Evidence map›Paper›PMID 31666677›Full record

ArticleCell research2019

Psp2, a novel regulator of autophagy that promotes autophagy-related protein translation.

Zhangyuan Yin, Xu Liu, Aileen Ariosa, Haina Huang, Meiyan Jin, Katrin Karbstein, Daniel J Klionsky

Open access · bronzeAbstract read
In one paragraph

Article in Cell research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
3.0field-weighted citation impact, top 8% 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

19 citing papers in PubMed, 1 synthesis or guideline pooled it, 31 citations in OpenAlex.

  1. Guideline
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  11. IL-6 secretion of CD4Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2022
    Article
  12. Article
  13. Review
  14. A dynamically evolving war between autophagy and pathogenic microorganisms.Journal of Zhejiang University. Science. B · 2022
    Article
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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

7 authors at 3 institutions in 1 country.

Zhangyuan YinLife Sciences Institute, and the Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, 48109, USA.
Xu LiuLife Sciences Institute, and the Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, 48109, USA.
Aileen AriosaLife Sciences Institute, and the Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, 48109, USA.
Haina HuangThe Scripps Research Institute, Department of Integrative Structural and Computational Biology, Jupiter, FL, 33458, USA.
Meiyan JinLife Sciences Institute, and the Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, 48109, USA.
Katrin KarbsteinThe Scripps Research Institute, Department of Integrative Structural and Computational Biology, Jupiter, FL, 33458, USA.
Daniel J KlionskyLife Sciences Institute, and the Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, 48109, USA. klionsky@umich.edu.ORCID http://orcid.org/0000-0002-7828-8118
University of Michigan · USScripps Research Institute · USBrigham and Women's Hospital · US

Funding

The mechanism and regulation of autophagyR35GM131919 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DANIEL J. KLIONSKY · 2019 to 2026
$6.4M
Quality Control in Ribosome Assembly - the Function of Regulatory ProteinsR01GM086451 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KARBSTEIN, KATRIN · 2009 to 2019
$4.8M
Kinase-mediated assembly of the mRNA entry channel in 40S ribosomesR01GM117093 · NIGMS · SCRIPPS FLORIDA · PI KARBSTEIN, KATRIN · 2016 to 2019
$1.7M
Howard Hughes Medical Institute (HHMI) 55108536NIGMS NIH HHS R01 GM086451NIGMS NIH HHS R01 GM117093NIGMS NIH HHS R35 GM131919U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) GM117093U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) GM131919
6 · The paper itself

Abstract

Macroautophagy/autophagy defines an evolutionarily conserved catabolic process that targets cytoplasmic components for lysosomal degradation. The process of autophagy from initiation to closure is tightly executed and controlled by the concerted action of autophagy-related (Atg) proteins. Although substantial progress has been made in characterizing transcriptional and post-translational regulation of ATG/Atg genes/proteins, little is known about the translational control of autophagy. Here we report that Psp2, an RGG motif protein, positively regulates autophagy through promoting the translation of Atg1 and Atg13, two proteins that are crucial in the initiation of autophagy. During nitrogen starvation conditions, Psp2 interacts with the 5' UTR of ATG1 and ATG13 transcripts in an RGG motif-dependent manner and with eIF4E and eIF4G2, components of the translation initiation machinery, to regulate the translation of these transcripts. Deletion of the PSP2 gene leads to a decrease in the synthesis of Atg1 and Atg13, which correlates with reduced autophagy activity and cell survival. Furthermore, deactivation of the methyltransferase Hmt1 constitutes a molecular switch that regulates Psp2 arginine methylation status as well as its mRNA binding activity in response to starvation. These results reveal a novel mechanism by which Atg proteins become upregulated to fulfill the increased demands of autophagy activity as part of translational reprogramming during stress conditions, and help explain how ATG genes bypass the general block in protein translation that occurs during starvation.

Indexed as

Adaptor Proteins, Signal TransducingAutophagyAutophagy-Related ProteinsEukaryotic Initiation Factor-4FLoss of Function MutationProtein-Arginine N-MethyltransferasesProtein BindingProtein BiosynthesisProtein KinasesRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingATG13 protein, S cerevisiaeATG1 protein, S cerevisiaeAutophagy-Related ProteinsEukaryotic Initiation Factor-4FHMT1 protein, S cerevisiaeProtein-Arginine N-MethyltransferasesProtein KinasesPSP2 protein, S cerevisiaeRepressor ProteinsSaccharomyces cerevisiae ProteinsTIF4632 protein, S cerevisiae

Identifiers

PMID31666677
PMCPMC6951345
OpenAlexW2982547531

What OpenQuestion holds

Textmetadata
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.