Evidence map›Paper›PMID 37823521›Full record

ArticleThe Plant cell2023

HOOKLESS1 acetylates AUTOPHAGY-RELATED PROTEIN18a to promote autophagy during nutrient starvation in Arabidopsis.

Li Huang, Xing Wen, Lian Jin, Huihui Han, Hongwei Guo

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
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  6. Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  11. Review
  12. Article
  13. Review
  14. Review
  15. Autophagy in plants.Autophagy reports · 2024
    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

5 authors at 1 institution in 1 country.

Li HuangNew Cornerstone Science Laboratory, Institute of Plant and Food Science, Department of Biology, School of Life Sciences, Southern University of Science and Technology (SUSTech), Shenzhen, Guangdong 518055, China.ORCID 0009-0002-1653-0527
Xing WenNew Cornerstone Science Laboratory, Institute of Plant and Food Science, Department of Biology, School of Life Sciences, Southern University of Science and Technology (SUSTech), Shenzhen, Guangdong 518055, China.ORCID 0000-0002-9322-2272
Lian JinNew Cornerstone Science Laboratory, Institute of Plant and Food Science, Department of Biology, School of Life Sciences, Southern University of Science and Technology (SUSTech), Shenzhen, Guangdong 518055, China.ORCID 0000-0001-7067-3807
Huihui HanNew Cornerstone Science Laboratory, Institute of Plant and Food Science, Department of Biology, School of Life Sciences, Southern University of Science and Technology (SUSTech), Shenzhen, Guangdong 518055, China.ORCID 0009-0001-0269-8321
Hongwei GuoNew Cornerstone Science Laboratory, Institute of Plant and Food Science, Department of Biology, School of Life Sciences, Southern University of Science and Technology (SUSTech), Shenzhen, Guangdong 518055, China.ORCID 0000-0002-7883-9477
Southern University of Science and Technology · CN

Funding

China Postdoctoral Science Fund Project 2019M662939National Natural Science Foundation of China 32230008New Cornerstone Science Foundation NCI202235Shenzhen Science and Technology Innovation Program 20200925161843002
6 · The paper itself

Abstract

Acetylation is an important posttranslational modification (PTM) that regulates almost all core processes of autophagy in yeast and mammals. However, the role of protein acetylation in plant autophagy and the underlying regulatory mechanisms remain unclear. Here, we show the essential role of the putative acetyltransferase HOOKLESS1 (HLS1) in acetylation of the autophagy-related protein ATG18a, a key autophagy component that regulates autophagosome formation in Arabidopsis (Arabidopsis thaliana). Loss of HLS1 function suppressed starvation-induced autophagy and increased plant susceptibility to nutrient deprivation. We discovered that HLS1 physically interacts with and directly acetylates ATG18a both in vitro and in vivo. In contrast, mutating putative active sites in HLS1 inhibited ATG18a acetylation and suppressed autophagy upon nutrient deprivation. Accordingly, overexpression of ATG18a mutant variants with lower acetylation levels inhibited the binding activity of ATG18a to PtdIns(3)P and autophagosome formation under starvation conditions. Moreover, HLS1-modulated autophagy was uncoupled from its function in hook development. Taken together, these findings shed light on a key regulator of autophagy and further elucidate the importance of PTMs in modulating autophagy in plants.

Indexed as

ArabidopsisArabidopsis ProteinsAutophagyNutrientsProtein Processing, Post-TranslationalArabidopsis ProteinsAt4g37580 protein, ArabidopsisNutrients

Identifiers

PMID37823521
PMCPMC10734606
OpenAlexW4387564098

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.