ArticleMolecular and cellular biology2011
The chaperone network connected to human ribosome-associated complex.
Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 87 citations in OpenAlex.
- Nascent chain folding status modulates ribosome dynamics and mRNA stability through the ribosome-associated chaperone Zuo1.Molecular cell · 2026Article
- Ago1 is required for the regulation of mitochondrial translation under heat stress in Schizosaccharomyces pombe.The Journal of biological chemistry · 2026Article
- The cotranslational cycle of the ribosome-bound Hsp70 homolog Ssb.Nature communications · 2026Article
- Developmentally-regulated post-apocrine cell death ofFrontiers in cell and developmental biology · 2026Article
- Mechanosensor-mediated Hsp70 phosphorylation orchestrates the landscape of the heat shock response.Nature communications · 2025Article
- Diphthamide synthesis is linked to the eEF2-client chaperone machinery.FEBS letters · 2025Article
- Chaperone Hsp70 helps Salmonella survive infection-relevant stress by reducing protein synthesis.PLoS biology · 2024Article
- The ribosome-associated chaperone Zuo1 controls translation upon TORC1 inhibition.The EMBO journal · 2023Article
- Yeast Chaperone Hsp70-Ssb Modulates a Variety of Protein-Based Heritable Elements.International journal of molecular sciences · 2023Article
- Exploration of the truncated cytosolic Hsp70 in plants - unveiling the diverse T1 lineage and the conserved T2 lineage.Frontiers in plant science · 2023Article
- Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications.PLoS biology · 2022Article
- The APE2 Exonuclease Is a Client of the Hsp70-Hsp90 Axis in Yeast and Mammalian Cells.Biomolecules · 2022Article
- Structural remodeling of ribosome associated Hsp40-Hsp70 chaperones during co-translational folding.Nature communications · 2022Article
- The C-terminal domain of Hsp70 is responsible for paralog-specific regulation of ribonucleotide reductase.PLoS genetics · 2022Article
- Pathway of Hsp70 interactions at the ribosome.Nature communications · 2021Article
- Dual roles of HSP70 chaperone HSPA1 in quality control of nascent and newly synthesized proteins.The EMBO journal · 2021Article
- A role for the ribosome-associated complex in activation of the IRE1 branch of UPR.Cell reports · 2021Article
- Evolution of chaperome gene expression and regulatory elements in the antarctic notothenioid fishes.Heredity · 2021Article
- Insights into the Molecular Basis of Genome Stability and Pristine Proteostasis in Naked Mole-Rats.Advances in experimental medicine and biology · 2021Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mammalian ribosome-associated complex (mRAC), consisting of the J-domain protein MPP11 and the atypical Hsp70 homolog (70-homolog) Hsp70L1, can partly complement the function of RAC, which is the homologous complex from Saccharomyces cerevisiae. RAC is the J-domain partner exclusively of the 70-homolog Ssb, which directly and independently of RAC binds to the ribosome. We here show that growth defects due to mRAC depletion in HeLa cells resemble those of yeast strains lacking RAC. Functional conservation, however, did not extend to the 70-homolog partner of mRAC. None of the major human 70-homologs was able to complement the growth defects of yeast strains lacking Ssb or was bound to ribosomes in an Ssb-like manner. Instead, our data suggest that mRAC was a specific partner of human Hsp70 but not of its close homolog Hsc70. On a mechanistic level, ATP binding, but not ATP hydrolysis, by Hsp70L1 affected mRAC's function as a J-domain partner of Hsp70. The combined data indicate that, while functionally conserved, yeast and mammalian cells have evolved distinct solutions to ensure that Hsp70-type chaperones can efficiently assist the biogenesis of newly synthesized polypeptide chains.
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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.