ArticleThe Journal of cell biology2015
Analysis of the interplay of protein biogenesis factors at the ribosome exit site reveals new role for NAC.
Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 41 citations in OpenAlex.
- Article
- A molecular switch in NAC prevents mitochondrial protein mistargeting by SRP.Nature communications · 2026Article
- NatA engages in multi-factor complexes at the ribosomal polypeptide tunnel exit.Nature communications · 2026Article
- NAC couples protein synthesis with nascent polypeptide myristoylation on the ribosome.The EMBO journal · 2025Article
- Multi-protein assemblies orchestrate co-translational enzymatic processing on the human ribosome.Nature communications · 2024Article
- Cytoplasmic ribosomes on mitochondria alter the local membrane environment for protein import.bioRxiv : the preprint server for biology · 2024Article
- NAC and Zuotin/Hsp70 chaperone systems coexist at the ribosome tunnel exit in vivo.Nucleic acids research · 2024Article
- Methionine aminopeptidase 2 and its autoproteolysis product have different binding sites on the ribosome.Nature communications · 2024Article
- The dynamic architecture of Map1- and NatB-ribosome complexes coordinates the sequential modifications of nascent polypeptide chains.PLoS biology · 2023Article
- The Endoplasmic Reticulum and the Fidelity of Nascent Protein Localization.Cold Spring Harbor perspectives in biology · 2023Review
- Article
- Targeting of Proteins for Translocation at the Endoplasmic Reticulum.International journal of molecular sciences · 2022Review
- Mechanism of signal sequence handover from NAC to SRP on ribosomes during ER-protein targeting.Science (New York, N.Y.) · 2022Article
- Ribosome-bound Get4/5 facilitates the capture of tail-anchored proteins by Sgt2 in yeast.Nature communications · 2021Article
- Ribosome pausing, a dangerous necessity for co-translational events.Nucleic acids research · 2020Review
- Chaperone Interactions at the Ribosome.Cold Spring Harbor perspectives in biology · 2019Review
- Dephosphorylation of the transcriptional cofactor NACA by the PP1A phosphatase enhances cJUN transcriptional activity and osteoblast differentiation.The Journal of biological chemistry · 2019Article
- Role for ribosome-associated complex and stress-seventy subfamily B (RAC-Ssb) in integral membrane protein translation.The Journal of biological chemistry · 2017Article
- Protein folding and tRNA biology.Biophysical reviews · 2017Review
- Structural basis of HypK regulating N-terminal acetylation by the NatA complex.Nature communications · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The ribosome exit site is a focal point for the interaction of protein-biogenesis factors that guide the fate of nascent polypeptides. These factors include chaperones such as NAC, N-terminal-modifying enzymes like Methionine aminopeptidase (MetAP), and the signal recognition particle (SRP), which targets secretory and membrane proteins to the ER. These factors potentially compete with one another in the short time-window when the nascent chain first emerges at the exit site, suggesting a need for regulation. Here, we show that MetAP contacts the ribosome at the universal adaptor site where it is adjacent to the α subunit of NAC. SRP is also known to contact the ribosome at this site. In the absence of NAC, MetAP and SRP antagonize each other, indicating a novel role for NAC in regulating the access of MetAP and SRP to the ribosome. NAC also functions in SRP-dependent targeting and helps to protect substrates from aggregation before translocation.
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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.