PUBLICATION

VprBP mitigates TGF-β and Activin signaling by promoting Smurf1-mediated type I receptor degradation

Authors
Li, Y., Cui, C., Xie, F., Kiełbasa, S., Mei, H., van Dinther, M., van Dam, H., Bauer, A., Zhang, L., Ten Dijke, P.
ID
ZDB-PUB-190712-9
Date
2019
Source
Journal of molecular cell biology   12(2): 138-151 (Journal)
Registered Authors
Keywords
Activin, Smurf1, TGF-β type I receptor, mesoderm induction, ubiquitination
MeSH Terms
  • Activins/metabolism*
  • Activins/pharmacology
  • Animals
  • Embryonic Development/drug effects
  • Embryonic Development/genetics
  • Embryonic Stem Cells/metabolism
  • Gene Knockdown Techniques
  • HEK293 Cells
  • HaCaT Cells
  • Hep G2 Cells
  • Humans
  • Mesoderm/embryology
  • Mesoderm/metabolism
  • Mice
  • Protein Serine-Threonine Kinases/genetics
  • Protein Serine-Threonine Kinases/metabolism*
  • Proteolysis*
  • Receptor, Transforming Growth Factor-beta Type I/metabolism*
  • Smad7 Protein/genetics
  • Smad7 Protein/metabolism
  • Transfection
  • Transforming Growth Factor beta/metabolism*
  • Transforming Growth Factor beta/pharmacology
  • Ubiquitin-Protein Ligases/genetics
  • Ubiquitin-Protein Ligases/metabolism*
  • Ubiquitination/genetics
  • Zebrafish/embryology
PubMed
31291647 Full text @ J. Mol. Cell Biol.
Abstract
The transforming growth factor-β (TGF-β) family controls embryogenesis, stem cell differentiation and tissue homeostasis. However, how post-translation modifications contribute to fine-tuning of TGF-β family signaling responses is not well understood. Inhibitory (I)-Smads can antagonize TGF-β/Smad signaling by recruiting Smurf E3 ubiquitin ligases to target the active TGF-β receptor for proteasomal degradation. A proteomic interaction screen identified Vpr binding protein (VprBP) as novel binding partner of I-Smad7. Mis-expression studies revealed that VprBP negatively controls Smad2 phosphorylation, Smad2-Smad4 interaction, as well as TGF-β target gene expression. VprBP was found to promote Smad7-Smurf1-TβRI complex formation and induce proteasomal degradation of TGF-β type I receptor (TβRI). Moreover, VprBP appears to stabilize Smurf1 by suppressing Smurf1 poly-ubiquitination. In multiple adult and mouse embryonic stem cells, depletion of VprBP promotes TGF-β or Activin-induced responses. In the mouse embryo VprBP expression negatively correlates with mesoderm marker expression, and VprBP attenuated mesoderm induction during zebrafish embryogenesis. Our findings thereby uncover a novel regulatory mechanism by which Smurf1 controls the TGF-β and Activin cascade and identify VprBP as a critical determinant of embryonic mesoderm induction.
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