The packing density of a supramolecular membrane protein cluster is controlled by cytoplasmic interactions

Elife. 2017 Jul 19:6:e20705. doi: 10.7554/eLife.20705.

Abstract

Molecule clustering is an important mechanism underlying cellular self-organization. In the cell membrane, a variety of fundamentally different mechanisms drive membrane protein clustering into nanometre-sized assemblies. To date, it is unknown whether this clustering process can be dissected into steps differentially regulated by independent mechanisms. Using clustered syntaxin molecules as an example, we study the influence of a cytoplasmic protein domain on the clustering behaviour. Analysing protein mobility, cluster size and accessibility to myc-epitopes we show that forces acting on the transmembrane segment produce loose clusters, while cytoplasmic protein interactions mediate a tightly packed state. We conclude that the data identify a hierarchy in membrane protein clustering likely being a paradigm for many cellular self-organization processes.

Keywords: SNAREs; biochemistry; cell biology; clustering; human; microdomains; nano-assemblies; plasma membrane; rat; self-organization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Membrane / metabolism
  • Cytoplasm / metabolism*
  • Hep G2 Cells
  • Humans
  • Protein Interaction Maps
  • Protein Multimerization*
  • Syntaxin 1 / metabolism*

Substances

  • Syntaxin 1

Grants and funding

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.