Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Cell July 28, 2016; 166 (3): 637-650.
Show Gene links Show Anatomy links

Amyloid-like Self-Assembly of a Cellular Compartment.

Boke E , Ruer M , Wühr M , Coughlin M , Lemaitre R , Gygi SP , Alberti S , Drechsel D , Hyman AA , Mitchison TJ .

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.

PubMed ID: 27471966
PMC ID: PMC5082712
Article link: Cell
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: prnp

References [+] :
Alberti, A systematic survey identifies prions and illuminates sequence features of prionogenic proteins. 2009, Pubmed