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G Protein - Guanine Nucleophile Binding Proteins
当然叫G更适当一些了!!!
A foundation for the 1994 Nobel Prize in Physiology or Medicine, guanine nucleotide binding proteins (G Proteins), so called because of their signaling mechanism, which depends on the dissociation of their alpha subunit from the beta and gamma subunit complex, stimulated by the exchange of guanine dinucleotide phosphate for guanine trinucleotide phosphate on the G subunit, are perhaps the most important signal transducing molecules in cells. In fact, diseases such as diabetes, alcoholism, and certain forms of pituitary cancer, among many others, are thought to have some root in the malfunction of g proteins, and thus a fundamental understanding of their function, signaling pathways and protein interactions may lead to eventual treatments and possibly the creation of various preventative approaches. There exist at least 20 different alpha subunits, which are separated into four main families; the stimulatory (Gαs), pertussis toxin sensitive inhibitory (Gαi), Go, and Gt, the Gq family which stimulates phospholipase C, and the G12/13 family important for regulating cytoskeleton, cell junctions and other processes. All G proteins transduce signals to intracellular effectors such as the example of adenylyl cyclase, which increase the second messenger cyclic Adenosine MonoPhosphate (cAMP). Second messengers then interact with other proteins down stream to cause a change in cell behavior. G subunits consist of two domains, the GTPase domain, and the alpha-helical domain. Both the α subunit and the β subunit complex act as signaling elements, capable of activating downstream molecules. The proteins operate with three “switches” which are located on the surfaces of the α subunit and are triggered by various regulators. These regulators effectively alter specific structures in the subunit, triggering the signaling pathway.
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