G proteins (guanine nucleotide-binding proteins) are a family of proteins involved in transmitting chemical signals outside the cell, and causing changes inside the cell. They communicate signals from many hormones, neurotransmitters, and other signaling factors. 
G protein-coupled receptors are transmembrane receptors. Signal molecules bind to a domain located outside the cell. An intracellular domain activates a G protein. The G protein activates a cascade of further compounds, and finally causes a change downstream in the cell.
G protein complexes bind to phosphate groups. They function as molecular switches. When they are attached to a complex with three phosphate groups (guanosine triphosphate [GTP]), they turn on. When they are attached to a complex with only two phosphate groups (guanosine diphosphate [GDP]), they turn off.
G proteins regulate metabolic enzymes, ion channels, transporters, and other parts of the cell machinery, controlling transcription, motility, contractility, and secretion, which in turn regulate systemic functions such as embryonic development, learning and memory, and homeostasis.
G proteins were discovered when Alfred G. Gilman and Martin Rodbell investigated stimulation of cells by adrenaline. They found that, when adrenaline binds to a receptor, the receptor does not stimulate enzymes directly. Instead, the receptor stimulates a G protein, which stimulates an enzyme. An example is adenylate cyclase, which produces the second messenger cyclic AMP. For this discovery, they won the 1994 Nobel Prize in Physiology or Medicine.
G proteins belong to the larger group of enzymes called GTPases.
G proteins are important signal transducing molecules in cells. "Malfunction of GPCR [G Protein-Coupled Receptor] signaling pathways are involved in many diseases, such as diabetes, blindness, allergies, depression, cardiovascular defects, and certain forms of cancer. It is estimated that more than half of the modern drugs' cellular targets are GPCRs." 
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