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Cryo-EM captures early intermediate steps in dynein activation by LIS1
Open accessPreprint — published as 10.1038/s41467-025-62185-z · Paper page
Abstract
Cytoplasmic dynein-1 (dynein) is an essential molecular motor in eukaryotic cells. Dynein primarily exists in an autoinhibited “Phi” state and requires conformational changes to assemble with its cofactors and form active transport complexes. LIS1, a key dynein regulator, enhances dynein activation and assembly. Using cryo-EM and a human dynein-LIS1 sample incubated with ATP, we mapped the conformational landscape of dynein activation by LIS1. We discovered a novel early intermediate state that we propose precedes our previously identified dynein-LIS1 “Chi” state. Mutations that disrupt this species, which we termed “Pre-Chi”, led to motility defects in vitro, emphasizing its functional importance. Together, our findings provide new insights into how LIS1 relieves dynein autoinhibition during the activation pathway.
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Highly accurate protein structure prediction with AlphaFold
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Metadata
- Authors
- Nguyen, K. H. V., Karasmanis, E. P., Kendrick, A. A., Reck-Peterson, S. L., & Leschziner, A. E.
- Affiliations
- University of California San Diego (US)
- Salk Institute for Biological Studies (US)
- Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA, USA
- ORCID
- Venue
- Nature Communications
- Publisher
- openRxiv
- Published
- 2025-01-14
- Volume
- 16
- Issue
- 1
- Pages
- 7054-7054
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC12317079
- OpenAlex
- W4412818674
- Cited by
- 5
- References
- 1
- Citations by year
- 2026: 5
- FWCI
- 2.50
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Howard Hughes Medical Institute
- U.S. Department of Health and Human Services (R35 GM145296, T32-GM008326, R35 GM141825)
- American Cancer Society
- Jane Coffin Childs Memorial Fund for Medical Research
- National Institutes of Health (CA014195)
- University of California, San Diego
- National Cancer Institute (P30CA014195)
- National Institute of General Medical Sciences (R01GM107214, T32GM008326, R35GM145296, R35GM141825, T32GM139795)
- 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 › Molecular Biology › Protein Structure and Dynamics
- Keywords
- cytoplasmic dynein-1, LIS1, dynein activation, molecular motors, motility defects
- MeSH terms
- Adenosine Triphosphate, Dyneins, Humans, Microtubule-Associated Proteins, Models, Molecular, Mutation, Protein Conformation, Cryoelectron Microscopy, 1-Alkyl-2-acetylglycerophosphocholine Esterase, Cytoplasmic Dyneins
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