Evidence map›Paper›PMID 35766863›Full record

ArticleThe Plant cell2022

Defects in autophagy lead to selective in vivo changes in turnover of cytosolic and organelle proteins in Arabidopsis.

Lei Li, Chun Pong Lee, Xinxin Ding, Yu Qin, Akila Wijerathna-Yapa, Martyna Broda, Marisa S Otegui, A Harvey Millar

Open access · hybridAbstract read
In one paragraph

Article in The Plant cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
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  7. Review
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  11. Article
  12. Autophagy in the Lifetime of Plants: From Seed to Seed.International journal of molecular sciences · 2022
    Review
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

8 authors at 3 institutions in 3 countries.

Lei LiFrontiers Science Center for Cell Responses, Department of Plant Biology and Ecology, College of Life Sciences, Nankai University, Tianjin 300071, China.ORCID 0000-0003-1508-5484
Chun Pong LeeARC Centre of Excellence in Plant Energy Biology, School of Molecular Science, The University of Western Australia, Crawley, WA 6009, Australia.ORCID 0000-0002-8760-5779
Xinxin DingDepartment of Botany and Center for Quantitative Cell Imaging, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.ORCID 0000-0002-3448-9444
Yu QinFrontiers Science Center for Cell Responses, Department of Plant Biology and Ecology, College of Life Sciences, Nankai University, Tianjin 300071, China.ORCID 0000-0002-2241-3442
Akila Wijerathna-YapaARC Centre of Excellence in Plant Energy Biology, School of Molecular Science, The University of Western Australia, Crawley, WA 6009, Australia.ORCID 0000-0003-1935-8590
Martyna BrodaARC Centre of Excellence in Plant Energy Biology, School of Molecular Science, The University of Western Australia, Crawley, WA 6009, Australia.ORCID 0000-0003-0591-7814
Marisa S OteguiDepartment of Botany and Center for Quantitative Cell Imaging, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.ORCID 0000-0003-4699-6950
A Harvey MillarARC Centre of Excellence in Plant Energy Biology, School of Molecular Science, The University of Western Australia, Crawley, WA 6009, Australia.ORCID 0000-0001-9679-1473
The University of Western Australia · AUUniversity of Wisconsin–Madison · USNankai University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Identification of autophagic protein cargo in plants in autophagy-related genes (ATG) mutants is complicated by changes in protein synthesis and protein degradation. To detect autophagic cargo, we measured protein degradation rate in shoots and roots of Arabidopsis (Arabidopsis thaliana) atg5 and atg11 mutants. These data show that less than a quarter of proteins changing in abundance are probable cargo and revealed roles of ATG11 and ATG5 in degradation of specific glycolytic enzymes and of other cytosol, chloroplast, and ER-resident proteins, and a specialized role for ATG11 in degradation of proteins from mitochondria and chloroplasts. Protein localization in transformed protoplasts and degradation assays in the presence of inhibitors confirm a role for autophagy in degrading glycolytic enzymes. Autophagy induction by phosphate (Pi) limitation changed metabolic profiles and the protein synthesis and degradation rates of atg5 and atg11 plants. A general decrease in the abundance of amino acids and increase in secondary metabolites in autophagy mutants was consistent with altered catabolism and changes in energy conversion caused by reduced degradation rate of specific proteins. Combining measures of changes in protein abundance and degradation rates, we also identify ATG11 and ATG5-associated protein cargo of low Pi-induced autophagy in chloroplasts and ER-resident proteins involved in secondary metabolism.

Indexed as

ArabidopsisArabidopsis ProteinsAmino AcidsAutophagyAutophagy-Related Protein 5ChloroplastsCytosolPhosphatesAmino AcidsArabidopsis ProteinsAutophagy-Related Protein 5Phosphates

Identifiers

PMID35766863
PMCPMC9516138
OpenAlexW4283723985

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.