ArticleJournal of cell science2019
RACK1 evolved species-specific multifunctionality in translational control through sequence plasticity within a loop domain.
Article in Journal of cell science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Structural basis for emetine inhibition of ribosome translocation inbioRxiv : the preprint server for biology · 2026Article
- A Duality of Function: An Integrative Model of RACK1 as a Switch Between Translational and Signaling Hubs.International journal of molecular sciences · 2025Review
- Distinct non-canonical translation initiation modes arise for specific host and viral mRNAs during poxvirus-induced shutoff.Nature microbiology · 2025Article
- Ribosome customization and functional diversification among P-stalk proteins regulate late poxvirus protein synthesis.Cell reports · 2025Article
- The ribosome-associated protein RACK1 represses Kir4.1 translation in astrocytes and influences neuronal activity.Cell reports · 2023Article
- Ribosomes in poxvirus infection.Current opinion in virology · 2022Review
- RACK1 Regulates Poxvirus Protein Synthesis Independently of Its Role in Ribosome-Based Stress Signaling.Journal of virology · 2022Article
- Association of the receptor for activated C-kinase 1 with ribosomes in Plasmodium falciparum.The Journal of biological chemistry · 2022Article
- Negative charge in the RACK1 loop broadens the translational capacity of the human ribosome.Cell reports · 2021Article
- Targeting of eIF6-driven translation induces a metabolic rewiring that reduces NAFLD and the consequent evolution to hepatocellular carcinoma.Nature communications · 2021Article
- Proteomic and mechanistic dissection of the poxvirus-customized ribosome.Journal of cell science · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Receptor of activated protein C kinase 1 (RACK1) is a highly conserved eukaryotic protein that regulates several aspects of mRNA translation; yet, how it does so, remains poorly understood. Here we show that, although RACK1 consists largely of conserved β-propeller domains that mediate binding to several other proteins, a short interconnecting loop between two of these blades varies across species to control distinct RACK1 functions during translation. Mutants and chimeras revealed that the amino acid composition of the loop is optimized to regulate interactions with eIF6, a eukaryotic initiation factor that controls 60S biogenesis and 80S ribosome assembly. Separately, phylogenetics revealed that, despite broad sequence divergence of the loop, there is striking conservation of negatively charged residues amongst protists and dicot plants, which is reintroduced to mammalian RACK1 by poxviruses through phosphorylation. Although both charged and uncharged loop mutants affect eIF6 interactions, only a negatively charged plant - but not uncharged yeast or human loop - enhances translation of mRNAs with adenosine-rich 5' untranslated regions (UTRs). Our findings reveal how sequence plasticity within the RACK1 loop confers multifunctionality in translational control across species.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.