Abstract
Guanine nucleotide binding proteins (G-proteins) function as second messengers to modulate several cellular processes in response to external stimuli. The most extensively studied G-proteins are GNAT1, GNAS1, and GNAI1. The gene product of GNAT1 activates cGMP phosphodiesterase by coupling to photolyzed rhodopsin, while gene products of GNAS1 or GNAI1 stimulate or inhibit adenylate cyclase catalytic activity in hormone-sensitive systems, respectively. All three proteins are heterotrimers composed of alpha, beta, and gamma subunits, and the individual subunits share similar enzymatic properties. The alpha subunits bind guanyl nucleotides and catalyze the hydrolysis of GTP to GDP and Pi. In addition to GNAT1, which has been localized to chromosome 3, other alpha G-proteins have also been cloned and mapped. Because of its exclusive retinal expression, regional mapping of the GNAT1 locus would facilitate linkage studies of inherited retinal diseases. Using in situ hybridization, the authors have localized the GNAT1 locus to 3p22.
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