@article{118996,
  keywords = {Animals, Protein Conformation, Humans, Protein Binding, Xenopus laevis, Microtubules, Spindle Apparatus, Cell Cycle Proteins, Tubulin, Microtubule-Associated Proteins, Microtubule-Organizing Center},
  author = {Jae-Geun Song and Matthew King and Rui Zhang and Rachel Kadzik and Akanksha Thawani and Sabine Petry},
  title = {Mechanism of how augmin directly targets the γ-tubulin ring complex to microtubules},
  abstract = {<p>Microtubules (MTs) must be generated from precise locations to form the structural frameworks required for cell shape and function. MTs are nucleated by the γ-tubulin ring complex (γ-TuRC), but it remains unclear how γ-TuRC gets to the right location. Augmin has been suggested to be a γ-TuRC targeting factor and is required for MT nucleation from preexisting MTs. To determine augmin{\textquoteright}s architecture and function, we purified augmin from insect cells. We demonstrate that augmin is sufficient to target γ-TuRC to MTs by in vitro reconstitution. Augmin is composed of two functional parts. One module (tetramer-II) is necessary for MT binding, whereas the other (tetramer-III) interacts with γ-TuRC. Negative-stain electron microscopy reveals that both tetramers fit into the Y-shape of augmin, and MT branching assays reveal that both are necessary for MT nucleation. The finding that augmin can directly bridge MTs with γ-TuRC via these two tetramers adds to our mechanistic understanding of how MTs can be nucleated from preexisting MTs.</p>
},
  year = {2018},
  journal = {J Cell Biol},
  volume = {217},
  pages = {2417-2428},
  month = {07/2018},
  issn = {1540-8140},
  doi = {10.1083/jcb.201711090},
  language = {eng},
}