An allosteric propofol-binding site in kinesin disrupts kinesin-mediated processive movement on microtubules
Open accessAbstract
Microtubule-based molecular motors mediate transport of intracellular cargo to subdomains in neurons. Previous evidence has suggested that the anesthetic propofol decreases the average run-length potential of the major anterograde transporters kinesin-1 and kinesin-2 without altering their velocity. This effect on kinesin has not been observed with other inhibitors, stimulating considerable interest in the underlying mechanism. Here, we used a photoactive derivative of propofol, meta -azipropofol (AziP m ), to search for potential propofol-binding sites in kinesin. Single-molecule motility assays confirmed that AziP m and propofol similarly inhibit kinesin-1 and kinesin-2. We then applied AziP m in semiquantitative radiolabeling and MS microsequencing assays to identify propofol-binding sites within microtubule–kinesin complexes. The radiolabeling experiments suggested preferential AziP m binding to the ATP-bound microtubule–kinesin complex. The photolabeled residues were contained within the kinesin motor domain rather than at the motor domain–β-tubulin interface. No residues within the P-loop of kinesin were photolabeled, indicating an inhibitory mechanism that does not directly affect ATPase activity and has an effect on run length without changing velocity. Our results also indicated that when the kinesin motor interacts with the microtubule during its processive run, a site forms in kinesin to which propofol can then bind and allosterically disrupt the kinesin–microtubule interaction, resulting in kinesin detachment and run termination. The discovery of the propofol-binding allosteric site in kinesin may improve our understanding of the strict coordination of the motor heads during the processive run. We hypothesize that propofol's potent effect on intracellular transport contributes to various components of its anesthetic action.
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Anesthetics cause microtubule-based molecular motors such as kinesin to reversibly detach from the microtubule lattice and disrupt transport of vesicles, proteins, and organelles to synapses.
“They can also cause microtubule-based molecular motors, such as kinesin, to reversibly fall off the microtubule lattice and thus disrupt transport of vesicles, proteins, and organelles to synapses [86].”
From The Biology of General Anesthesia from Paramecium to Primate (2019) · cites this paper as [86]
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- Authors
- Woll, K. A., Guzik-Lendrum, S., Bensel, B. M., Bhanu, N. V., Dailey, W. P., Garcia, B. A., Gilbert, S. P., & Eckenhoff, R. G.
- Affiliations
- University of Pennsylvania (US)
- Rensselaer Polytechnic Institute (US)
- Corresponding author
- Eckenhoff, Roderic G.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2018-07
- Volume
- 293
- Issue
- 29
- Pages
- 11283-11295
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC6065180
- OpenAlex
- W2805863058
- Cited by
- 23
- References
- 62
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 3 · 2023: 1 · 2022: 4 · 2021: 4 · 2020: 2 · 2019: 3 · 2018: 1
- FWCI
- 1.38
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- HHS | National Institutes of Health (NIH) (R37-GM054141, P01-GM55876, GM110174, AI118891)
- National Science Foundation (NSF) (DGE-1321851)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Neuroscience › Developmental Neuroscience › Anesthesia and Neurotoxicity Research
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- propofol, kinesin-1, kinesin-2, allosteric site, processive movement, run length, anesthetic mechanisms, intracellular transport, microsequencing
- MeSH terms
- Allosteric Site, Amino Acid Sequence, Binding Sites, Humans, Microtubules, Propofol, Kinesins, Crystallography, X-Ray, Anesthetics, Intravenous, Molecular Docking Simulation
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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