UC Riverside

Phosphoproteomic analysis is a relatively recently devised method used to quantify a phosphoproteome and identify specific amino acid residues on proteins that are phosphorylated in order to further analyze their role in cellular processes. Our lab studies the role of the gene protein tyrosine phosphatase non-receptor Type 2 (PTPN2) in the intestinal epithelium. This gene codes for T-Cell Protein Tyrosine Phosphatase (TCPTP). Loss-of-function mutations in the PTPN2 gene locus are associated with an increased risk of developing several auto-inflammatory diseases such as Inflammatory Bowel Disease (IBD), Celiac Disease, Rheumatoid Arthritis and Type 1 Diabetes. Considering that our candidate gene codes for a phosphatase, we can hypothesize that this will have effect on the quantity and identity of phosphopeptides present. We hoped to find out how changes in the phosphoproteome in PTPN2 knockout (KO) mice compared to wild type (WT) mice. Surprisingly, we found no significant changes in the quantity of phosphoproteins and their residues, no significant changes in phosphorylation of TCPTP substrates, and no significant changes in the pathways identified as a result of the phosphorylated proteins between the two groups.