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Phosphorylation of the ribosomal protein RPL12/uL11 affects translation during mitosis

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Item Type:Article
Title:Phosphorylation of the ribosomal protein RPL12/uL11 affects translation during mitosis
Creators Name:Imami, K., Milek, M., Bogdanow, B., Yasuda, T., Kastelic, N., Zauber, H., Ishihama, Y., Landthaler, M. and Selbach, M.
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:Proteomics, Ribosome, Ribosome Heterogeneity, Translation, Phosphorylation, Phosphoproteomics, RNA, Mitosis, Cell Cycle, Protein-Protein Interaction
Source:Molecular Cell
Publisher:Elsevier / Cell Press
Page Range:84-98
Date:4 October 2018
Additional Information:Copyright © 2018. This manuscript version is made available under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
Official Publication:https://doi.org/10.1016/j.molcel.2018.08.019
PubMed:View item in PubMed

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