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

Clathrin light chains (CLCa and CLCb) are major constituents of clathrin-coated vesicles. Here authors find and structurally characterize the selective interaction between CLCa and the actin motor protein myosin VI which act together to generate the force that leads to invagination and fission at th...

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Main Authors: 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, Simona Polo
Format: Article
Language:English
Published: Nature Portfolio 2019-10-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-12855-6
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author 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
Simona Polo
author_facet 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
Simona Polo
author_sort Matteo Biancospino
collection DOAJ
description Clathrin light chains (CLCa and CLCb) are major constituents of clathrin-coated vesicles. Here authors find and structurally characterize the selective interaction between CLCa and the actin motor protein myosin VI which act together to generate the force that leads to invagination and fission at the apical surface.
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spelling doaj.art-8f91af4c82334c6394eedff499f3dee12022-12-21T21:35:25ZengNature PortfolioNature Communications2041-17232019-10-0110111510.1038/s41467-019-12855-6Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tensionMatteo Biancospino0Gwen R. Buel1Carlos A. Niño2Elena Maspero3Rossella Scotto di Perrotolo4Andrea Raimondi5Lisa Redlingshöfer6Janine Weber7Frances M. Brodsky8Kylie J. Walters9Simona Polo10IFOM, Fondazione Istituto FIRC di Oncologia MolecolareStructural Biophysics Laboratory, Center for Cancer Research, National Cancer InstituteIFOM, Fondazione Istituto FIRC di Oncologia MolecolareIFOM, Fondazione Istituto FIRC di Oncologia MolecolareIFOM, Fondazione Istituto FIRC di Oncologia MolecolareExperimental Imaging Center, San Raffaele Scientific InstituteDivision of Biosciences, University College LondonIFOM, Fondazione Istituto FIRC di Oncologia MolecolareDivision of Biosciences, University College LondonStructural Biophysics Laboratory, Center for Cancer Research, National Cancer InstituteIFOM, Fondazione Istituto FIRC di Oncologia MolecolareClathrin light chains (CLCa and CLCb) are major constituents of clathrin-coated vesicles. Here authors find and structurally characterize the selective interaction between CLCa and the actin motor protein myosin VI which act together to generate the force that leads to invagination and fission at the apical surface.https://doi.org/10.1038/s41467-019-12855-6
spellingShingle 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
Simona Polo
Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension
Nature Communications
title Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension
title_full Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension
title_fullStr Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension
title_full_unstemmed Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension
title_short Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension
title_sort clathrin light chain a drives selective myosin vi recruitment to clathrin coated pits under membrane tension
url https://doi.org/10.1038/s41467-019-12855-6
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