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Open AccessArticle

yRACK1/Asc1 proxiOMICs—Towards Illuminating Ships Passing in the Night

Department of Molecular Microbiology and Genetics, Institute of Microbiology and Genetics, Göttingen Center for Molecular Biosciences (GZMB), Georg-August-University Göttingen, 37077 Göttingen, Germany
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Cells 2019, 8(11), 1384; https://doi.org/10.3390/cells8111384
Received: 30 September 2019 / Revised: 25 October 2019 / Accepted: 29 October 2019 / Published: 4 November 2019
(This article belongs to the Special Issue 25 Years of Proteomics in Cell Biology)
Diverse signals and stress factors regulate the activity and homeostasis of ribosomes in all cells. The Saccharomyces cerevisiae protein Asc1/yRACK1 occupies an exposed site at the head region of the 40S ribosomal subunit (hr40S) 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 hr40S. 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, as well as the ubiquitin E3 ligase Hel2 as neighbors of Asc1. We observed Asc1-dependency of hr40S localization of mRNA-binding proteins and the Ubp3 co-factor Bre5. Hel2 and Ubp3-Bre5 are described to balance the mono-ubiquitination of Rps3 (uS3) during ribosome quality control. Here, we show that the absence of Asc1 resulted in massive exposure and accessibility of the C-terminal tail of its ribosomal neighbor Rps3 (uS3). Asc1 and some of its direct neighbors together might form a ribosomal decision tree that is tightly connected to close-by signaling modules. View Full-Text
Keywords: Asc1/RACK1; Rps2; Rps3; Ubp3-Bre5; Def1; Vps30; biotin identification; ribosome; translation; ribosome-associated quality control (RQC); autophagy; mRNA-binding protein Asc1/RACK1; Rps2; Rps3; Ubp3-Bre5; Def1; Vps30; biotin identification; ribosome; translation; ribosome-associated quality control (RQC); autophagy; mRNA-binding protein
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Schmitt, K.; Valerius, O. yRACK1/Asc1 proxiOMICs—Towards Illuminating Ships Passing in the Night. Cells 2019, 8, 1384.

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