{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["96(9)"],"submitter":["Kisselev OG"],"pubmed_abstract":["Photoactivation of the retinal photoreceptor rhodopsin proceeds through a cascade of intermediates, resulting in protein-protein interactions catalyzing the activation of the G-protein transducin (Gt). Using stabilization and photoregeneration of the receptor's signaling state and Gt activation assays, we provide evidence for a two-site sequential fit mechanism of Gt activation. We show that the C-terminal peptide from the Gt gamma-subunit, Gtgamma(50-71)farnesyl, can replace the holoprotein in stabilizing rhodopsin's active intermediate metarhodopsin II (MII). However, the peptide cannot replace the Gtbeta gamma complex in direct activation assays. Competition by Gtgamma(50-71)farnesyl with Gt for the active receptor suggests a pivotal role for Gtbeta gamma in signal transfer from MII to "],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["4898-903"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC21788"],"repository":["biostudies-literature"],"pubmed_title":["Signal transfer from rhodopsin to the G-protein: evidence for a two-site sequential fit mechanism."],"pmcid":["PMC21788"],"pubmed_authors":["Meyer CK","Kisselev OG","Heck M","Ernst OP","Hofmann KP"],"additional_accession":[]},"is_claimable":false,"name":"Signal transfer from rhodopsin to the G-protein: evidence for a two-site sequential fit mechanism.","description":"Photoactivation of the retinal photoreceptor rhodopsin proceeds through a cascade of intermediates, resulting in protein-protein interactions catalyzing the activation of the G-protein transducin (Gt). Using stabilization and photoregeneration of the receptor's signaling state and Gt activation assays, we provide evidence for a two-site sequential fit mechanism of Gt activation. We show that the C-terminal peptide from the Gt gamma-subunit, Gtgamma(50-71)farnesyl, can replace the holoprotein in stabilizing rhodopsin's active intermediate metarhodopsin II (MII). However, the peptide cannot replace the Gtbeta gamma complex in direct activation assays. Competition by Gtgamma(50-71)farnesyl with Gt for the active receptor suggests a pivotal role for Gtbeta gamma in signal transfer from MII to ","dates":{"release":"1999-01-01T00:00:00Z","publication":"1999 Apr","modification":"2025-05-29T19:44:14.631Z","creation":"2019-03-27T00:17:48Z"},"accession":"S-EPMC21788","cross_references":{"pubmed":["10220390"],"doi":["10.1073/pnas.96.9.4898"]}}