PUBLICATION
Amyloid-like Self-Assembly of a Cellular Compartment
- Authors
- Boke, E., Ruer, M., Wühr, M., Coughlin, M., Lemaitre, R., Gygi, S.P., Alberti, S., Drechsel, D., Hyman, A.A., Mitchison, T.J.
- ID
- ZDB-PUB-170214-21
- Date
- 2016
- Source
- Cell 166: 637-50 (Journal)
- Registered Authors
- Keywords
- velo1
- MeSH Terms
-
- Amyloid/metabolism*
- Animals
- Female
- Fluorescent Dyes
- Mitochondria/metabolism
- Oocytes/cytology
- Organelle Biogenesis*
- Organelles/metabolism
- Prions/chemistry
- Protein Domains
- Protein Transport
- RNA, Messenger/metabolism
- Recombinant Fusion Proteins/genetics
- Recombinant Fusion Proteins/metabolism
- Sf9 Cells
- T-Box Domain Proteins/chemistry
- T-Box Domain Proteins/genetics
- T-Box Domain Proteins/metabolism*
- Thiazoles
- Xenopus Proteins/chemistry
- Xenopus Proteins/genetics
- Xenopus Proteins/metabolism*
- Xenopus laevis
- Zebrafish
- PubMed
- 27471966 Full text @ Cell
Citation
Boke, E., Ruer, M., Wühr, M., Coughlin, M., Lemaitre, R., Gygi, S.P., Alberti, S., Drechsel, D., Hyman, A.A., Mitchison, T.J. (2016) Amyloid-like Self-Assembly of a Cellular Compartment. Cell. 166:637-50.
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping