Cell cycle regulation of microtubule interactomes: multi-layered regulation is critical for the interphase/mitosis transition
Open accessAbstract
Microtubules dramatically change their dynamics and organization at the entry into mitosis. Although this change is mediated by microtubule-associated proteins (MAPs), how MAPs themselves are regulated is not well understood. Here we used an integrated multi-level approach to establish the framework and biological significance of MAP regulation critical for the interphase/mitosis transition. Firstly, we applied quantitative proteomics to determine global cell cycle changes in the profiles of MAPs in human and Drosophila cells. This uncovered a wide range of cell cycle regulations of MAPs previously unidentified. Secondly, systematic studies of human kinesins highlighted an overlooked aspect of kinesins: most mitotic kinesins suppress their affinity to microtubules or reduce their protein levels in interphase in combination with nuclear localization. Thirdly, in-depth analysis of a novel Drosophila MAP (Mink) revealed that the suppression of the microtubule affinity of this mitotic MAP in combination with nuclear localization is essential for microtubule organization in interphase, and phosphorylation of Mink is needed for kinetochore-microtubule attachment in mitosis. Thus, this first comprehensive analysis of MAP regulation for the interphase/mitosis transition advances our understanding of kinesin biology and reveals the prevalence and importance of multi-layered MAP regulation.
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Newer proteomics approaches are identifying novel protein-protein interactions and putative sites of phosphoregulation and other post-translational modifications, which should provide a complete roadmap of the mitotic spindle.
“In addition, newer proteomics approaches are identifying novel protein-protein interactions and putative sites of phosphoregulation and other post-translational modifications, which should provide a complete roadmap of the mitotic spindle [61, 62].”
From Regulatory mechanisms that control mitotic kinesins (2015) · cites this paper as [61]
The Results report phosphorylation-site measurements, and the Experimental Procedures describe mapping an interaction network for identified microtubule-associated proteins. But the Discussion says other modifications were not actively maintained and notes that the method missed proteins binding exclusively to dynamic microtubule ends. The paper therefore supports proteomics as a way to build a broader picture, not the claim that it should provide a complete roadmap of the mitotic spindle. (LLM, conf=0.87)
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BackgroundTwo-step interphase microtubule disassembly aids spindle morphogenesis
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Two-step interphase microtubule disassembly aids spindle morphogenesisPreprint
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Further Reading | Microtubule Plus and Minus End Binding Proteins
Mosby, L. S., & Straube, A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00318-2
- Authors
- Syred, H. M., Welburn, J., Rappsilber, J., & Ohkura, H.
- Affiliations
- Wellcome Centre for Cell Biology (GB)
- Corresponding author
- Rappsilber, Juri
- Ohkura, Hiroyuki
- Venue
- Molecular & Cellular Proteomics
- Publisher
- Elsevier BV
- Published
- 2013-11
- Volume
- 12
- Issue
- 11
- Pages
- 3135-3147
- ISSN
- 1535-9476 (ISSN-L)
- PMC
- PMC3820929
- OpenAlex
- W2140591566
- Cited by
- 25
- References
- 51
- Citations by year
- 2026: 1 · 2025: 2 · 2022: 3 · 2021: 1 · 2019: 2 · 2018: 8 · 2017: 1 · 2016: 1 · 2015: 5 · 2013: 1
- FWCI
- 1.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular & Cellular Proteomics (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, other-oa)
- Funders
- Wellcome Trust (98030, 091020, 084229, 098030, 081849, 092076, 098030/Z/11/Z)
- Cancer Research UK (12840, C40377/A12840)
- University of Warwick
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Biotin and Related Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- microtubule-associated proteins, cell cycle regulation, kinesin, nuclear localization, mink, kinetochore-microtubule attachment, microtubule dynamics, protein phosphorylation, Drosophila cells, human cells
- MeSH terms
- Amino Acid Sequence, Animals, Cell Line, Drosophila melanogaster, HeLa Cells, Humans, Interphase, Microtubule-Associated Proteins, Microtubules, Molecular Sequence Data, Phosphorylation, Recombinant Fusion Proteins, Mutagenesis, Site-Directed, Kinesins, Sequence Homology, Amino Acid, Kinetochores, Amino Acid Substitution, Drosophila Proteins, Proteomics, Protein Interaction Domains and Motifs, Cell Cycle Checkpoints, M Phase Cell Cycle Checkpoints
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