Screening and verification of proteins that interact with HSPC238.

摘要: HSPC238 is a recently identified tumor suppressor and demonstrates ubiquitin ligase E3 enzyme activity. was found to be significantly downregulated in human hepatocellular carcinoma (HCC) vivo inhibit the proliferation invasion of hepatoma cells vitro; however, underlying molecular mechanism largely unknown. In present study, we screened for proteins that physically interact with HSPC238. A bait vector yeast two-hybrid constructed gene cDNA. Yeast screening performed using fetal liver cDNA library. Multiple reporter assays, DNA sequencing BLAST comparison analysis were on positive clones. Protein interaction candidates further validated by confocal microscopy, co-immunoprecipitation pull-down assays. demonstrated 124 assays LacZ, HIS ADE2 selective media 12 genes. Further co-localization, HMOX1, RPS27A, ubiquitinB MT2A interacted These four are involved development progression, associated ubiquitin-proteasome pathway. Our results suggest may play role these via The identification validation interacting HSP238 lead discovery novel mechanisms through which suppresses tumorigenesis carcinoma.