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


Journal

Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555

Informations de publication

Date de publication:
31 10 2019
Historique:
received: 03 06 2019
accepted: 27 09 2019
entrez: 2 11 2019
pubmed: 2 11 2019
medline: 4 3 2020
Statut: epublish

Résumé

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.

Identifiants

pubmed: 31672988
doi: 10.1038/s41467-019-12855-6
pii: 10.1038/s41467-019-12855-6
pmc: PMC6823378
doi:

Substances chimiques

Actins 0
Adaptor Proteins, Signal Transducing 0
Clathrin Light Chains 0
HIP1R protein, human 0
Microfilament Proteins 0
Protein Isoforms 0
myosin VI 0
Myosin Heavy Chains EC 3.6.4.1

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

4974

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Auteurs

Matteo Biancospino (M)

IFOM, Fondazione Istituto FIRC di Oncologia Molecolare, 20139, Milan, Italy.

Gwen R Buel (GR)

Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702, USA.

Carlos A Niño (CA)

IFOM, Fondazione Istituto FIRC di Oncologia Molecolare, 20139, Milan, Italy.

Elena Maspero (E)

IFOM, Fondazione Istituto FIRC di Oncologia Molecolare, 20139, Milan, Italy.

Rossella Scotto di Perrotolo (R)

IFOM, Fondazione Istituto FIRC di Oncologia Molecolare, 20139, Milan, Italy.

Andrea Raimondi (A)

Experimental Imaging Center, San Raffaele Scientific Institute, Milan, Italy.

Lisa Redlingshöfer (L)

Division of Biosciences, University College London, London, WC1E 6BT, UK.

Janine Weber (J)

IFOM, Fondazione Istituto FIRC di Oncologia Molecolare, 20139, Milan, Italy.

Frances M Brodsky (FM)

Division of Biosciences, University College London, London, WC1E 6BT, UK. f.brodsky@ucl.ac.uk.

Kylie J Walters (KJ)

Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD, 21702, USA. kylie.walters@nih.gov.

Simona Polo (S)

IFOM, Fondazione Istituto FIRC di Oncologia Molecolare, 20139, Milan, Italy. simona.polo@ifom.eu.
Dipartimento di Oncologia ed Emato-oncologia, Universita' degli Studi di Milano, 20122, Milan, Italy. simona.polo@ifom.eu.

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Classifications MeSH