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Related Experiment Video

Updated: Jul 14, 2026

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
09:47

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Published on: May 10, 2022

Ufl1-Mediated UFMylation Sustains Amelogenesis by Stabilizing RUNX2.

Da Liu1, Lin Chen1, Huning Xu2

  • 1Zhejiang Key Laboratory of Organ Development and Regeneration, College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, Zhejiang, China.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|July 13, 2026
PubMed
Summary

The UFMylation pathway

Keywords:
AmeloblastsAmelogenesis Imperfectadental enamelgene deletionprotein stabilitytooth development

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Last Updated: Jul 14, 2026

Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
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Comparative Strategies for Ubiquitination Detection in Mammalian Cell Lysates Using SMAD2/SMURF2 as a Model

Published on: April 17, 2026

Area of Science:

  • Biochemistry
  • Developmental Biology
  • Genetics

Background:

  • UFMylation is a critical post-translational modification regulating protein stability and tissue homeostasis.
  • Its specific role in amelogenesis, the process of tooth enamel formation, is not well understood.
  • UFL1 is the only known E3 ligase in the UFMylation pathway.

Purpose of the Study:

  • To investigate the function of UFL1 in mammalian enamel development.
  • To elucidate the molecular mechanisms underlying UFL1's role in amelogenesis.
  • To identify potential therapeutic targets for dental enamel defects.

Main Methods:

  • Utilized K14-Cre-mediated epithelial-specific Ufl1 knockout mice.
  • Performed transcriptomic profiling to analyze gene expression changes.
  • Investigated protein interactions between UFL1, DDRGK1, and RUNX2.

Main Results:

  • Ufl1 ablation led to severe amelogenesis imperfecta, characterized by impaired enamel deposition and hypomineralization.
  • Endoplasmic reticulum stress and dysregulated expression of enamel mineralization genes were observed.
  • UFL1-mediated UFMylation was found to stabilize RUNX2, a key regulator of amelogenesis.

Conclusions:

  • A novel UFMylation-RUNX2 regulatory axis essential for amelogenesis has been identified.
  • This study provides new mechanistic insights into amelogenesis imperfecta.
  • The findings suggest potential therapeutic targets for dental enamel defects.