External push and internal pull forces recruit curvature-sensing N-BAR domain proteins to the plasma membrane. Academic Article uri icon

Overview

abstract

  • Many of the more than 20 mammalian proteins with N-BAR domains control cell architecture and endocytosis by associating with curved sections of the plasma membrane. It is not well understood whether N-BAR proteins are recruited directly by processes that mechanically curve the plasma membrane or indirectly by plasma-membrane-associated adaptor proteins that recruit proteins with N-BAR domains that then induce membrane curvature. Here, we show that externally induced inward deformation of the plasma membrane by cone-shaped nanostructures (nanocones) and internally induced inward deformation by contracting actin cables both trigger recruitment of isolated N-BAR domains to the curved plasma membrane. Markedly, live-cell imaging in adherent cells showed selective recruitment of full-length N-BAR proteins and isolated N-BAR domains to plasma membrane sub-regions above nanocone stripes. Electron microscopy confirmed that N-BAR domains are recruited to local membrane sites curved by nanocones. We further showed that N-BAR domains are periodically recruited to curved plasma membrane sites during local lamellipodia retraction in the front of migrating cells. Recruitment required myosin-II-generated force applied to plasma-membrane-connected actin cables. Together, our results show that N-BAR domains can be directly recruited to the plasma membrane by external push or internal pull forces that locally curve the plasma membrane.

publication date

  • July 1, 2012

Research

keywords

  • Actins
  • Cell Membrane
  • Cytoskeletal Proteins
  • Mechanical Phenomena
  • Nanostructures
  • Protein Interaction Domains and Motifs

Identity

PubMed Central ID

  • PMC3519285

Scopus Document Identifier

  • 84864871279

Digital Object Identifier (DOI)

  • 10.1016/j.cell.2006.12.039

PubMed ID

  • 22750946

Additional Document Info

volume

  • 14

issue

  • 8