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

Koshi Imami, Miha Milek, Boris Bogdanow, Tomoharu Yasuda, Nicolai Kastelic, Henrik Zauber, Yasushi Ishihama, Markus Landthaler, Matthias Selbach

Research output: Contribution to journalArticlepeer-review

57 Citations (Scopus)


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. Multiple regulatory layers shape gene expression. Imami et al. show that protein production in mitosis can be regulated by phosphorylation of the ribosomal protein RPL12/uL11.

Original languageEnglish
Pages (from-to)84-98.e9
JournalMolecular Cell
Issue number1
Publication statusPublished - Oct 4 2018

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology


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