Understanding the Chaperone Code
Proteins have to form into specific shapes for them to be able to carry out their specific jobs in cells. This "protein origami" is carried out by proteins called Chaperones. Our laboratory is centered on understanding the role and regulation of the Hsp70 chaperone which is found in all cells from bacteria to humans. Because Hsp70 helps fold proteins, it can keep mutated cancer proteins active. On the other hand, Hsp70 can break apart toxic proteins that cause neurodegenerative illnesses such as Huntington's disease, Alzheimer's disease and Amyotrophic Lateral Sclerosis (ALS).
In particular, we are interested in modifications that are added to Hsp70 as it goes about its job in the cell, known as the "Chaperone Code". Our goal is to understand this Hsp70 chaperone code at both a basic level and in human illnesses that include cancer and neurodegenerative disease.
Our group is multidisciplinary, integrating biochemistry, biophysics, structural biology and proteomics. We study these chaperone dynamics in a range of systems including purified proteins, bacteria, budding yeast and in cancer cell lines.
Check out our new publication "Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications" in PLOS Biology [link]
Our team is a vibrant mix of undergraduate and graduate trainees, technicians and post-doctoral researchers who study all aspects of the chaperone code from an evolutionary perspective through to implications for human disease. Meet the team here!
Our Research Team
About
Our Space
Dr. Truman’s laboratory (approximately 1200 sq. ft.) is located in Woodward Hall, a state-of-the-art science and technology building on the UNC Charlotte campus. In addition, a dedicated cell culture room (150 sq. ft.) are included in his lab. His laboratory is one of the Biomedical Research Groups in the Department of Biological Sciences, occupying more than 18,000 sq. ft. of laboratory space in total.
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