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A Scalable, Cell-Based Method for the Functional Assessment of Ube3a Variants
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RYBP modulates stability and function of Ring1B through targeting UBE3A.

Meng Li1, Shiqiang Zhang1, Wen Zhao1

  • 1Department of Biochemistry and Molecular Biology, State Key Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and School of Basic Medicine, Peking Union Medical College, Beijing, China; and.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|July 25, 2018
PubMed
Summary

Ring1 and yin yang 1-binding protein (RYBP) stabilizes Ring1B by targeting UBE3A for degradation. This enhances nc-PRC1 activity, impacting development and disease.

Keywords:
polycomb-repressive complex 1proteasomeprotein interactionubiquitination

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Area of Science:

  • Epigenetics
  • Molecular Biology
  • Developmental Biology

Background:

  • Noncanonical polycomb-repressive complex 1 (nc-PRC1) is crucial for development.
  • The precise role of RYBP within nc-PRC1 has remained unclear.
  • nc-PRC1 regulates gene expression through histone modification.

Purpose of the Study:

  • To elucidate the molecular function of RYBP in nc-PRC1.
  • To investigate how RYBP influences the stability and activity of Ring1B.
  • To understand the regulatory mechanism governing Ring1B within the nc-PRC1 complex.

Main Methods:

  • In vitro binding assays to detect RYBP-UBE3A interaction.
  • Ubiquitination assays to assess protein degradation pathways.
  • Western blotting to quantify protein levels of Ring1B and UBE3A.
  • Chromatin immunoprecipitation to analyze target gene regulation.

Main Results:

  • RYBP inhibits Ring1B polyubiquitination and proteasomal degradation, enhancing Ring1B stability and activity.
  • RYBP directly binds to UBE3A, promoting UBE3A ubiquitination and degradation.
  • Reduced UBE3A levels alleviate its degradation of Ring1B, leading to increased nc-PRC1-mediated transcriptional repression.

Conclusions:

  • RYBP acts as a critical regulator of nc-PRC1 stability and function by modulating Ring1B and UBE3A.
  • This mechanism is vital for normal development, stem cell maintenance, and has implications in carcinogenesis.
  • Findings provide a foundation for understanding RYBP's role in epigenetic regulation.