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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
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The ubiquitin carboxyl hydrolase BAP1 forms a ternary complex with YY1 and HCF-1 and is a critical regulator of gene

Helen Yu1, Nazar Mashtalir, Salima Daou

  • 1University of Montréal, Maisonneuve-Rosemont Hospital Research Center, Department of Medicine, Montréal, Québec, Canada.

Molecular and Cellular Biology
|September 1, 2010
PubMed

Insights

The tumor suppressor BAP1 (deubiquitinating enzyme) directly interacts with transcription factors YY1 and HCF-1 to regulate gene expression. This reveals a novel mechanism linking ubiquitin signaling to cell growth and proliferation control.

Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Ubiquitin Signaling

Background:

  • The tumor suppressor BAP1, a deubiquitinating enzyme (DUB), regulates cell proliferation but its mechanisms are unclear.
  • BAP1 interacts with and deubiquitinates the transcriptional regulator HCF-1.

Purpose of the Study:

  • To elucidate the molecular mechanisms of BAP1 in transcriptional regulation.
  • To investigate the interaction of BAP1 with transcription factors HCF-1 and YY1.

Main Methods:

  • Co-immunoprecipitation assays to study protein interactions.
  • In vivo studies to confirm complex formation.
  • Reporter gene assays to assess transcriptional activity.
  • Analysis of gene expression changes.

Main Results:

  • BAP1 forms multiprotein complexes with HCF-1 and YY1.
  • BAP1 directly binds to YY1 via its coiled-coil motif.
  • HCF-1 mediates the interaction between BAP1 and YY1.
  • BAP1 activates transcription in an enzymatic-activity-dependent manner.
  • YY1 recruits BAP1 and HCF-1 to target gene promoters, like cox7c.

Conclusions:

  • BAP1 directly links to transcriptional control of genes involved in cell growth and proliferation.
  • A novel mechanism of transcription regulation involving ubiquitin signaling is uncovered.

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