Surfing on microtubule ends

Trends Cell Biol. 2003 May;13(5):229-37. doi: 10.1016/s0962-8924(03)00074-6.


A crowd of proteins seems to have gathered around the plus-ends of microtubules. A rapidly expanding group of proteins known as plus-end tracking proteins (+TIPs) have been identified that seem to be able to 'surf' the dynamic ends of microtubules. Microtubule plus-ends exist in multiple conformational and chemical states. In principle, altering this plus-end microenvironment is an appealing way for regulators such as the +TIPS to control microtubule dynamics; however, specific mechanisms are poorly defined. Here, we focus on new findings addressing the underlying mechanisms of plus-end tracking and the mechanisms by which +TIPS control microtubule dynamics. We review the evidence that plus-end-binding and the control of microtubule dynamics are mechanistically linked. We also consider the possibility that, by studying +TIPs, we might learn more about the dynamic structural changes at the microtubule ends that are at the heart of dynamic instability.

Publication types

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

MeSH terms

  • Animals
  • Dynactin Complex
  • Guanosine Triphosphate / chemistry
  • Humans
  • Microtubule-Associated Proteins / physiology
  • Microtubules / physiology*
  • Microtubules / ultrastructure*
  • Models, Biological
  • Neoplasm Proteins
  • Protein Structure, Tertiary
  • Tubulin / chemistry
  • Yeasts / physiology


  • Dynactin Complex
  • Microtubule-Associated Proteins
  • Neoplasm Proteins
  • Tubulin
  • cytoplasmic linker protein 170
  • Guanosine Triphosphate