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Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension

  1. Author:
    Biancospino, Matteo
    Buel,Gwen [ORCID]
    Niño, Carlos A
    Maspero, Elena
    di Perrotolo, Rossella Scotto
    Raimondi, Andrea [ORCID]
    Redlingshöfer, Lisa
    Weber, Janine
    Brodsky, Frances M
    Walters,Kylie
    Polo, Simona [ORCID]

  2. Author Address

    IFOM, Fondazione Istituto FIRC di Oncologia Molecolare, 20139, Milan, Italy., Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702, USA., Experimental Imaging Center, San Raffaele Scientific Institute, Milan, Italy., Division of Biosciences, University College London, London, WC1E 6BT, UK., Division of Biosciences, University College London, London, WC1E 6BT, UK. f.brodsky@ucl.ac.uk., Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702, USA. kylie.walters@nih.gov., IFOM, Fondazione Istituto FIRC di Oncologia Molecolare, 20139, Milan, Italy. simona.polo@ifom.eu., Dipartimento di Oncologia ed Emato-oncologia, Universita 39; degli Studi di Milano, 20122, Milan, Italy. simona.polo@ifom.eu.,
    1. Year: 2019
    2. Date: Oct 31
    3. Epub Date: 2019 10 31
  2. Journal: Nature communications
    1. 10
    2. 1
    3. Pages: 4974
  4. Type of Article: Article
  5. Article Number: 4974
  6. ISSN: 2041-1723
  1. Abstract:

    Clathrin light chains (CLCa and CLCb) are major constituents of clathrin-coated vesicles. Unique functions for these evolutionary conserved paralogs remain elusive, and their role in clathrin-mediated endocytosis in mammalian cells is debated. Here, we find and structurally characterize a direct and selective interaction between CLCa and the long isoform of the actin motor protein myosin VI, which is expressed exclusively in highly polarized tissues. Using genetically-reconstituted Caco-2 cysts as proxy for polarized epithelia, we provide evidence for coordinated action of myosin VI and CLCa at the apical surface where these proteins are essential for fission of clathrin-coated pits. We further find that myosin VI and Huntingtin-interacting protein 1-related protein (Hip1R) are mutually exclusive interactors with CLCa, and suggest a model for the sequential function of myosin VI and Hip1R in actin-mediated clathrin-coated vesicle budding.

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External Sources

  1. View Full Text
  2. DOI: 10.1038/s41467-019-12855-6
  3. PMID: 31672988
  4. View record in Web of Science®
  5. WOS: 000493438700022
  6. PII : 10.1038/s41467-019-12855-6

Library Notes

  1. Fiscal Year: FY2019-2020
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