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Complexes between photoactivated rhodopsin and transducin: progress and questions Jastrzebska B; Tsybovsky Y; Palczewski KBiochem J 2010[Apr]; 428 (1): 1-10Activation of GPCRs (G-protein-coupled receptors) leads to conformational changes that ultimately initiate signal transduction. Activated GPCRs transiently combine with and activate heterotrimeric G-proteins resulting in GTP replacement of GDP on the G-protein alpha subunit. Both the detailed structural changes essential for productive GDP/GTP exchange on the G-protein alpha subunit and the structure of the GPCR-G-protein complex itself have yet to be elucidated. Nevertheless, transient GPCR-G-protein complexes can be trapped by nucleotide depletion, yielding an empty-nucleotide G-protein-GPCR complex that can be isolated. Whereas early biochemical studies indicated formation of a complex between G-protein and activated receptor only, more recent results suggest that G-protein can bind to pre-activated states of receptor or even couple transiently to non-activated receptor to facilitate rapid responses to stimuli. Efficient and reproducible formation of physiologically relevant, conformationally homogenous GPCR-G-protein complexes is a prerequisite for structural studies designed to address these possibilities.|Animals[MESH]|Heterotrimeric GTP-Binding Proteins/chemistry[MESH]|Humans[MESH]|Models, Biological[MESH]|Receptors, G-Protein-Coupled/chemistry[MESH]|Rhodopsin/*chemistry[MESH]|Signal Transduction[MESH]|Transducin/*chemistry[MESH] |
