The ubiquitin-conjugating enzyme UBE2O modulates c-Maf stability and induces myeloma cell apoptosis.

ABSTRACT:

Background

UBE2O is proposed as a ubiquitin-conjugating enzyme, but its function was largely unknown.

Methods

Mass spectrometry was applied to identify c-Maf ubiquitination-associated proteins. Immunoprecipitation was applied for c-Maf and UBE2O interaction. Immunoblotting was used for Maf protein stability. Luciferase assay was used for c-Maf transcriptional activity. Lentiviral infections were applied for UBE2O function in multiple myeloma (MM) cells. Flow cytometry and nude mice xenografts were applied for MM cell apoptosis and tumor growth assay, respectively.

Results

UBE2O was found to interact with c-Maf, a critical transcription factor in MM, by the affinity purification/tandem mass spectrometry assay and co-immunoprecipitation assays. Subsequent studies showed

SUBMITTER: Xu Y 

PROVIDER: S-EPMC5496436 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature