Amyloid-like Self-Assembly of a Cellular Compartment

被引:287
作者
Boke, Elvan [1 ]
Ruer, Martine [2 ]
Wuehr, Martin [1 ,3 ]
Coughlin, Margaret [1 ]
Lemaitre, Regis [2 ]
Gygi, Steven P. [3 ]
Alberti, Simon [2 ]
Drechsel, David [2 ]
Hyman, Anthony A. [2 ]
Mitchison, Timothy J. [1 ]
机构
[1] Harvard Med Sch, Dept Syst Biol, Boston, MA 02115 USA
[2] Max Planck Inst Mol Cell Biol & Genet, D-01307 Dresden, Germany
[3] Harvard Med Sch, Dept Cell Biol, Boston, MA 02115 USA
关键词
XENOPUS-LAEVIS; GERM PLASM; MITOCHONDRIAL CLOUD; FIBRIL FORMATION; BALBIANI BODY; MOUSE OOCYTES; NEURODEGENERATION; LOCALIZATION; DETERMINANTS; AGGREGATION;
D O I
10.1016/j.cell.2016.06.051
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:637 / 650
页数:14
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