BIN1 regulates actin-membrane interactions during IRSp53-dependent filopodia formation

Commun Biol. 2024 May 9;7(1):549. doi: 10.1038/s42003-024-06168-8.

Abstract

Amphiphysin 2 (BIN1) is a membrane and actin remodeling protein mutated in congenital and adult centronuclear myopathies. Here, we report an unexpected function of this N-BAR domain protein BIN1 in filopodia formation. We demonstrated that BIN1 expression is necessary and sufficient to induce filopodia formation. BIN1 is present at the base of forming filopodia and all along filopodia, where it colocalizes with F-actin. We identify that BIN1-mediated filopodia formation requires IRSp53, which allows its localization at negatively-curved membrane topologies. Our results show that BIN1 bundles actin in vitro. Finally, we identify that BIN1 regulates the membrane-to-cortex architecture and functions as a molecular platform to recruit actin-binding proteins, dynamin and ezrin, to promote filopodia formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Adaptor Proteins, Signal Transducing* / metabolism
  • Animals
  • Cell Line
  • Cell Membrane / metabolism
  • HeLa Cells
  • Humans
  • Nerve Tissue Proteins* / metabolism
  • Nuclear Proteins* / metabolism
  • Pseudopodia* / metabolism
  • Tumor Suppressor Proteins* / metabolism

Substances

  • Bin1 protein, mouse
  • Actins
  • Nuclear Proteins
  • Tumor Suppressor Proteins
  • Adaptor Proteins, Signal Transducing
  • Nerve Tissue Proteins
  • BAIAP2 protein, human
  • Baiap2 protein, mouse