Plasmodesmata viewed as specialised membrane adhesion sites

Protoplasma. 2011 Jan;248(1):39-60. doi: 10.1007/s00709-010-0217-6. Epub 2010 Oct 12.

Abstract

A significant amount of work has been expended to identify the elusive components of plasmodesmata (PD) to help understand their structure, as well as how proteins are targeted to them. This review focuses on the role that lipid membranes may play in defining PD both structurally and as subcellular targeting addresses. Parallels are drawn to findings in other areas of research which focus on the lateral segregation of membrane domains and the generation of three-dimensional organellar shapes from flat lipid bilayers. We conclude that consideration of the protein-lipid interactions in cell biological studies of PD components and PD-targeted proteins may yield new insights into some of the many open questions regarding these unique structures.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Carrier Proteins / chemistry
  • Carrier Proteins / metabolism
  • Cell Adhesion*
  • Cell Membrane / chemistry*
  • Cell Membrane / metabolism
  • Cell Membrane / ultrastructure
  • Cytoskeleton / chemistry
  • Cytoskeleton / metabolism
  • Diffusion
  • Endoplasmic Reticulum / chemistry
  • Endoplasmic Reticulum / metabolism
  • Endoplasmic Reticulum / ultrastructure
  • Membrane Microdomains / chemistry
  • Membrane Microdomains / metabolism
  • Membrane Microdomains / ultrastructure
  • Monomeric GTP-Binding Proteins / metabolism
  • Phosphatidylinositols / metabolism
  • Phosphoproteins / chemistry
  • Phosphoproteins / metabolism
  • Plant Proteins / chemistry*
  • Plant Proteins / metabolism
  • Plant Viral Movement Proteins / chemistry
  • Plant Viral Movement Proteins / metabolism
  • Plasmodesmata / chemistry*
  • Plasmodesmata / metabolism
  • Plasmodesmata / ultrastructure
  • Protein Transport

Substances

  • Carrier Proteins
  • Phosphatidylinositols
  • Phosphoproteins
  • Plant Proteins
  • Plant Viral Movement Proteins
  • remorin
  • Monomeric GTP-Binding Proteins