Evidence map›Paper›PMID 34718777›Full record

ArticleThe Plant cell2022

FYVE2, a phosphatidylinositol 3-phosphate effector, interacts with the COPII machinery to control autophagosome formation in Arabidopsis.

Jeong Hun Kim, Han Nim Lee, Xiao Huang, Hyera Jung, Marisa S Otegui, Faqiang Li, Taijoon Chung

Open access · bronzeAbstract 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 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.1field-weighted citation impact, top 5% 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, 39 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Biomolecular condensation of ERC1 recruits ATG8 and NBR1 to drive autophagosome formation for plant heat tolerance.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Autophagy in plants.Autophagy reports · 2024
    Review
  10. Interactome ofInternational journal of molecular sciences · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 3 countries.

Jeong Hun KimDepartment of Biological Sciences, Pusan National University, Busan 46241, Republic of Korea.ORCID 0000-0001-5049-5417
Han Nim LeeDepartment of Biological Sciences, Pusan National University, Busan 46241, Republic of Korea.ORCID 0000-0002-0429-6297
Xiao HuangCollege of Life Sciences, South China Agricultural University, Guangzhou 510642, P. R. China.ORCID 0000-0002-3724-7440
Hyera JungDepartment of Biological Sciences, Pusan National University, Busan 46241, Republic of Korea.ORCID 0000-0001-8039-4115
Marisa S OteguiDepartment of Botany and Center for Quantitative Cell Imaging, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.ORCID 0000-0003-4699-6950
Faqiang LiCollege of Life Sciences, South China Agricultural University, Guangzhou 510642, P. R. China.ORCID 0000-0003-4117-2450
Taijoon ChungDepartment of Biological Sciences, Pusan National University, Busan 46241, Republic of Korea.ORCID 0000-0002-5318-9105
Pusan National University · KRSouth China Agricultural University · CNUniversity of Wisconsin–Madison · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is an intracellular trafficking mechanism by which cytosolic macromolecules and organelles are sequestered into autophagosomes for degradation inside the vacuole. In various eukaryotes including yeast, metazoans, and plants, the precursor of the autophagosome, termed the phagophore, nucleates in the vicinity of the endoplasmic reticulum (ER) with the participation of phosphatidylinositol 3-phosphate (PI3P) and the coat protein complex II (COPII). Here we show that Arabidopsis thaliana FYVE2, a plant-specific PI3P-binding protein, provides a functional link between the COPII machinery and autophagy. FYVE2 interacts with the small GTPase Secretion-associated Ras-related GTPase 1 (SAR1), which is essential for the budding of COPII vesicles. FYVE2 also interacts with ATG18A, another PI3P effector on the phagophore membrane. Fluorescently tagged FYVE2 localized to autophagic membranes near the ER and was delivered to vacuoles. SAR1 fusion proteins were also targeted to the vacuole via FYVE2-dependent autophagy. Either mutations in FYVE2 or the expression of dominant-negative mutant SAR1B proteins resulted in reduced autophagic flux and the accumulation of autophagic organelles. We propose that FYVE2 regulates autophagosome biogenesis through its interaction with ATG18A and the COPII machinery, acting downstream of ATG2.

Indexed as

ArabidopsisAutophagosomesVesicular Transport ProteinsArabidopsis ProteinsAutophagy-Related ProteinsArabidopsis ProteinsAt3g43230 protein, ArabidopsisAutophagy-Related ProteinsVesicular Transport Proteins

Identifiers

PMID34718777
PMCPMC8846182
OpenAlexW3211290334

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.