Characterizing the Interaction Between Polo-like Kinase 4 (PLK4) and Janus Kinase 2 (JAK2) Proteins
Standing
Undergraduate
Type of Proposal
Oral Research Presentation
Challenges Theme
Open Challenge
Faculty Sponsor
Dr. John Hudson
Proposal
The role of the protein Janus kinase 2 (JAK2) in the cell is not completely understood. Our objective is to further characterize JAK2 and determine whether it can activate another protein called Polo-like kinase 4 (PLK4). PLK4 is a key regulator of animal cell duplication through cellular structures called centrosomes, which play an important role cell division. JAK2 has previously been shown to localize to these centrosome, and PLK4 was shown to have structural sites that are compatible with JAK2 protein. The two proteins also form a complex in a purification technique known as co-immunoprecipitation. To further examine the interactions between JAK2 and PLK4, we use two animal cell lines that were genetically manipulated to express modified forms of each protein. First, protein extraction and quantification of JAK2 and PLK4 proteins from these cell lines is performed. Subsequently, JAK2 protein is purified and then a kinase assay with PLK4 is performed. This kinase assay confirms the interaction of the two proteins, in which JAK2 places a functional phosphate group on the compatible sites of PLK4. Determination of the function of this interaction and whether it plays a role in activating PLK4 and cell duplication is relevant to the study of cancer, a field known as oncology. When aiming to kill cancerous cells, it is important to understand how certain proteins are involved in their growth. Being able to inhibit these specific proteins could potentially act as a treatment in cancer tissue.
Grand Challenges
Viable, Healthy and Safe Communities
Characterizing the Interaction Between Polo-like Kinase 4 (PLK4) and Janus Kinase 2 (JAK2) Proteins
The role of the protein Janus kinase 2 (JAK2) in the cell is not completely understood. Our objective is to further characterize JAK2 and determine whether it can activate another protein called Polo-like kinase 4 (PLK4). PLK4 is a key regulator of animal cell duplication through cellular structures called centrosomes, which play an important role cell division. JAK2 has previously been shown to localize to these centrosome, and PLK4 was shown to have structural sites that are compatible with JAK2 protein. The two proteins also form a complex in a purification technique known as co-immunoprecipitation. To further examine the interactions between JAK2 and PLK4, we use two animal cell lines that were genetically manipulated to express modified forms of each protein. First, protein extraction and quantification of JAK2 and PLK4 proteins from these cell lines is performed. Subsequently, JAK2 protein is purified and then a kinase assay with PLK4 is performed. This kinase assay confirms the interaction of the two proteins, in which JAK2 places a functional phosphate group on the compatible sites of PLK4. Determination of the function of this interaction and whether it plays a role in activating PLK4 and cell duplication is relevant to the study of cancer, a field known as oncology. When aiming to kill cancerous cells, it is important to understand how certain proteins are involved in their growth. Being able to inhibit these specific proteins could potentially act as a treatment in cancer tissue.