The tumor suppressor BAP1 cooperates with BRAFV600E to promote tumor formation in cutaneous melanoma

Pigment Cell Melanoma Res. 2019 Mar;32(2):269-279. doi: 10.1111/pcmr.12735. Epub 2018 Sep 24.

Abstract

The deubiquitinating enzyme BAP1 is mutated in a hereditary cancer syndrome with a high risk of mesothelioma and melanocytic tumors. Here, we show that Bap1 deletion in melanocytes cooperates with the constitutively active, oncogenic form of BRAF (BRAFV600E ) and UV to cause melanoma in mice, albeit at very low frequency. In addition, Bap1-null melanoma cells derived from mouse tumors are more aggressive and colonize and grow at distant sites more than their wild-type counterparts. Molecularly, Bap1-null melanoma cell lines have increased DNA damage measured by γH2aX and hyperubiquitination of histone H2a. Therapeutically, these Bap1-null tumors are completely responsive to BRAF- and MEK-targeted therapies. Therefore, BAP1 functions as a tumor suppressor and limits tumor progression in melanoma.

Keywords: BAP1; melanoma; tumor suppressor.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Carcinogenesis / genetics*
  • Carcinogenesis / pathology*
  • Cell Line, Tumor
  • Cell Proliferation
  • DNA Damage
  • Epithelial-Mesenchymal Transition / genetics
  • Gene Deletion
  • Gene Expression Regulation, Neoplastic
  • Histones / metabolism
  • Lung Neoplasms / genetics
  • Lung Neoplasms / pathology
  • Melanocytes / metabolism
  • Melanocytes / pathology
  • Melanoma / genetics*
  • Melanoma / pathology*
  • Melanoma, Cutaneous Malignant
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Mutation / genetics*
  • Proto-Oncogene Proteins B-raf / genetics*
  • Skin Neoplasms / genetics*
  • Skin Neoplasms / pathology*
  • Transcription, Genetic
  • Tumor Suppressor Proteins / metabolism*
  • Ubiquitin Thiolesterase / metabolism*
  • Ubiquitination

Substances

  • BAP1 protein, mouse
  • Histones
  • Tumor Suppressor Proteins
  • Proto-Oncogene Proteins B-raf
  • Ubiquitin Thiolesterase