Molecular basis for gβγ-effector interaction: Structural correlation with ga binding site

This work is a collaborative study by several laboratories directed at localizing sites of interaction between Gβγ, an important mediator of transmembrane signaling, and numerous downstream partners. To this end we have targeted residues on Gβγ that contact the Get subunit in the heterotrimeric complex, since Ga often acts as a negative regulator of Gβy. A traditional alanine scanning mutagenesis approach was used to evaluate the role of each amino acid residue within Ga binding surface of Gβ in the ability of dimer to interact with G-protein receptor kinase 2 (βARK). inward rectifying potassium channel (GIRK), and the a subunits of Ca-channels The data presented supports the idea that Gβγ interacts uniquely with different effectors, although sites of interaction can overlap.

Duke Scholars

Author Robert J. Lefkowitz Medicine, Cardiology

Author Nikolai Petrovich Skiba Ophthalmology