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The Mammalian Ribo-interactome Reveals Ribosome Functional Diversity and Heterogeneity
Open accessAbstract
During eukaryotic evolution, ribosomes have considerably increased in size, forming a surface-exposed ribosomal RNA (rRNA) shell of unknown function, which may create an interface for yet uncharacterized interacting proteins. To investigate such protein interactions, we establish a ribosome affinity purification method that unexpectedly identifies hundreds of ribosome-associated proteins (RAPs) from categories including metabolism and cell cycle, as well as RNA- and protein-modifying enzymes that functionally diversify mammalian ribosomes. By further characterizing RAPs, we discover the presence of ufmylation, a metazoan-specific post-translational modification (PTM), on ribosomes and define its direct substrates. Moreover, we show that the metabolic enzyme, pyruvate kinase muscle (PKM), interacts with sub-pools of endoplasmic reticulum (ER)-associated ribosomes, exerting a non-canonical function as an RNA-binding protein in the translation of ER-destined mRNAs. Therefore, RAPs interconnect one of life's most ancient molecular machines with diverse cellular processes, providing an additional layer of regulatory potential to protein expression.
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“This is characterized by the striated muscle-specific paralog RPL3L, which is prevalent in resting tissue. Following hypertrophic overload, RPL3L expression plummets and is replaced by the ubiquitous isoform RPL3.”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [189]
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“Rather than altering mRNA selectivity for contractile proteins, this paralog switch enables the RPL3-containing ribosomes to physically anchor to mitochondria, maximizing the local ATP supply required to sustain the massive energetic cost of hypertrophy [187,189].”
From Ribosome Biogenesis as a Putative Bottleneck to Skeletal Muscle Hypertrophy: Mechanisms, Human Evidence, and Practical Modulators (2026) · cites this paper as [189]
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The Sequence Alignment/Map format and SAMtools
Li, H., Handsaker, B., Wysoker, A., Fennell, T., Ruan, J., Homer, N., Marth, G., Abecasis, G., Durbin, R., & 1000 Genome Project Data Processing Subgroup (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp352 · Cited by 62,041
Fast gapped-read alignment with Bowtie 2
Langmead, B., & Salzberg, S. L. (2012) · Nature Methods · doi:10.1038/nmeth.1923 · Cited by 56,400
STAR: ultrafast universal RNA-seq aligner
Dobin, A., Davis, C. A., Schlesinger, F., Drenkow, J., Zaleski, C., Jha, S., Batut, P., Chaisson, M., & Gingeras, T. R. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts635 · Cited by 51,709
limma powers differential expression analyses for RNA-sequencing and microarray studies
Ritchie, M. E., Phipson, B., Wu, D., Hu, Y., Law, C. W., Shi, W., & Smyth, G. K. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv007 · Cited by 40,458
Cutadapt removes adapter sequences from high-throughput sequencing reads
Martin, M. (2011) · EMBnet.journal · doi:10.14806/ej.17.1.200 · Cited by 33,889
Multiplex Genome Engineering Using CRISPR/Cas Systems
Cong, L., Ran, F. A., Cox, D., Lin, S., Barretto, R., Habib, N., Hsu, P. D., Wu, X., Jiang, W., Marraffini, L. A., et al. (2013) · Science · doi:10.1126/science.1231143 · Cited by 15,339
The new frontier of genome engineering with CRISPR-Cas9
Doudna, J. A., & Charpentier, E. (2014) · Science · doi:10.1126/science.1258096 · Cited by 7,062
N6-methyladenosine Modulates Messenger RNA Translation Efficiency
Wang, X., Zhao, B. S., Roundtree, I. A., Lu, Z., Han, D., Ma, H., Weng, X., Chen, K., Shi, H., & He, C. (2015) · Cell · doi:10.1016/j.cell.2015.05.014 · Cited by 3,483
Thompson, A., Schäfer, J., Kuhn, K., Kienle, S., Schwarz, J., Schmidt, G., Neumann, T., & Hamon, C. (2003) · Analytical Chemistry · doi:10.1021/ac0262560 · Cited by 2,425
Ingolia, N. T., Lareau, L. F., & Weissman, J. S. (2011) · Cell · doi:10.1016/j.cell.2011.10.002 · Cited by 2,187
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Liu, F., Ma, M., Gao, A., Ma, F., Ma, G., Liu, P., Jia, C., Wang, Y., Donahue, K., Zhang, S., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021108065 · Cited by 63
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Nicolet, B. P., & Wolkers, M. C. (2022) · PLOS ONE · doi:10.1371/journal.pone.0276294 · Cited by 62
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Zang, Y., Xia, R., Yuan, J., Wu, H., Wang, Y., Li, H., Teng, H., & Sun, Z. (2024) · Briefings in Bioinformatics · doi:10.1093/bib/bbae023 · Cited by 56
Breindel, L., DeMott, C. M., Burz, D. S., & Shekhtman, A. G. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00938 · Cited by 55
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Milenkovic, I., Vieira, H. G. S., Lucas, M. C., Ruiz‐Orera, J., Patone, G., Kesteven, S. H., Wu, J., Feneley, M. P., Espadas, G., Sabidó, E., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad121 · Cited by 56
Wei, H. Y., Fan, X., Hu, Y., Tian, X., Guo, M., Mao, M., Fang, Z., Wu, P., Gao, S., Peng, C., et al. (2021) · 中国科学通报：英文版 · doi:10.1016/j.scib.2021.01.004 · Cited by 52
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Metadata
- Authors
- Simsek, D., Tiu, G. C., Flynn, R. A., Byeon, G. W., Leppek, K., Xu, A. F., Chang, H. Y., & Barna, M.
- Affiliations
- Stanford University (US)
- Stanford Medicine (US)
- Corresponding author
- Barna, Maria
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2017-06
- Volume
- 169
- Issue
- 6
- Pages
- 1051-1065.e18
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC5548193
- OpenAlex
- W2621126205
- Cited by
- 439
- References
- 74
- Citations by year
- 2026: 34 · 2025: 62 · 2024: 44 · 2023: 40 · 2022: 29 · 2021: 53 · 2020: 63 · 2019: 48 · 2018: 47 · 2017: 18
- FWCI
- 19.65
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- New York Stem Cell Foundation (NYSCF-R-I36)
- NIH Director’s New Innovator Award (7DP2OD008509, R21HD086730)
- Alfred P. Sloan Research Fellowship (BR2014)
- Mallinckrodt Foundation Award
- Pew Scholars Award (P50-HG007735, R01-HG004361, R01-ES023168)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- ribosome-associated proteins, ribosome heterogeneity, UFMylation, post-translational modification, RNA-binding proteins
- MeSH terms
- Thyroid Hormone-Binding Proteins, Animals, Carrier Proteins, Endoplasmic Reticulum, Membrane Proteins, Protein Processing, Post-Translational, Ribosomal Proteins, Ribosomes, Mass Spectrometry, Thyroid Hormones, Protein Biosynthesis, Protein Interaction Mapping, Ubiquitin-Protein Ligases, Mice, Embryonic Stem Cells
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