Mechanism of how augmin directly targets the γ-tubulin ring complex to microtubules.

TitleMechanism of how augmin directly targets the γ-tubulin ring complex to microtubules.
Publication TypeJournal Article
Year of Publication2018
AuthorsSong, J-G, King, MR, Zhang, R, Kadzik, RS, Thawani, A, Petry, S
JournalJ Cell Biol
Date Published2018 Jul 02
KeywordsAnimals, Cell Cycle Proteins, Humans, Microtubule-Associated Proteins, Microtubule-Organizing Center, Microtubules, Protein Binding, Protein Conformation, Spindle Apparatus, Tubulin, Xenopus laevis

<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'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>

Alternate JournalJ Cell Biol
PubMed ID29875259
PubMed Central IDPMC6028527
Grant ListDP2 GM123493 / GM / NIGMS NIH HHS / United States