Amyloid-like Self-Assembly of a Cellular Compartment
Publikation: Beitrag in Fachzeitschrift › Forschungsartikel › Beigetragen › Begutachtung
Beitragende
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.
Details
Originalsprache | Englisch |
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Seiten (von - bis) | 637-650 |
Seitenumfang | 14 |
Fachzeitschrift | Cell |
Jahrgang | 166 |
Ausgabenummer | 3 |
Publikationsstatus | Veröffentlicht - 28 Juli 2016 |
Peer-Review-Status | Ja |
Extern publiziert | Ja |
Externe IDs
PubMed | 27471966 |
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ORCID | /0000-0003-4017-6505/work/142253872 |
Schlagworte
ASJC Scopus Sachgebiete
Schlagwörter
- velo1