ArticleThe Journal of cell biology2020
Clathrin's adaptor interaction sites are repurposed to stabilize microtubules during mitosis.
Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 33 citations in OpenAlex.
- 45A ncRNA Expression Leads to Chromosomal Instability and Cytoskeletal Dynamics Impairment by Modulating GTSE1/p53/AurB Subcellular Localization.International journal of molecular sciences · 2026Article
- SAPCD2 phosphorylation modulates astral microtubule stability to control spindle orientation.Communications biology · 2026Article
- Inhibition of the Clathrin Terminal Domain-Amphiphysin Protein-Protein Interaction. Probing the Pitstop 2 Aromatic Moiety.ChemMedChem · 2025Article
- Large-scale phosphomimetic screening identifies phospho-modulated motif-based protein interactions.Molecular systems biology · 2023Article
- Large-scale phage-based screening reveals extensive pan-viral mimicry of host short linear motifs.Nature communications · 2023Article
- Defining endogenous TACC3-chTOG-clathrin-GTSE1 interactions at the mitotic spindle using induced relocalization.Journal of cell science · 2021Article
- ESI mutagenesis: a one-step method for introducing mutations into bacterial artificial chromosomes.Life science alliance · 2021Article
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Authors and funding
16 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clathrin ensures mitotic spindle stability and efficient chromosome alignment, independently of its vesicle trafficking function. Although clathrin localizes to the mitotic spindle and kinetochore fiber microtubule bundles, the mechanisms by which clathrin stabilizes microtubules are unclear. We show that clathrin adaptor interaction sites on clathrin heavy chain (CHC) are repurposed during mitosis to directly recruit the microtubule-stabilizing protein GTSE1 to the spindle. Structural analyses reveal that these sites interact directly with clathrin-box motifs on GTSE1. Disruption of this interaction releases GTSE1 from spindles, causing defects in chromosome alignment. Surprisingly, this disruption destabilizes astral microtubules, but not kinetochore-microtubule attachments, and chromosome alignment defects are due to a failure of chromosome congression independent of kinetochore-microtubule attachment stability. GTSE1 recruited to the spindle by clathrin stabilizes microtubules by inhibiting the microtubule depolymerase MCAK. This work uncovers a novel role of clathrin adaptor-type interactions to stabilize nonkinetochore fiber microtubules to support chromosome congression, defining for the first time a repurposing of this endocytic interaction mechanism during mitosis.
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