{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Motani K"],"funding":["MEXT | Japan Society for the Promotion of Science"],"pagination":["11174-11183"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7415991"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["295(32)"],"pubmed_abstract":["Stimulator of interferon genes (STING) mediates cytosolic DNA-induced innate immune signaling via membrane trafficking. The global identification of proteins that spatiotemporally interact with STING will provide a better understanding of its trafficking mechanisms and of STING signaling pathways. Proximity-dependent biotin identification (BioID) is a powerful technology to identify physiologically relevant protein-protein interactions in living cells. However, biotinylated peptides are rarely detected in the conventional BioID method, which uses streptavidin beads to pull down biotinylated proteins, because the biotin-streptavidin interaction is too strong. As a result, only nonbiotinylated peptides are identified, which cannot be distinguished from peptides of nonspecifically pull-downed"],"journal":["The Journal of biological chemistry"],"pubmed_title":["BioID screening of biotinylation sites using the avidin-like protein Tamavidin 2-REV identifies global interactors of stimulator of interferon genes (STING)."],"pmcid":["PMC7415991"],"funding_grant_id":["19H04966","20K07340","20K06628","18KK0229","17K08661"],"pubmed_authors":["Kosako H","Motani K"],"additional_accession":[]},"is_claimable":false,"name":"BioID screening of biotinylation sites using the avidin-like protein Tamavidin 2-REV identifies global interactors of stimulator of interferon genes (STING).","description":"Stimulator of interferon genes (STING) mediates cytosolic DNA-induced innate immune signaling via membrane trafficking. The global identification of proteins that spatiotemporally interact with STING will provide a better understanding of its trafficking mechanisms and of STING signaling pathways. Proximity-dependent biotin identification (BioID) is a powerful technology to identify physiologically relevant protein-protein interactions in living cells. However, biotinylated peptides are rarely detected in the conventional BioID method, which uses streptavidin beads to pull down biotinylated proteins, because the biotin-streptavidin interaction is too strong. As a result, only nonbiotinylated peptides are identified, which cannot be distinguished from peptides of nonspecifically pull-downed","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Aug","modification":"2025-04-05T12:03:30.476Z","creation":"2022-02-11T04:29:32.216Z"},"accession":"S-EPMC7415991","cross_references":{"pubmed":["32554809"],"doi":["10.1074/jbc.RA120.014323","10.1074/jbc.ra120.014323"]}}