Rxivist logo

Tdrd6a regulates the aggregation of Buc into functional subcellular compartments that drive germ cell specification

By Elke F. Roovers, Lucas JT Kaaij, Stefan Redl, Alfred W Bronkhorst, Kay Wiebrands, António Miguel de Jesus Domingues, Hsin-Yi Huang, Chung-Ting Han, Willi Salvenmoser, Dominic Grün, Falk Butter, Alexander van Oudenaarden, René F. Ketting

Posted 19 Feb 2018
bioRxiv DOI: 10.1101/267971 (published DOI: 10.1016/j.devcel.2018.07.009)

In recent years, it has become clear that phase separation represents an important class of subcellular compartmentalization. However, relatively little is known about how the formation or disassembly of such compartments is regulated. In zebrafish, the Balbiani body (Bb) and the germ plasm (Gp) are phase-separated structures essential for germ cell specification and home to many germ cell-specific mRNAs and proteins. Throughout development, these structures range from a single large aggregate (Bb), to a dispersed state and back to relatively large assemblies (Gp). Formation of the Bb requires Bucky ball (Buc), a protein with prion-like properties. We found that the multi-tudor domain-containing protein Tdrd6a interacts directly with Buc, affecting its mobility and aggregation properties. Importantly, lack of this regulatory interaction leads to significant defects in germ cell development. Our work presents a new mechanism for how prion-like protein-aggregations can be regulated and highlights the biological relevance of such regulatory events.

Download data

  • Downloaded 456 times
  • Download rankings, all-time:
    • Site-wide: 28,611 out of 76,982
    • In molecular biology: 852 out of 2,533
  • Year to date:
    • Site-wide: 71,133 out of 76,982
  • Since beginning of last month:
    • Site-wide: 68,559 out of 76,982

Altmetric data

Downloads over time

Distribution of downloads per paper, site-wide


Sign up for the Rxivist weekly newsletter! (Click here for more details.)