{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Opitz N"],"funding":["Deutsche Forschungsgemeinschaft"],"pagination":["2199-2218"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5724181"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(12)"],"pubmed_abstract":["The Asc1 protein of <i>Saccharomyces cerevisiae</i> is a scaffold protein at the head region of ribosomal 40S that links mRNA translation to cellular signaling. In this study, proteins that colocalize with Asc1p were identified with proximity-dependent <i>Bio</i>tin <i>ID</i>entification (BioID), an <i>in vivo</i> labeling technique described here for the first time for yeast. Biotinylated Asc1p-birA*-proximal proteins were identified and quantitatively verified against controls applying SILAC and mass spectrometry. The mRNA-binding proteins Sro9p and Gis2p appeared together with Scp160p, each providing ribosomes with nuclear transcripts. The cap-binding protein eIF4E (Cdc33p) and the eIF3/a-subunit (Rpg1p) were identified reflecting the encounter of proteins involved in the initiation of "],"journal":["Molecular & cellular proteomics : MCP"],"pubmed_title":["Capturing the Asc1p/<i>R</i>eceptor for <i>A</i>ctivated <i>C K</i>inase <i>1</i> (RACK1) Microenvironment at the Head Region of the 40S Ribosome with Quantitative BioID in Yeast."],"pmcid":["PMC5724181"],"funding_grant_id":["GSC 226/2","VA352/2–1","SFB860"],"pubmed_authors":["Neumann B","Krebber H","Opitz N","Schmitt K","Hofer-Pretz V","Braus GH","Valerius O"],"additional_accession":[]},"is_claimable":false,"name":"Capturing the Asc1p/<i>R</i>eceptor for <i>A</i>ctivated <i>C K</i>inase <i>1</i> (RACK1) Microenvironment at the Head Region of the 40S Ribosome with Quantitative BioID in Yeast.","description":"The Asc1 protein of <i>Saccharomyces cerevisiae</i> is a scaffold protein at the head region of ribosomal 40S that links mRNA translation to cellular signaling. In this study, proteins that colocalize with Asc1p were identified with proximity-dependent <i>Bio</i>tin <i>ID</i>entification (BioID), an <i>in vivo</i> labeling technique described here for the first time for yeast. Biotinylated Asc1p-birA*-proximal proteins were identified and quantitatively verified against controls applying SILAC and mass spectrometry. The mRNA-binding proteins Sro9p and Gis2p appeared together with Scp160p, each providing ribosomes with nuclear transcripts. The cap-binding protein eIF4E (Cdc33p) and the eIF3/a-subunit (Rpg1p) were identified reflecting the encounter of proteins involved in the initiation of ","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Dec","modification":"2026-05-03T03:54:07.77Z","creation":"2019-03-27T00:09:22Z"},"accession":"S-EPMC5724181","cross_references":{"pubmed":["28982715"],"doi":["10.1074/mcp.M116.066654","10.1074/mcp.m116.066654"]}}