ArticleNature communications2017
Molecular basis for protection of ribosomal protein L4 from cellular degradation.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 36 citations in OpenAlex.
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- A new Karyopherin-β2 binding PY-NLS epitope of HNRNPH2 linked to neurodevelopmental disorders.Structure (London, England : 1993) · 2023Article
- Dissecting the Nuclear Import of the Ribosomal Protein Rps2 (uS5).Biomolecules · 2023Article
- CRISPR-based oligo recombineering prioritizes apicomplexan cysteines for drug discovery.Nature microbiology · 2022Article
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- Mutant Presenilin 1 Dysregulates Exosomal Proteome Cargo Produced by Human-Induced Pluripotent Stem Cell Neurons.ACS omega · 2021Article
- Ubiquitin and Ubiquitin-Like Proteins and Domains in Ribosome Production and Function: Chance or Necessity?International journal of molecular sciences · 2021Review
- Transportin-1: A Nuclear Import Receptor with Moonlighting Functions.Frontiers in molecular biosciences · 2021Review
- Nonclassical nuclear localization signals mediate nuclear import of CIRBP.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- In vitro dimerization of human RIO2 kinase.RNA biology · 2019Article
- Tsr4 Is a Cytoplasmic Chaperone for the Ribosomal Protein Rps2 in Saccharomyces cerevisiae.Molecular and cellular biology · 2019Article
- Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME.Nucleic acids research · 2019Article
- Dual-Family Peptidylprolyl Isomerases (Immunophilins) of Select Monocellular Organisms.Biomolecules · 2018Review
- Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2.Nature communications · 2018Article
- Ribosomal protein L14 contributes to the early assembly of 60S ribosomal subunits in Saccharomyces cerevisiae.Nucleic acids research · 2018Article
- YAAM: Yeast Amino Acid Modifications Database.Database : the journal of biological databases and curation · 2018Article
- The full-length interleukin-33 (FLIL33)-importin-5 interaction does not regulate nuclear localization of FLIL33 but controls its intracellular degradation.The Journal of biological chemistry · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Eukaryotic ribosome biogenesis requires the nuclear import of ∼80 nascent ribosomal proteins and the elimination of excess amounts by the cellular degradation machinery. Assembly chaperones recognize nascent unassembled ribosomal proteins and transport them together with karyopherins to their nuclear destination. We report the crystal structure of ribosomal protein L4 (RpL4) bound to its dedicated assembly chaperone of L4 (Acl4), revealing extensive interactions sequestering 70 exposed residues of the extended RpL4 loop. The observed molecular recognition fundamentally differs from canonical promiscuous chaperone-substrate interactions. We demonstrate that the eukaryote-specific RpL4 extension harbours overlapping binding sites for Acl4 and the nuclear transport factor Kap104, facilitating its continuous protection from the cellular degradation machinery. Thus, Acl4 serves a dual function to facilitate nuclear import and simultaneously protect unassembled RpL4 from the cellular degradation machinery.
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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.