Regulation of microtubule dynamics by TOG-domain proteins XMAP215/Dis1 and CLASP

Trends Cell Biol. 2011 Oct;21(10):604-14. doi: 10.1016/j.tcb.2011.06.007. Epub 2011 Jul 23.


The molecular mechanisms by which microtubule-associated proteins (MAPs) regulate the dynamic properties of microtubules (MTs) are still poorly understood. We review recent advances in our understanding of two conserved families of MAPs, the XMAP215/Dis1 and CLASP family of proteins. In vivo and in vitro studies show that XMAP215 proteins act as microtubule polymerases at MT plus ends to accelerate MT assembly, and CLASP proteins promote MT rescue and suppress MT catastrophe events. These are structurally related proteins that use conserved TOG domains to recruit tubulin dimers to MTs. We discuss models for how these proteins might use these individual tubulin dimers to regulate dynamic behavior of MT plus ends.

Publication types

  • Review

MeSH terms

  • Animals
  • Humans
  • Microtubule-Associated Proteins / chemistry*
  • Microtubule-Associated Proteins / metabolism*
  • Microtubules / chemistry*
  • Microtubules / metabolism*
  • Models, Molecular*
  • Tubulin / chemistry
  • Tubulin / metabolism
  • Xenopus Proteins / chemistry
  • Xenopus Proteins / metabolism


  • CKAP5 protein, Xenopus
  • CKAP5 protein, human
  • CLASP1 protein, human
  • CLASP2 protein, human
  • Microtubule-Associated Proteins
  • Tubulin
  • Xenopus Proteins