Flat clathrin lattices are dynamic actin-controlled hubs for clathrin-mediated endocytosis and signalling of specific receptors

Daniela Leyton-Puig, Tadamoto Isogai, Elisabetta Argenzio, Bram Van Den Broek, Jeffrey Klarenbeek, Hans Janssen, Kees Jalink, Metello Innocenti

Research output: Contribution to journalArticle

28 Scopus citations

Abstract

Clathrin lattices at the plasma membrane coat both invaginated and flat regions forming clathrin-coated pits and clathrin plaques, respectively. The function and regulation of clathrin-coated pits in endocytosis are well understood but clathrin plaques remain enigmatic nanodomains. Here we use super-resolution microscopy, molecular genetics and cell biology to show that clathrin plaques contain the machinery for clathrin-mediated endocytosis and cell adhesion, and associate with both clathrin-coated pits and filamentous actin. We also find that actin polymerization promoted by N-WASP through the Arp2/3 complex is crucial for the regulation of plaques but not pits. Clathrin plaques oppose cell migration and undergo actin-and N-WASP-dependent disassembly upon activation of LPA receptor 1, but not EGF receptor. Most importantly, plaque disassembly correlates with the endocytosis of LPA receptor 1 and down-modulation of AKT activity. Thus, clathrin plaques serve as dynamic actin-controlled hubs for clathrin-mediated endocytosis and signalling that exhibit receptor specificity.

Original languageEnglish (US)
Article number16068
JournalNature communications
Volume8
DOIs
StatePublished - Jul 13 2017
Externally publishedYes

ASJC Scopus subject areas

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

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    Leyton-Puig, D., Isogai, T., Argenzio, E., Van Den Broek, B., Klarenbeek, J., Janssen, H., Jalink, K., & Innocenti, M. (2017). Flat clathrin lattices are dynamic actin-controlled hubs for clathrin-mediated endocytosis and signalling of specific receptors. Nature communications, 8, [16068]. https://doi.org/10.1038/ncomms16068