Self organization of membrane proteins via dimerization

Biophys Chem. 2003 May 1;104(1):217-27. doi: 10.1016/s0301-4622(02)00369-1.


Protein-protein dimerization is ubiquitous in biology, but its role in self-organization remains unexplored. Here we use Monte Carlo simulations to demonstrate that under diffusion-limited conditions, reversible dimerization alone can cause membrane proteins to cluster into oligomer-like structures. When multiple distinct protein species are able to form dimers, then heterodimerization and homodimerization can organize proteins into structured clusters that can affect cellular physiology. As an example, we demonstrate how receptor dimerization could provide a physical mechanism for regulating information flow by controlling receptor-receptor cross talk. These results are physically realistic for some membrane proteins, including members of the G-protein coupled receptor family, and may provide a physiological reason as to why many proteins dimerize.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Dimerization
  • GTP-Binding Proteins / chemistry*
  • GTP-Binding Proteins / metabolism
  • Monte Carlo Method
  • Particle Size
  • Protein Conformation
  • Receptors, G-Protein-Coupled / chemistry*
  • Receptors, G-Protein-Coupled / metabolism
  • Signal Transduction
  • Structure-Activity Relationship


  • Receptors, G-Protein-Coupled
  • GTP-Binding Proteins