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PBRM1 suppresses tumor growth as a novel p53 acetylation reader

Weijia Cai1, Liya Su1, Haifeng Yang1

  • 1Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, PA, USA.

Molecular & Cellular Oncology
|May 12, 2020
PubMed

Insights

Polybromo-1 (PBRM1) is identified as a key protein that binds to acetylated tumor antigen p53. This interaction is crucial for suppressing tumor growth in kidney cancer.

Area of Science:

  • Molecular biology
  • Cancer research
  • Biochemistry

Background:

  • The specific proteins that bind to acetylated tumor antigen p53 (a crucial tumor suppressor) were not well understood.
  • Identifying these "readers" is essential for understanding p53's function in cancer.

Purpose of the Study:

  • To identify the protein that binds to acetylated p53.
  • To investigate the role of this interaction in kidney cancer.

Main Methods:

  • Utilized biochemical assays to identify protein interactions with acetylated p53.
  • Generated and tested mutants of the identified protein (PBRM1) to assess functional impact.

Main Results:

  • Identified Polybromo-1 (PBRM1) as a reader of acetylated lysine382 on p53 via its bromodomain 4 (BD4).
  • PBRM1's BD4 domain is essential for supporting p53 transcriptional activity.
  • Mutants lacking functional PBRM1 BD4 failed to suppress tumor growth.

Conclusions:

  • PBRM1 binds to acetylated p53 through its BD4 domain.
  • PBRM1 acts as a tumor suppressor in kidney cancer by modulating p53 activity.
  • This finding provides a new therapeutic target for kidney cancer treatment.
Keywords:
PBRM1lysine acetylationp53renal cancer

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