Abstract
Heterotrimeric guanine nucleotide binding proteins (G proteins), upon activation by cell surface G protein coupled receptors (GPCRs) via external stimuli, transmit signals to downstream pathways regulating a variety of cellular responses, such as cell proliferation and cytoskeletal rearrangements. The G12/13 subfamily of G proteins, consisting of Gα12 and Gα13, has been demonstrated to promote uncontrolled growth of cells and play a role in metastatic cancer progression. In diverse animal taxa from sea sponge to humans, the G12/13 subfamily of G proteins showed a highly conserved Q/Q amino acid pair at a precise structural position in the switch II region of G12/13 proteins, whereas mammalian Gα13 reverted back to E/K pair common to other G protein subfamilies. The reversion was studied by examining the binding of effector proteins to Gα13 containing a substitution for the Gα12 residues Q/Q at this position. The study shows that the preferential binding of TPR and E-cadherin to Gα12 may involve these specific residues.
How to Cite
Cho, S., (2015) “Effect of reverting switch II amino acids in Gα13 to their ancestral forms”, Capstone, The UNC Asheville Journal of Undergraduate Scholarship 28(1).
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