Amyloid-like Self-Assembly of a Cellular Compartment

Elvan Boke, Martine Ruer, Martin Wühr, Margaret Coughlin, Regis Lemaitre, Steven P. Gygi, Simon Alberti, David Drechsel, Anthony A. Hyman, Timothy J. Mitchison

Research output: Contribution to journalArticlepeer-review

121 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)637-650
Number of pages14
JournalCell
Volume166
Issue number3
DOIs
StatePublished - Jul 28 2016
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)

Keywords

  • velo1

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