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Single-molecule investigation of the interference between kinesin, tau and MAP2c
Open accessAbstract
Motor proteins and microtubule-associated proteins (MAPs) play important roles in cellular transport, regulation of shape and polarity of cells. While motor proteins generate motility, MAPs are thought to stabilize the microtubule tracks. However, the proteins also interfere with each other, such that MAPs are able to inhibit transport of vesicles and organelles in cells. In order to investigate the mechanism of MAP-motor interference in molecular detail, we have studied single kinesin molecules by total internal reflection fluorescence microscopy in the presence of different neuronal MAPs (tau, MAP2c). The parameters observed included run-length (a measure of processivity), velocity and frequency of attachment. The main effect of MAPs was to reduce the attachment frequency of motors. This effect was dependent on the concentration, the affinity to microtubules and the domain composition of MAPs. In contrast, once attached, the motors did not show a change in speed, nor in their run-length. The results suggest that MAPs can regulate motor activity on the level of initial attachment, but not during motion.
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“MAP2 has been shown to block the path of kinesin motors in in vitro assays (46, 47, 48, 49, 50).”
From Active transport by cytoplasmic dynein sustains dendritic MAP2 localization in developing neurons (2026) · cites this paper as [49]
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“Another indirect function is the inhibition of MT-dependent transport by motor proteins, which is based on the competition between motors (kinesin, dynein) and MAPs for binding sites on the MTsurface (Seitz et al. 2002; Stamer et al. 2002; Dixit et al. 2008).”
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Metadata
- Authors
- Seitz, A., Kojima, H., Oiwa, K., Mandelkow, E.-M., Song, Y.-H., & Mandelkow, E.
- Affiliations
- Max Planck Unit for Structural Molecular Biology (DE)
- Corresponding author
- Seitz, Arne
- Venue
- The EMBO Journal
- Published
- 2002-09-16
- Volume
- 21
- Issue
- 18
- Pages
- 4896-4905
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC126299
- OpenAlex
- W1968991344
- Cited by
- 257
- References
- 49
- Citations by year
- 2026: 3 · 2025: 12 · 2024: 4 · 2023: 5 · 2022: 5 · 2021: 8 · 2020: 8 · 2019: 12 · 2018: 7 · 2017: 15 · 2016: 11 · 2015: 12 · 2014: 18 · 2013: 10 · 2012: 12
- FWCI
- 3.04
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Desy publication database (The Deutsches Elektronen-Synchrotron) (submittedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Funders
- Deutsche Forschungsgemeinschaft
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- kinesin, tau protein, MAP2c, microtubule-associated proteins, microtubule stabilization, single-molecule tracking, total internal reflection fluorescence microscopy, run length, processivity, motor speed, neuronal transport
- MeSH terms
- Adenosine Triphosphatases, Animals, Biological Transport, Humans, Isoelectric Point, Microscopy, Fluorescence, Microtubule-Associated Proteins, Microtubules, Models, Biological, Protein Binding, Recombinant Proteins, Kinesins, tau Proteins, Genes, Reporter, Protein Isoforms, Molecular Motor Proteins, Rats
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