Date of Award
Doctor of Philosophy (PhD)
It is well established that covalent lipid-modification of proteins can play an important role in the spatial and temporal organization of many intracellular signaling proteins. In particular, protein palmitoylation, the thioester linkage of a palmitate moiety to a cysteine residue, plays a critical role in promoting membrane binding. It also serves as a versatile sorting signal for membrane trafficking and precise microdomain partitioning. Classical studies using metabolic labeling have revealed that palmitoylation is dynamic, in which many substrates undergo palmitate cycling, and that turnover is regulated by extracellular signals. As such, the kinetics of palmitoylation cycling is dependent on the interplay between the palmitoyl transferases and thioesterases for efficient and precise localization and activity. Here, I present evidence for the regulation of GPCR signaling via protein depalmitoylation as well as the identification of a novel thioesterase that could potentially mediate this effect.
Chair and Committee
Kendall J Blumer
Thomas Baranski, Ron Bose, Michael Bruchas, Phyllis Hanson, Hanson Huettner
Maktabi, Mohammad H., "The Role of Reversible Palmitoylation in Regulating Diverse Biological Processes" (2015). Arts & Sciences Electronic Theses and Dissertations. 665.