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The TRE17/USP6 oncogene: a riddle wrapped in a mystery inside an enigma

Andre M Oliveira1, Margaret M Chou

  • 1Department of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, MN, USA.

Frontiers in Bioscience (Scholar Edition)
|December 29, 2011
PubMed

Insights

Ubiquitin-specific protease 6 (USP6), also known as TRE17, is an oncogene involved in cell transformation. Recent studies highlight its role in aneurysmal bone cyst (ABC) pathogenesis.

Area of Science:

  • Molecular Biology
  • Oncology
  • Biochemistry

Background:

  • De-ubiquitinating enzymes (DUBs) regulate critical cellular processes like trafficking and transformation.
  • TRE17/USP6/Tre-2 is the first identified DUB oncogene, possessing both USP and TBC domains.
  • Despite its identification nearly two decades ago, TRE17's functions remain largely uncharacterized.

Purpose of the Study:

  • To review the latest findings on TRE17's molecular functions.
  • To elucidate the roles of TRE17's USP and TBC domains.
  • To explore TRE17's contribution to cell transformation and aneurysmal bone cyst (ABC) pathogenesis.

Main Methods:

  • Literature review of recent research on TRE17.
  • Analysis of studies investigating TRE17's USP and TBC domains.
  • Examination of proposed models for TRE17's role in oncogenesis.

Main Results:

  • TRE17 is implicated as a key etiological factor in aneurysmal bone cysts (ABCs).
  • Recent work has identified potential pathways through which TRE17 contributes to ABC development.
  • The dual functionality of TRE17's USP and TBC domains is crucial for its cellular roles.

Conclusions:

  • TRE17 plays a significant role in the pathogenesis of ABCs, a pediatric bone tumor.
  • Understanding TRE17's molecular mechanisms is vital for developing targeted therapies.
  • Further research is needed to fully elucidate TRE17's complex functions in cellular transformation.

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