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Journal of Undergraduate Research

Keywords

phosducin-like protein, eukaryotic cytosolic chaperonin, G protein coupled receptors, GPCRs

College

Physical and Mathematical Sciences

Department

Chemistry and Biochemistry

Abstract

Eukaryotic cells employ G protein coupled receptors (GPCRs) to detect various extracellular signaling molecules, including many that control cell proliferation. As a result, a knowledge of G protein pathway components and their mechanisms of interaction and regulation is essential in understanding cell transformation. Phosducin-like protein (PhLP) is a broadly expressed regulator of G protein signaling that exerts its effect by binding to G protein âã subunits [1-3]. When a signaling molecule binds to the extracellular surface of the receptor, it results in a conformational change in the receptor. This causes an interaction between the receptor and a heterotrimeric G protein on the intracellular surface of the membrane, catalyzing the exchange of GDP for GTP on the Gá subunit. In its GTP-bound conformation, Gá dissociates from the Gâã subunit complex and the receptor. Both GáGTP and Gâã are then free to interact with effector enzymes or ion channels and thereby regulate their activity. These effectors in turn control second messenger concentrations and kinase cascades that dictate intermediary metabolism, cell growth and differentiation [4-5].

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