<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Schmitt K</submitter><funding>Deutsche Forschungsgemeinschaft</funding><pagination>E1384</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6912217</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>8(11)</volume><pubmed_abstract>Diverse signals and stress factors regulate the activity and homeostasis of ribosomes in all cells. The &lt;i>Saccharomyces cerevisiae&lt;/i> protein Asc1/yRACK1 occupies an exposed site at the head region of the 40S ribosomal subunit (&lt;i>hr40S&lt;/i>) and represents a central hub for signaling pathways. Asc1 strongly affects protein phosphorylation and is involved in quality control pathways induced by translation elongation arrest. Therefore, it is important to understand the dynamics of protein formations in the Asc1 microenvironment at the &lt;i>hr40S&lt;/i>. We made use of the in vivo protein-proximity labeling technique Biotin IDentification (BioID). Unbiased proxiOMICs from two adjacent perspectives identified nucleocytoplasmic shuttling mRNA-binding proteins, the deubiquitinase complex Ubp3-Bre5,</pubmed_abstract><journal>Cells</journal><pubmed_title>yRACK1/Asc1 proxiOMICs-Towards Illuminating Ships Passing in the Night.</pubmed_title><pmcid>PMC6912217</pmcid><funding_grant_id>VA 352/2-2</funding_grant_id><funding_grant_id>A 630 (ZUK41/1)</funding_grant_id><funding_grant_id>INST 186/1230-1 FUGG</funding_grant_id><pubmed_authors>Schmitt K</pubmed_authors><pubmed_authors>Valerius O</pubmed_authors></additional><is_claimable>false</is_claimable><name>yRACK1/Asc1 proxiOMICs-Towards Illuminating Ships Passing in the Night.</name><description>Diverse signals and stress factors regulate the activity and homeostasis of ribosomes in all cells. The &lt;i>Saccharomyces cerevisiae&lt;/i> protein Asc1/yRACK1 occupies an exposed site at the head region of the 40S ribosomal subunit (&lt;i>hr40S&lt;/i>) and represents a central hub for signaling pathways. Asc1 strongly affects protein phosphorylation and is involved in quality control pathways induced by translation elongation arrest. Therefore, it is important to understand the dynamics of protein formations in the Asc1 microenvironment at the &lt;i>hr40S&lt;/i>. We made use of the in vivo protein-proximity labeling technique Biotin IDentification (BioID). Unbiased proxiOMICs from two adjacent perspectives identified nucleocytoplasmic shuttling mRNA-binding proteins, the deubiquitinase complex Ubp3-Bre5,</description><dates><release>2019-01-01T00:00:00Z</release><publication>2019 Nov</publication><modification>2026-04-08T03:02:15.943Z</modification><creation>2020-05-22T07:11:36Z</creation></dates><accession>S-EPMC6912217</accession><cross_references><pubmed>31689955</pubmed><doi>10.3390/cells8111384</doi></cross_references></HashMap>