Research Areas

There are four main areas of study in the Yang Laboratory.


S-acylproteomics

The Yang Laboratory has a long track record in characterizing the human S-acylproteome (also known as palmitoyl-proteome) and studying the roles of protein S-acylation (more commonly called palmitoylation) in cancer development and progression. The Yang Lab has developed a powerful S-acylproteomics technology termed palmitoyl protein identification and site characterization. Currently, the Yang Lab focus is on developing more powerful technologies for high-throughput, proteome-wide and site-specific analysis of protein S-acylation. In addition, by coupling the S-acylproteomics technologies with various molecular and cellular biology techniques, the lab is investigating the functions and substrate proteins of S-acylation enzymes that play key roles in prostate cancer metastasis and castration resistance.


Phosphoproteomics and Kinome Profiling

Kinases are a major class of drug targets for targeted cancer therapy. The Yang Laboratory has been characterizing the functions, substrates, and signaling pathways of receptor-interacting protein kinase 2 in prostate cancer.


Interactome Analysis

The Yang Laboratory applies label-free quantitative proteomics to identify components of specific protein complexes and uses TMT10plex-based multiplexed quantitative proteomics to study the global remodeling of protein complexes along cancer progression in tissue specimens.


Proteogenomics

Proteogenomics harnesses the power of next-generation sequencing and global proteome profiling to identify novel protein variants, which have a great potential of serving as novel cancer-specific biomarkers and neoantigens. The Yang Laboratory applied whole proteome sequencing to determine the copy numbers of more than 10,000 expressed proteins and to identify protein products of point mutations, unusual splice variants, 5' untranslated region translation and gene fusions. The Yang Lab also applied a high-throughput targeted mass spectrometry technology termed TOMAHAQ to quantify the expression levels of these novel proteogenomic variants in cancer tissue specimens and cell line models.