Evidence map›Paper›PMID 29540532›Full record

ArticleMolecular biology of the cell2018

Mapping the mammalian ribosome quality control complex interactome using proximity labeling approaches.

Nathan Zuzow, Arit Ghosh, Marilyn Leonard, Jeffrey Liao, Bing Yang, Eric J Bennett

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.8field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 23 citations in OpenAlex.

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  8. Protein interaction landscapes revealed by advanced in vivo cross-linking-mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Proximity-dependent labeling methods for proteomic profiling in living cells: An update.Wiley interdisciplinary reviews. Developmental biology · 2021
    Review
  10. Article
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  12. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Nathan ZuzowSection of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093.
Arit GhoshSection of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093.
Marilyn LeonardSection of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093.
Jeffrey LiaoSection of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093.
Bing YangSection of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093.
Eric J BennettSection of Cell and Developmental Biology, Division of Biological Sciences, University of California, San Diego, La Jolla, CA 92093.
University of California San Diego · US

Funding

GENETIC MECHANISMS AND REGULATIONT32GM007240 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HAMPTON, RANDOLPH Y. · 1985 to 2019
$23.8M
Manipulating Protein Homeostasis through Specialized Quality Control RibosomesDP2GM119132 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BENNETT, ERIC J · 2015 to 2015
$2.3M
NIGMS NIH HHS DP2 GM119132NIGMS NIH HHS T32 GM007240
6 · The paper itself

Abstract

Previous genetic and biochemical studies from Saccharomyces cerevisiae have identified a critical ribosome-associated quality control complex (RQC) that facilitates resolution of stalled ribosomal complexes. While components of the mammalian RQC have been examined in vitro, a systematic characterization of RQC protein interactions in mammalian cells has yet to be described. Here we utilize both proximity-labeling proteomic approaches, BioID and APEX, and traditional affinity-based strategies to both identify interacting proteins of mammalian RQC members and putative substrates for the RQC resident E3 ligase, Ltn1. Surprisingly, validation studies revealed that a subset of substrates are ubiquitylated by Ltn1 in a regulatory manner that does not result in subsequent substrate degradation. We demonstrate that Ltn1 catalyzes the regulatory ubiquitylation of ribosomal protein S6 kinase 1 and 2 (RPS6KA1, RPS6KA3). Further, loss of Ltn1 function results in hyperactivation of RSK1/2 signaling without impacting RSK1/2 protein turnover. These results suggest that Ltn1-mediated RSK1/2 ubiquitylation is inhibitory and establishes a new role for Ltn1 in regulating mitogen-activated kinase signaling via regulatory RSK1/2 ubiquitylation. Taken together, our results suggest that mammalian RQC interactions are difficult to observe and may be more transient than the homologous complex in S. cerevisiae and that Ltn1 has RQC-independent functions.

Indexed as

Protein Interaction MappingStaining and LabelingAnimalsCell LineHumansMammalsMitogensPhosphorylationProtein BindingProteomicsRibosomesSignal TransductionUbiquitinationMitogens

Identifiers

PMID29540532
PMCPMC5935074
OpenAlexW2792821259

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.