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USP26 functions as a negative regulator of cellular reprogramming by stabilising PRC1 complex components

Bo Ning1, Wei Zhao1,2, Chen Qian1

  • 1Center for Inflammation and Epigenetics, Houston Methodist Research Institute, Houston, TX, 77030, USA.

Nature Communications
|August 26, 2017
PubMed

Insights

Ubiquitin-specific protease 26 negatively regulates somatic cell reprogramming. It stabilizes key proteins in Polycomb-Repressive Complex 1, repressing pluripotency gene expression.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Epigenetics

Background:

  • Somatic cell reprogramming is crucial for regenerative medicine, but its regulatory mechanisms, especially negative regulation, are poorly understood.
  • The ubiquitin-proteasome system plays a role in regulating reprogramming by degrading pluripotency factors.

Purpose of the Study:

  • To investigate the role of ubiquitin-specific protease 26 (USP26) in the negative regulation of somatic cell reprogramming.
  • To elucidate the molecular mechanism by which USP26 influences reprogramming.

Main Methods:

  • Investigated the interaction between USP26 and Polycomb-Repressive Complex 1 (PRC1) components.
  • Analyzed the ubiquitination status of CBX4 and CBX6 proteins.
  • Assessed the impact of USP26 on pluripotency gene expression (Sox2, Nanog) and histone modifications.

Main Results:

  • USP26 was found to negatively regulate somatic cell reprogramming.
  • USP26 deubiquitinates CBX4 and CBX6 by removing K48-linked polyubiquitination, thereby stabilizing these PRC1 components.
  • Stabilized CBX4 and CBX6 lead to repression of pluripotency genes (Sox2, Nanog) via PRC1-mediated histone H2A ubiquitination at their promoters.

Conclusions:

  • USP26 plays a critical role in the negative regulation of somatic cell reprogramming.
  • USP26 functions through the Polycomb-Repressive Complex 1 pathway by stabilizing CBX4 and CBX6, ultimately repressing pluripotency gene expression.

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