Recycling domains in plant cell morphogenesis: small GTPase effectors, plasma membrane signalling and the exocyst

Biochem Soc Trans. 2010 Apr;38(2):723-8. doi: 10.1042/BST0380723.

Abstract

The Rho/Rop small GTPase regulatory module is central for initiating exocytotically ACDs (active cortical domains) in plant cell cortex, and a growing array of Rop regulators and effectors are being discovered in plants. Structural membrane phospholipids are important constituents of cells as well as signals, and phospholipid-modifying enzymes are well known effectors of small GTPases. We have shown that PLDs (phospholipases D) and their product, PA (phosphatidic acid), belong to the regulators of the secretory pathway in plants. We have also shown that specific NOXs (NADPH oxidases) producing ROS (reactive oxygen species) are involved in cell growth as exemplified by pollen tubes and root hairs. Most plant cells exhibit several distinct plasma membrane domains (ACDs), established and maintained by endocytosis/exocytosis-driven membrane protein recycling. We proposed recently the concept of a 'recycling domain' (RD), uniting the ACD and the connected endosomal recycling compartment (endosome), as a dynamic spatiotemporal entity. We have described a putative GTPase-effector complex exocyst involved in exocytic vesicle tethering in plants. Owing to the multiplicity of its Exo70 subunits, this complex, along with many RabA GTPases (putative recycling endosome organizers), may belong to core regulators of RD organization in plants.

Publication types

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

MeSH terms

  • Cell Membrane / metabolism*
  • Cell Membrane / physiology
  • Cell Physiological Phenomena
  • Cells / metabolism
  • Exocytosis* / physiology
  • Models, Biological
  • Monomeric GTP-Binding Proteins / metabolism
  • Monomeric GTP-Binding Proteins / physiology*
  • Morphogenesis / physiology*
  • Organoids / metabolism
  • Organoids / physiology
  • Plant Development*
  • Plant Structures / metabolism*
  • Plant Structures / physiology
  • Signal Transduction / physiology

Substances

  • Monomeric GTP-Binding Proteins