@article{60491,
  author = {Elvan Boke and Martine Ruer and Martin W{\"u}hr and Margaret Coughlin and Regis Lemaitre and Steven Gygi and Simon Alberti and David Drechsel and Anthony Hyman and Timothy Mitchison},
  title = {Amyloid-like Self-Assembly of a Cellular Compartment},
  abstract = { <p>Most vertebrate oocytes contain a Balbiani body, a<br>large, non-membrane-bound compartment packed<br>with RNA, mitochondria, and other organelles. Little<br>is known about this compartment, though it specifies<br>germline identity in many non-mammalian vertebrates.<br>We show Xvelo, a disordered protein with<br>an N-terminal prion-like domain, is an abundant constituent<br>of Xenopus Balbiani bodies. Disruption of the<br>prion-like domain of Xvelo, or substitution with a<br>prion-like domain from an unrelated protein, interferes<br>with its incorporation into Balbiani bodies<br>in vivo. Recombinant Xvelo forms amyloid-like networks<br>in vitro. Amyloid-like assemblies of Xvelo recruit<br>both RNA and mitochondria in binding assays.<br>We propose that Xenopus Balbiani bodies form by<br>amyloid-like assembly of Xvelo, accompanied by<br>co-recruitment of mitochondria and RNA. Prion-like<br>domains are found in germ plasm organizing proteins<br>in other species, suggesting that Balbiani<br>body formation by amyloid-like assembly could be<br>a conserved mechanism that helps oocytes function<br>as long-lived germ cells.</p> },
  year = {2016},
  journal = {Cell},
  volume = {166},
  pages = {637{\textendash}650},
  language = {eng},
}