Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension
Matteo Biancospino,
Gwen R. Buel,
Carlos A. Niño,
Elena Maspero,
Rossella Scotto di Perrotolo,
Andrea Raimondi,
Lisa Redlingshöfer,
Janine Weber,
Frances M. Brodsky (),
Kylie J. Walters () and
Simona Polo ()
Additional contact information
Matteo Biancospino: IFOM, Fondazione Istituto FIRC di Oncologia Molecolare
Gwen R. Buel: National Cancer Institute
Carlos A. Niño: IFOM, Fondazione Istituto FIRC di Oncologia Molecolare
Elena Maspero: IFOM, Fondazione Istituto FIRC di Oncologia Molecolare
Rossella Scotto di Perrotolo: IFOM, Fondazione Istituto FIRC di Oncologia Molecolare
Andrea Raimondi: San Raffaele Scientific Institute
Lisa Redlingshöfer: University College London
Janine Weber: IFOM, Fondazione Istituto FIRC di Oncologia Molecolare
Frances M. Brodsky: University College London
Kylie J. Walters: National Cancer Institute
Simona Polo: IFOM, Fondazione Istituto FIRC di Oncologia Molecolare
Nature Communications, 2019, vol. 10, issue 1, 1-15
Abstract:
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.
Date: 2019
References: Add references at CitEc
Citations: View citations in EconPapers (2)
Downloads: (external link)
https://www.nature.com/articles/s41467-019-12855-6 Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12855-6
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/s41467-019-12855-6
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().