Microtubule-dependent motility and orientation of the cortical endoplasmic reticulum in elongating characean internodal cells

Cell Motil Cytoskeleton. 2009 Mar;66(3):142-55. doi: 10.1002/cm.20337.

Abstract

Motility of the endoplasmic reticulum (ER) is predominantly microtubule- dependent in animal cells but thought to be entirely actomyosin-dependent in plant cells. Using live cell imaging and transmission electron microscopy to examine ER motility and structural organization in giant internodal cells of characean algae, we discovered that at the onset of cell elongation, the cortical ER situated near the plasma membrane formed a tight meshwork of predominantly transverse ER tubules that frequently coaligned with microtubules. Microtubule depolymerization increased mesh size and decreased the dynamics of the cortical ER. In contrast, perturbing the cortical actin array with cytochalasins did not affect the transverse orientation but decreased mesh size and increased ER dynamics. Our data suggest that myosin-dependent ER motility is confined to the ER strands in the streaming endoplasm, while the more sedate cortical ER uses microtubule-based mechanisms for organization and motility during early stages of cell elongation. We show further that the ER has an inherent, NEM-sensitive dynamics which can be altered via interaction with the cytoskeleton and that tubule formation and fusion events are cytoskeleton-independent.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Angiogenesis Inhibitors / pharmacology
  • Cell Movement / drug effects
  • Cell Movement / physiology*
  • Cells, Cultured
  • Chloroplasts / metabolism
  • Cytochalasin D / pharmacology
  • Cytochalasins / pharmacology
  • Cytoplasm / metabolism
  • Cytoplasmic Streaming / drug effects
  • Cytoplasmic Streaming / physiology*
  • Cytoskeleton / metabolism*
  • Endoplasmic Reticulum / drug effects
  • Endoplasmic Reticulum / metabolism*
  • Fluorescence
  • Microtubules / metabolism*
  • Mycotoxins
  • Myosins / metabolism
  • Nitella / metabolism*
  • Nucleic Acid Synthesis Inhibitors / pharmacology

Substances

  • Actins
  • Angiogenesis Inhibitors
  • Cytochalasins
  • Mycotoxins
  • Nucleic Acid Synthesis Inhibitors
  • Cytochalasin D
  • cytochalasin E
  • Myosins