An Abl-FBP17 mechanosensing system couples local plasma membrane curvature and stress fiber remodeling during mechanoadaptation

Nat Commun. 2019 Dec 20;10(1):5828. doi: 10.1038/s41467-019-13782-2.


Cells remodel their structure in response to mechanical strain. However, how mechanical forces are translated into biochemical signals that coordinate the structural changes observed at the plasma membrane (PM) and the underlying cytoskeleton during mechanoadaptation is unclear. Here, we show that PM mechanoadaptation is controlled by a tension-sensing pathway composed of c-Abl tyrosine kinase and membrane curvature regulator FBP17. FBP17 is recruited to caveolae to induce the formation of caveolar rosettes. FBP17 deficient cells have reduced rosette density, lack PM tension buffering capacity under osmotic shock, and cannot adapt to mechanical strain. Mechanistically, tension is transduced to the FBP17 F-BAR domain by direct phosphorylation mediated by c-Abl, a mechanosensitive molecule. This modification inhibits FBP17 membrane bending activity and releases FBP17-controlled inhibition of mDia1-dependent stress fibers, favoring membrane adaptation to increased tension. This mechanoprotective mechanism adapts the cell to changes in mechanical tension by coupling PM and actin cytoskeleton remodeling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Caveolae / metabolism*
  • Caveolae / ultrastructure
  • Fatty Acid-Binding Proteins / genetics
  • Fatty Acid-Binding Proteins / metabolism*
  • Fibroblasts
  • Gene Knockout Techniques
  • HEK293 Cells
  • HeLa Cells
  • Humans
  • Mechanotransduction, Cellular*
  • Microscopy, Electron
  • Phosphorylation
  • Proto-Oncogene Proteins c-abl / metabolism*
  • RNA, Small Interfering / metabolism
  • Stress Fibers / metabolism*
  • Stress Fibers / ultrastructure
  • Stress, Mechanical


  • FNBP1 protein, human
  • Fatty Acid-Binding Proteins
  • RNA, Small Interfering
  • Proto-Oncogene Proteins c-abl