Structural basis for plant plasma membrane protein dynamics and organization into functional nanodomains

Elife. 2017 Jul 31;6:e26404. doi: 10.7554/eLife.26404.

Abstract

Plasma Membrane is the primary structure for adjusting to ever changing conditions. PM sub-compartmentalization in domains is thought to orchestrate signaling. Yet, mechanisms governing membrane organization are mostly uncharacterized. The plant-specific REMORINs are proteins regulating hormonal crosstalk and host invasion. REMs are the best-characterized nanodomain markers via an uncharacterized moiety called REMORIN C-terminal Anchor. By coupling biophysical methods, super-resolution microscopy and physiology, we decipher an original mechanism regulating the dynamic and organization of nanodomains. We showed that targeting of REMORIN is independent of the COP-II-dependent secretory pathway and mediated by PI4P and sterol. REM-CA is an unconventional lipid-binding motif that confers nanodomain organization. Analyses of REM-CA mutants by single particle tracking demonstrate that mobility and supramolecular organization are critical for immunity. This study provides a unique mechanistic insight into how the tight control of spatial segregation is critical in the definition of PM domain necessary to support biological function.

Keywords: Membrane domain; Nicotiana benthamiana; membrane structure; phospholipids; plant biology; sterols; targeting.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biophysical Phenomena
  • Cell Membrane / chemistry*
  • Microscopy
  • Plant Proteins / analysis*
  • Tobacco / chemistry*
  • Tobacco / physiology*

Substances

  • Plant Proteins