Date of Graduation

Fall 2019


Master of Natural and Applied Science in Biology



Committee Chair

Christopher Lupfer


NOD-like receptors, yeast-2-hybrid, inflammation, colitis, anti-inflammatory, ubiquitin, NF-κB, autoimmune disease

Subject Categories

Biological Phenomena, Cell Phenomena, and Immunity | Digestive System Diseases | Immune System Diseases | Medical Cell Biology | Medical Immunology | Medical Molecular Biology | Virus Diseases


The protein NOD- like receptor pyrin domain containing 12 (NLRP12) comes from a family of protein receptors with a wide range of functions including fertility as well as anti-inflammatory properties. The biological role of NLRP12 is poorly understood: research on the mechanisms behind its function and/or activation remains contradictory between different cell models. Current research suggests its involvement in a multi-protein complex named the inflammasome. The alternative hypothesis that has also been proposed is that NLRP12 is not a part of the inflammasome, rather it negatively regulates a transcription factor known as NF-��B down stream of Toll-like receptors. NLRP12 is important because if it is mutated, research has found it can cause severe inflammation in the colon (colitis) and even lead to certain types of colorectal cancer. Other experiments have shown that NLRP12 is also responsible for causing a wide range of autoimmune diseases in humans. Thus, if we can control NLRP12, we might be able to provide better treatments for these debilitating diseases. I propose that by performing a yeast-2-hybrid screen, that I can find new proteins that can unveil NLRP12’s function(s). My research has identified three ubiquitin associated proteins that interact with NLRP12; including: CUL3, RNF2, and COPS5 proteins. The functions of all three of these proteins lead me to believe NLRP12 may participate in a ubiquitin pathway to regulate inflammation. In addition, I found NLRP12 also interacted with IFIT1, which is known to interfere with virus infection and is also associated with ubiquitination. This new information could help provide details to unveiling how NLRP12 functions in relation to different proteins it interacts with in vivo.


© Abbigale Julia Brown

Open Access