Proteomics

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RPL12 phosphorylation regulates translation during mitosis - pSILAC HEK293 -

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 impact of posttranslational modifications has not yet been studied systematically. Analyzing ribosome heterogeneity is challenging since individual proteins can be part of different subcomplexes (40S, 60S, 80S and polysomes). Here, we develop polysome proteome profiling (3P) to obtain unbiased proteomic maps across ribosomal subcomplexes. 3P 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 3P fractions reveals that phosphorylation of serine 38 in RPL12 -- a known mitotic CDK1 substrate -- is strongly depleted in polysomes. Follow-up experiments confirm that RPL12 phosphorylation regulates translation of specific subsets of mRNAs during mitosis. Together, our results show that posttranslational modification of ribosomal proteins can regulate translation.

OTHER RELATED OMICS DATASETS IN: GSE112185GSE112186GSE112183GSE112187

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Koshi Imami  

LAB HEAD: Matthias Selbach

PROVIDER: PXD009267 | Pride | 2018-09-03

REPOSITORIES: Pride

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Publications

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

Imami Koshi K   Milek Miha M   Bogdanow Boris B   Yasuda Tomoharu T   Kastelic Nicolai N   Zauber Henrik H   Ishihama Yasushi Y   Landthaler Markus M   Selbach Matthias M  

Molecular cell 20180913 1

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 unbia  ...[more]

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