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Journal of Undergraduate Research

Keywords

G protein regulation, chaperonins, phosducin-like protein, PhLP

College

Physical and Mathematical Sciences

Department

Chemistry and Biochemistry

Abstract

G proteins participate in a myriad of cell signaling processes by shuttling information between cell surface receptors and intracellular effectors(1). The importance of G protein signaling is evidenced by the fact that ~5% of human genes encode G protein-coupled receptors, G protein subunits of effectors. Phosducin-like protein (PhLP) is a widely expressed protein with homology to the retinal photoreceptor protein phosducin(2). Like phosducin, PhLP binds G protein âã subunit complexes(3). Phosducin is believed to inhibit light signaling in photoreceptor cells as a part of the mechanism of light adaptation. Because of its homology to phosducin and its broad expression, PhLP has been hypothesized to be a general regulation of G protein signaling. However, the precise role of PhLP has not been elucidated. We have recently discovered that PhLP binds the chapreonin containing TCP1 (CCT) complexes and inhibits its function. CCT is a protein-folding chaperone, involved primarily in the proper folding of actins and tubulins. Thus, a potential link exists between G protein signaling and CCT-dependent protein folding through PhLP.

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