@article {957081,
	title = {Amyloid-like Self-Assembly of a Cellular Compartment},
	journal = {Cell},
	volume = {166},
	number = {3},
	year = {2016},
	month = {2016 Jul 28},
	pages = {637-50},
	abstract = {Most vertebrate oocytes contain a Balbiani body, a large, non-membrane-bound compartment packed with RNA, mitochondria, and other organelles. Little is known about this compartment, though it specifies germline identity in many non-mammalian vertebrates. We show Xvelo, a disordered protein with an N-terminal prion-like domain, is an abundant constituent of Xenopus Balbiani bodies. Disruption of the prion-like domain of Xvelo, or substitution with a prion-like domain from an unrelated protein, interferes with its incorporation into Balbiani bodies in~vivo. Recombinant Xvelo forms amyloid-like networks in~vitro. Amyloid-like assemblies of Xvelo recruit both RNA and mitochondria in binding assays. We propose that Xenopus Balbiani bodies form by amyloid-like assembly of Xvelo, accompanied by co-recruitment of mitochondria and RNA. Prion-like domains are found in germ plasm organizing proteins~in other species, suggesting that Balbiani body formation by amyloid-like assembly could be a conserved mechanism that helps oocytes function as long-lived germ cells.},
	keywords = {Amyloid, Animals, Female, Fluorescent Dyes, Mitochondria, Oocytes, Organelle Biogenesis, Organelles, Prions, Protein Domains, Protein Transport, Recombinant Fusion Proteins, RNA, Messenger, Sf9 Cells, T-Box Domain Proteins, Thiazoles, Xenopus laevis, Xenopus Proteins, Zebrafish},
	issn = {1097-4172},
	doi = {10.1016/j.cell.2016.06.051},
	author = {Boke, Elvan and Ruer, Martine and W{\"u}hr, Martin and Coughlin, Margaret and Lemaitre, Regis and Gygi, Steven P and Alberti, Simon and Drechsel, David and Hyman, Anthony a and Mitchison, Timothy J.}
}
