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Mol Cell. 2018 Oct 4;72(1):84-98.e9. doi: 10.1016/j.molcel.2018.08.019. Epub 2018 Sep 13.

Phosphorylation of the Ribosomal Protein RPL12/uL11 Affects Translation during Mitosis.

Author information

1
Max Delbrück Center for Molecular Medicine, Robert-Rössle-Str. 10, 13092 Berlin, Germany; Department of Molecular and Cellular BioAnalysis, Kyoto University, 606-8501 Kyoto, Japan. Electronic address: imami.koshi.3z@kyoto-u.ac.jp.
2
Max Delbrück Center for Molecular Medicine, Robert-Rössle-Str. 10, 13092 Berlin, Germany.
3
Department of Molecular and Cellular BioAnalysis, Kyoto University, 606-8501 Kyoto, Japan.
4
Max Delbrück Center for Molecular Medicine, Robert-Rössle-Str. 10, 13092 Berlin, Germany; IRI Life Sciences, Institute für Biologie, Humboldt Universität zu Berlin, Philippstraße 13, 10115 Berlin, Germany.
5
Max Delbrück Center for Molecular Medicine, Robert-Rössle-Str. 10, 13092 Berlin, Germany; Charité-Universitätsmedizin Berlin, 10117 Berlin, Germany. Electronic address: matthias.selbach@mdc-berlin.de.

Abstract

Emerging evidence indicates that heterogeneity in ribosome composition can give rise to specialized functions. Until now, research mainly focused on differences in core ribosomal proteins and associated factors. The effect of posttranslational modifications has not been studied systematically. Analyzing ribosome heterogeneity is challenging because individual proteins can be part of different subcomplexes (40S, 60S, 80S, and polysomes). Here we develop polysome proteome profiling to obtain unbiased proteomic maps across ribosomal subcomplexes. Our method combines extensive fractionation by sucrose gradient centrifugation with quantitative mass spectrometry. The high resolution of the profiles allows us to assign proteins to specific subcomplexes. Phosphoproteomics on the fractions reveals that phosphorylation of serine 38 in RPL12/uL11, a known mitotic CDK1 substrate, is strongly depleted in polysomes. Follow-up experiments confirm that RPL12/uL11 phosphorylation regulates the translation of specific subsets of mRNAs during mitosis. Together, our results show that posttranslational modification of ribosomal proteins can regulate translation.

KEYWORDS:

RNA; cell cycle; mitosis; phosphoproteomics; phosphorylation; protein-protein interaction; proteomics; ribosome; ribosome heterogeneity; translation

PMID:
30220558
DOI:
10.1016/j.molcel.2018.08.019
[Indexed for MEDLINE]
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