Microtubule binding proteins CLIP-170, EB1, and p150Glued form distinct plus-end complexes

FEBS Lett. 2006 Feb 20;580(5):1327-32. doi: 10.1016/j.febslet.2006.01.050. Epub 2006 Jan 26.

Abstract

Microtubule plus-end proteins CLIP-170 and EB1 dynamically track the tips of growing microtubules in vivo. Here we examine the association of these proteins with microtubules in vitro. CLIP-170 binds tubulin dimers and co-assembles into growing microtubules. EB1 binds tubulin dimers more weakly, so no co-assembly is observed. However, EB1 binds to CLIP-170, and forms a co-complex with CLIP-170 and tubulin that is recruited to growing microtubule plus ends. The interaction between CLIP-170 and EB1 is competitively inhibited by the related CAP-Gly protein p150Glued, which also localizes to microtubule plus ends in vivo. Based on these observations, we propose a model in which the formation of distinct plus-end complexes may differentially affect microtubule dynamics in vivo.

MeSH terms

  • Animals
  • Dynactin Complex
  • Microtubule-Associated Proteins / metabolism*
  • Microtubules / metabolism
  • Multiprotein Complexes*
  • Neoplasm Proteins / metabolism
  • Protein Binding
  • Recombinant Proteins
  • Tubulin / pharmacology

Substances

  • Dynactin Complex
  • EB1 microtubule binding proteins
  • Microtubule-Associated Proteins
  • Multiprotein Complexes
  • Neoplasm Proteins
  • Recombinant Proteins
  • Tubulin
  • cytoplasmic linker protein 170