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Structural characterization and inhibition of the interaction between ch-TOG and TACC3
Open accessPreprint — published as 10.1083/jcb.202407002 · Paper page
Abstract
The mitotic spindle is a bipolar array of microtubules, radiating from the poles which each contain a centrosome, embedded in pericentriolar material. Two proteins, ch-TOG and TACC3, have multiple functions at the mitotic spindle due to operating alone, together or in complex with other proteins. To distinguish these activities, we need new molecular tools to dissect their function. Here, we present the structure of the α -helical bundle domain of ch-TOG that mediates its interaction with TACC3 and a structural model describing the interaction, supported by biophysical and biochemical data. We have isolated Affimer tools to precisely target the ch-TOG-binding site on TACC3 in live cells, which displace ch-TOG without affecting the spindle localization of other protein complex components. Inhibition of the TACC3–ch-TOG interaction led unexpectedly to fragmentation of the pericentriolar material in metaphase cells following the formation of a bipolar spindle and delayed mitotic progression; uncovering a novel role of TACC3–ch-TOG in maintaining pericentriolar material integrity during mitosis to ensure timely cell division.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Shelford, J., Burgess, S. G., Rostkova, E., Richards, M. W., Tiede, C., Fielding, A. J., Daviter, T., Tomlinson, D. C., Calabrese, A. N., Pfuhl, M., Bayliss, R., & Royle, S. J.
- Affiliations
- University of Warwick (GB)
- University of Leeds (GB)
- King's College London (GB)
- Liverpool John Moores University (GB)
- Institute of Cancer Research (GB)
- Corresponding author
- Pfuhl, Mark
- Bayliss, Richard
- Royle, Stephen J.
- ORCID
- Venue
- The Journal of Cell Biology
- Publisher
- openRxiv
- Published
- 2024-05-31
- Volume
- 224
- Issue
- 6
- ISSN
- 0021-9525 (ISSN-L)
- PMC
- PMC11921806
- OpenAlex
- W4408617308
- Cited by
- 2
- References
- 1
- Citations by year
- 2026: 2
- FWCI
- 0.99
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (acceptedVersion)
- Liverpool John Moores University (acceptedVersion)
- Warwick Research Archive Portal (University of Warwick) (acceptedVersion)
- Funders
- Wellcome Trust (220628/Z/20/Z, 220628)
- Cancer Research UK (C25425/A27718)
- Royal Society (220628/Z/20/Z)
- Directorate for Biological Sciences
- Medical Research Council (MR/X008673/1)
- Engineering and Physical Sciences Research Council (NS/A000055/1)
- Biotechnology and Biological Sciences Research Council (BB/M012573/1, BB/M01116X/1, BB/L023113/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Physical Sciences › Chemistry › Organic Chemistry › Heterocyclic Compound Synthesis and Bioactivity
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- TACC3, mitotic spindle, pericentriolar material, protein-protein interaction, Affimers, binding sites, protein structure, mitotic progression
- MeSH terms
- Binding Sites, HeLa Cells, Humans, Microtubule-Associated Proteins, Microtubules, Mitosis, Spindle Apparatus, Models, Molecular, Protein Binding, Centrosome
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