RT Journal Article
SR Electronic
T1 Tdrd6a regulates the aggregation of Buc into functional subcellular compartments that drive germ cell specification
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 267971
DO 10.1101/267971
A1 Elke F. Roovers
A1 Lucas J.T. Kaaij
A1 Stefan Redl
A1 Alfred W. Bronkhorst
A1 Kay Wiebrands
A1 António M. de Jesus Domingues
A1 Hsin-Yi Huang
A1 Chung-Ting Han
A1 Willi Salvenmoser
A1 Dominic Grün
A1 Falk Butter
A1 Alexander van Oudenaarden
A1 René F. Ketting
YR 2018
UL http://biorxiv.org/content/early/2018/02/19/267971.abstract
AB 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.