiary
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