@article{144856,
  keywords = {Animals, signal transduction, Protein Binding, Time Factors, Multiprotein Complexes, Xenopus Proteins, Xenopus laevis, Microtubules, Protein Interaction Domains and Motifs, Tubulin, Microtubule-Associated Proteins, Microtubule-Organizing Center},
  author = {Akanksha Thawani and Rachel Kadzik and Sabine Petry},
  title = {XMAP215 is a microtubule nucleation factor that functions synergistically with the γ-tubulin ring complex},
  abstract = {<p>How microtubules (MTs) are generated in the cell is a major question in understanding how the cytoskeleton is assembled. For several decades, γ-tubulin has been accepted as the universal MT nucleator of the cell. Although there is evidence that γ-tubulin complexes are not the sole MT nucleators, identification of other nucleation factors has proven difficult. Here, we report that the well-characterized MT polymerase XMAP215 (chTOG/Msps/Stu2p/Alp14/Dis1 homologue) is essential for MT nucleation in Xenopus egg extracts. The concentration of XMAP215 determines the extent of MT nucleation. Even though XMAP215 and the γ-tubulin ring complex (γ-TuRC) possess minimal nucleation activity individually, together, these factors synergistically stimulate MT nucleation in vitro. The amino-terminal TOG domains 1-5 of XMAP215 bind to αβ-tubulin and promote MT polymerization, whereas the conserved carboxy terminus is required for efficient MT nucleation and directly binds to γ-tubulin. In summary, XMAP215 and γ-TuRC together function as the principal nucleation module that generates MTs in cells.</p>
},
  year = {2018},
  journal = {Nat Cell Biol},
  volume = {20},
  pages = {575-585},
  month = {05/2018},
  issn = {1476-4679},
  doi = {10.1038/s41556-018-0091-6},
  language = {eng},
}