CINaM - Centre Interdisciplinaire de Nanoscience de Marseille

Partenaires

CINaM
CNRS
Logo tutelle
UMI



Rechercher

Sur le Web du CNRS


  • CINaM
  • Campus de Luminy
  • Case 913
  • 13288 Marseille Cedex 9
  •  
  • Tel : +33(0)4 91 17 28 00
  • Fax : +33(0)4 91 41 89 16

Accueil du site > À la une > Membrane fluctuations mediate lateral interaction between cadherin bonds

Membrane fluctuations mediate lateral interaction between cadherin bonds

S. F. Fenz, T. Bihr, D. Schmidt, R. Merkel, U. Seifert, K. Sengupta and A-S Smith.
Nature Physics (2017) | doi:10.1038/nphys4138

The integrity of living tissues is maintained by domains of trans-bonds formed between cadherin proteins residing on opposing membranes of neighbouring cells. These domains are stabilized by lateral cis-interactions between the cadherins on the same cell. However, the origin of cis-interactions remains perplexing since they are detected only in the context of trans-bonds. We identified bending fluctuations of membranes as a source of long-range cis-interactions, and a regulator of trans-interactions. Specifically, nanometric membrane bending and fluctuations introduce cooperative effects that modulate the affinity and binding/unbinding rates for trans-dimerization, dramatically affecting the nucleation and growth of adhesion domains. Importantly, this regulation relies on physical principles and not on details of protein–protein interactions. These omnipresent fluctuations can thus act as a generic control mechanism in all types of cell adhesion, suggesting a hitherto unknown physiological role for recently identified active fluctuations of cellular membranes.

JPG - 24.7 ko
Different types of adhesion domains obtained from experimental data
Each column shows two examples of identical cadherin carrying GUVs adhered to cadherin decorated substrates. The experimentally detected adhesion domains are painted with different colours. For GUVs membranes that fluctuate less, only one (blue) domain is seen. For higher fluctuations, more numerous (variously coloured) domains are formed. The final morphology of adhesion domains seen here is in fact determined by the adhesion dynamics, itself modified by the membrane fluctuations.