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Clathrin is required for the function of the mitotic spindle

Author

Listed:
  • Stephen J. Royle

    (MRC Laboratory of Molecular Biology)

  • Nicholas A. Bright

    (University of Cambridge, Addenbrooke's Hospital)

  • Leon Lagnado

    (MRC Laboratory of Molecular Biology)

Abstract

Clathrin has an established function in the generation of vesicles that transfer membrane and proteins around the cell1,2,3,4. The formation of clathrin-coated vesicles occurs continuously in non-dividing cells5, but is shut down during mitosis6, when clathrin concentrates at the spindle apparatus7,8. Here, we show that clathrin stabilizes fibres of the mitotic spindle to aid congression of chromosomes. Clathrin bound to the spindle directly by the amino-terminal domain of clathrin heavy chain. Depletion of clathrin heavy chain using RNA interference prolonged mitosis; kinetochore fibres were destabilized, leading to defective congression of chromosomes to the metaphase plate and persistent activation of the spindle checkpoint. Normal mitosis was rescued by clathrin triskelia but not the N-terminal domain of clathrin heavy chain, indicating that stabilization of kinetochore fibres was dependent on the unique structure of clathrin. The importance of clathrin for normal mitosis may be relevant to understanding human cancers that involve gene fusions of clathrin heavy chain.

Suggested Citation

  • Stephen J. Royle & Nicholas A. Bright & Leon Lagnado, 2005. "Clathrin is required for the function of the mitotic spindle," Nature, Nature, vol. 434(7037), pages 1152-1157, April.
  • Handle: RePEc:nat:nature:v:434:y:2005:i:7037:d:10.1038_nature03502
    DOI: 10.1038/nature03502
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    Cited by:

    1. Nicola Hellen & Gregory I. Mashanov & Ianina L. Conte & Sophie Trionnaire & Victor Babich & Laura Knipe & Alamin Mohammed & Kazim Ogmen & Silvia Martin-Almedina & Katalin Török & Matthew J. Hannah & J, 2022. "P-selectin mobility undergoes a sol-gel transition as it diffuses from exocytosis sites into the cell membrane," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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