<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Motani K</submitter><funding>MEXT | Japan Society for the Promotion of Science</funding><pagination>11174-11183</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC7415991</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>295(32)</volume><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</pubmed_abstract><journal>The Journal of biological chemistry</journal><pubmed_title>BioID screening of biotinylation sites using the avidin-like protein Tamavidin 2-REV identifies global interactors of stimulator of interferon genes (STING).</pubmed_title><pmcid>PMC7415991</pmcid><funding_grant_id>19H04966</funding_grant_id><funding_grant_id>20K07340</funding_grant_id><funding_grant_id>20K06628</funding_grant_id><funding_grant_id>18KK0229</funding_grant_id><funding_grant_id>17K08661</funding_grant_id><pubmed_authors>Kosako H</pubmed_authors><pubmed_authors>Motani K</pubmed_authors></additional><is_claimable>false</is_claimable><name>BioID screening of biotinylation sites using the avidin-like protein Tamavidin 2-REV identifies global interactors of stimulator of interferon genes (STING).</name><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</description><dates><release>2020-01-01T00:00:00Z</release><publication>2020 Aug</publication><modification>2025-04-05T12:03:30.476Z</modification><creation>2022-02-11T04:29:32.216Z</creation></dates><accession>S-EPMC7415991</accession><cross_references><pubmed>32554809</pubmed><doi>10.1074/jbc.RA120.014323</doi><doi>10.1074/jbc.ra120.014323</doi></cross_references></HashMap>