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Wednesday, April 26 • 8:30am - 10:00am
Engineering of alternative lipidation sites in Gα13 to examine effects on growth signalling

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G proteins relay information from G-coupled protein receptors (GPCRs) to downstream molecular targets, driving large scale cellular process such as proliferation, differentiation, and migration. Overexpression of Gα13, a member of the G12/13 subfamily, is demonstrably oncogenic and has been implicated in breast, oral, esophageal and colon cancer. Lipidation is a post translational modification universal to G proteins, in which a fatty acid chain is attached to the protein, localizing it to the plasma membrane. These fatty acid adducts play a large role in how G proteins are regulated, and there is evidence they are involved in protein binding. Lipidations such as myristoylation (14:0) and palmitoylation (16:0) occur in all G proteins, sometimes in combination. Gα13 which is only palmitoylated, was previously engineered with PCR mutagenesis to remove amino acids necessary for palmitoylation to occur. These mutants were then modified at the N terminus with the DNA coding sequence from GαT and Gαi, both of which are myristoylated. Lysates from HEK 293 cells transfected with these plasmids were then tested for their ability to drive an SRE-luciferase assay. Loss of SRE signaling by non-palmitoylated chimeras was rescued by the addition of myristoylation sites. Future work will use GST fusion proteins to determine each chimera’s ability to bind with known G13 effectors.


Wednesday April 26, 2017 8:30am - 10:00am PDT
Concourse - Wilma Sherrill Center