KIF1C activates and extends dynein movement through the FHF cargo adapter
Open accessPublished version of a preprint
Abstract
Cellular cargos move bidirectionally on microtubules by recruiting opposite polarity motors dynein and kinesin. These motors show codependence, where one requires the activity of the other, although the mechanism is unknown. Here we show that kinesin-3 KIF1C acts as both an activator and a processivity factor for dynein, using in vitro reconstitutions of human proteins. Activation requires only a fragment of the KIF1C nonmotor stalk binding the cargo adapter HOOK3. The interaction site is separate from the constitutive factors FTS and FHIP, which link HOOK3 to small G-proteins on cargos. We provide a structural model for the autoinhibited FTS–HOOK3–FHIP1B (an FHF complex) and explain how KIF1C relieves it. Collectively, we explain codependency by revealing how mutual activation of dynein and kinesin occurs through their shared adapter. Many adapters bind both dynein and kinesins, suggesting this mechanism could be generalized to other bidirectional complexes.
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Highly accurate protein structure prediction with AlphaFold
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ColabFold - Making protein folding accessible to all
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Mechanism and regulation of kinesin motors.
Yildiz, A. (2025) · Nature reviews. Molecular cell biology · doi:10.1038/s41580-024-00780-6 · Cited by 88 · see citing works
- Authors
- Abid Ali, F., Zwetsloot, A. J., Stone, C. E., Morgan, T. E., Wademan, R. F., Carter, A. P., & Straube, A.
- Affiliations
- University of Warwick (GB)
- John Innes Centre (GB)
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Carter, Andrew P.
- Straube, Anne
- ORCID
- Venue
- Nature Structural & Molecular Biology
- Published
- 2025-01-02
- Volume
- 32
- Issue
- 4
- Pages
- 756-766
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC11996680
- OpenAlex
- W4405996020
- Cited by
- 30
- References
- 4
- Citations by year
- 2026: 11 · 2025: 16 · 2024: 3
- FWCI
- 13.32
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Nature Structural & Molecular Biology (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Warwick Research Archive Portal (University of Warwick) (acceptedVersion)
- Explore Bristol Research (submittedVersion, cc-by)
- Bristol Research (University of Bristol) (submittedVersion, cc-by)
- Funders
- Wellcome Trust
- University of Warwick
- Federal Aviation Administration
- Medical Research Council (1788496, MC_UP_A025_1011, MR/N014294, MR/N014294/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Biotin and Related Studies
- Keywords
- KIF1C, kinesin-3, dynein, HOOK3, FTS, motor activation, autoinhibition
- MeSH terms
- Dyneins, Humans, Microtubule-Associated Proteins, Models, Molecular, Protein Binding, Kinesins, Intracellular Signaling Peptides and Proteins
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