Microtubule organization in the green kingdom: chaos or self-order?

J Cell Sci. 2002 Apr 1;115(Pt 7):1345-54. doi: 10.1242/jcs.115.7.1345.

Abstract

Plant microtubule arrays differ fundamentally from their animal, fungal and protistan counterparts. These differences largely reflect the requirements of plant composite polymer cell walls and probably also relate to the acquisition of chloroplasts. Plant microtubules are usually dispersed and lack conspicuous organizing centres. The key to understanding this dispersed nature is the identification of proteins that interact with and regulate the spatial and dynamic properties of microtubules. Over the past decade, a number of these proteins have been uncovered, including numerous kinesin-related proteins and a 65 kDa class of structural microtubule-associated proteins that appear to be unique to plants. Mutational analysis has identified MOR1, a probable stabilizer of microtubules that is a homologue of the TOGp-XMAP215 class of high-molecular-weight microtubule-associated proteins, and a katanin p60 subunit homologue implicated in the severing of microtubules. The identification of these two proteins provides new insights into the mechanisms controlling microtubule assembly and dynamics, particularly in the dispersed cortical array found in highly polarized plant cells.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Cell Wall / ultrastructure
  • Centrosome / chemistry
  • Centrosome / metabolism
  • Chloroplasts / physiology
  • Katanin
  • Kinesins / metabolism
  • Microtubule-Associated Proteins / analysis
  • Microtubule-Associated Proteins / chemistry
  • Microtubule-Associated Proteins / metabolism
  • Microtubules / ultrastructure*
  • Models, Biological
  • Plant Proteins*
  • Plants / chemistry
  • Plants / metabolism
  • Plants / ultrastructure*
  • Schizosaccharomyces pombe Proteins*

Substances

  • Microtubule-Associated Proteins
  • Plant Proteins
  • Schizosaccharomyces pombe Proteins
  • dis1 protein, S pombe
  • Adenosine Triphosphatases
  • Kinesins
  • Katanin