PUBLICATION

Nanog safeguards early embryogenesis against global activation of maternal β-catenin activity by interfering with TCF factors

Authors
He, M., Zhang, R., Jiao, S., Zhang, F., Ye, D., Wang, H., Sun, Y.
ID
ZDB-PUB-200724-27
Date
2020
Source
PLoS Biology   18: e3000561 (Journal)
Registered Authors
He, Mudan, Sun, Yonghua, Ye, Ding
Keywords
none
MeSH Terms
  • Animals
  • Body Patterning/genetics
  • Cell Nucleus/metabolism
  • Embryonic Development/genetics*
  • Female
  • Gene Expression Regulation, Developmental
  • Gene Knockdown Techniques
  • Male
  • Mutation/genetics
  • Nanog Homeobox Protein/chemistry
  • Nanog Homeobox Protein/genetics
  • Nanog Homeobox Protein/metabolism*
  • Protein Binding
  • Protein Transport
  • Repressor Proteins/metabolism
  • Trans-Activators/metabolism*
  • Transcription, Genetic
  • Wnt Signaling Pathway/genetics
  • Zebrafish/embryology*
  • Zebrafish/genetics*
  • Zebrafish Proteins/chemistry
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/metabolism*
  • Zygote/metabolism
  • beta Catenin/metabolism*
PubMed
32702011 Full text @ PLoS Biol.
Abstract
Maternal β-catenin activity is essential and critical for dorsal induction and its dorsal activation has been thoroughly studied. However, how the maternal β-catenin activity is suppressed in the nondorsal cells remains poorly understood. Nanog is known to play a central role for maintenance of the pluripotency and maternal -zygotic transition (MZT). Here, we reveal a novel role of Nanog as a strong repressor of maternal β-catenin signaling to safeguard the embryo against hyperactivation of maternal β-catenin activity and hyperdorsalization. In zebrafish, knockdown of nanog at different levels led to either posteriorization or dorsalization, mimicking zygotic or maternal activation of Wnt/β-catenin activities, and the maternal zygotic mutant of nanog (MZnanog) showed strong activation of maternal β-catenin activity and hyperdorsalization. Although a constitutive activator-type Nanog (Vp16-Nanog, lacking the N terminal) perfectly rescued the MZT defects of MZnanog, it did not rescue the phenotypes resulting from β-catenin signaling activation. Mechanistically, the N terminal of Nanog directly interacts with T-cell factor (TCF) and interferes with the binding of β-catenin to TCF, thereby attenuating the transcriptional activity of β-catenin. Therefore, our study establishes a novel role for Nanog in repressing maternal β-catenin activity and demonstrates a transcriptional switch between β-catenin/TCF and Nanog/TCF complexes, which safeguards the embryo from global activation of maternal β-catenin activity.
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Human Disease / Model
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Mapping