Evidence map›Paper›PMID 35089338›Full record

ArticleThe Plant cell2022

The TGN/EE SNARE protein SYP61 and the ubiquitin ligase ATL31 cooperatively regulate plant responses to carbon/nitrogen conditions in Arabidopsis.

Yoko Hasegawa, Thais Huarancca Reyes, Tomohiro Uemura, Anirban Baral, Akari Fujimaki, Yongming Luo, Yoshie Morita, Yasushi Saeki, Shugo Maekawa, Shigetaka Yasuda and 8 more

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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

11 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Post-Golgi Trafficking in Plant Cells.Sub-cellular biochemistry · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Pyrenoid proteomics reveals independent evolution of the COProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Review
  11. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

18 authors at 6 institutions in 2 countries.

Yoko HasegawaFaculty of Science and Graduate School of Life Science, Hokkaido University, Kita-ku N10-W8, Sapporo 060-0810, Japan.ORCID 0000-0002-2541-9364
Thais Huarancca ReyesFaculty of Science and Graduate School of Life Science, Hokkaido University, Kita-ku N10-W8, Sapporo 060-0810, Japan.ORCID 0000-0003-2988-0980
Tomohiro UemuraGraduate School of Humanities and Sciences, Ochanomizu University, Bunkyo-ku, Tokyo 112-8610, Japan.ORCID 0000-0001-7270-7986
Anirban BaralUmeå Plant Science Centre, Forest Genetics and Plant Physiology, Swedish University of Agricultural Sciences, Umeå S-901 83, Sweden.ORCID 0000-0001-6676-284X
Akari FujimakiFaculty of Science and Graduate School of Life Science, Hokkaido University, Kita-ku N10-W8, Sapporo 060-0810, Japan.ORCID 0000-0002-9950-4289
Yongming LuoFaculty of Science and Graduate School of Life Science, Hokkaido University, Kita-ku N10-W8, Sapporo 060-0810, Japan.ORCID 0000-0002-0474-060X
Yoshie MoritaFaculty of Science and Graduate School of Life Science, Hokkaido University, Kita-ku N10-W8, Sapporo 060-0810, Japan.ORCID 0000-0003-2645-6711
Yasushi SaekiLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan.ORCID 0000-0002-9202-5453
Shugo MaekawaFaculty of Science and Graduate School of Life Science, Hokkaido University, Kita-ku N10-W8, Sapporo 060-0810, Japan.ORCID 0000-0002-6021-505X
Shigetaka YasudaFaculty of Science and Graduate School of Life Science, Hokkaido University, Kita-ku N10-W8, Sapporo 060-0810, Japan.ORCID 0000-0002-4602-6404
Koki MukutaFaculty of Science and Graduate School of Life Science, Hokkaido University, Kita-ku N10-W8, Sapporo 060-0810, Japan.ORCID 0000-0003-3746-1719
Yoichiro FukaoDepartment of Bioinformatics, Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan.ORCID 0000-0003-0760-570X
Keiji TanakaLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan.ORCID 0000-0003-3098-4760
Akihiko NakanoLive Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics, Wako, Saitama 351-0198, Japan.ORCID 0000-0003-3635-548X
Junpei TakagiFaculty of Science and Graduate School of Life Science, Hokkaido University, Kita-ku N10-W8, Sapporo 060-0810, Japan.ORCID 0000-0002-2409-1205
Rishikesh P BhaleraoUmeå Plant Science Centre, Forest Genetics and Plant Physiology, Swedish University of Agricultural Sciences, Umeå S-901 83, Sweden.ORCID 0000-0003-4384-7036
Junji YamaguchiFaculty of Science and Graduate School of Life Science, Hokkaido University, Kita-ku N10-W8, Sapporo 060-0810, Japan.ORCID 0000-0002-8023-8507
Takeo SatoFaculty of Science and Graduate School of Life Science, Hokkaido University, Kita-ku N10-W8, Sapporo 060-0810, Japan.ORCID 0000-0001-6707-0706
Hokkaido University · JPSwedish University of Agricultural Sciences · SETokyo Metropolitan Institute of Medical Science · JPOchanomizu University · JPRIKEN Center for Advanced Photonics · JPRitsumeikan University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitination is a post-translational modification involving the reversible attachment of the small protein ubiquitin to a target protein. Ubiquitination is involved in numerous cellular processes, including the membrane trafficking of cargo proteins. However, the ubiquitination of the trafficking machinery components and their involvement in environmental responses are not well understood. Here, we report that the Arabidopsis thaliana trans-Golgi network/early endosome localized SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein SYP61 interacts with the transmembrane ubiquitin ligase ATL31, a key regulator of resistance to disrupted carbon (C)/nitrogen/(N)-nutrient conditions. SYP61 is a key component of membrane trafficking in Arabidopsis. The subcellular localization of ATL31 was disrupted in knockdown mutants of SYP61, and the insensitivity of ATL31-overexpressing plants to high C/low N-stress was repressed in these mutants, suggesting that SYP61 and ATL31 cooperatively function in plant responses to nutrient stress. SYP61 is ubiquitinated in plants, and its ubiquitination level is upregulated under low C/high N-nutrient conditions. These findings provide important insights into the ubiquitin signaling and membrane trafficking machinery in plants.

Indexed as

ArabidopsisArabidopsis ProteinsCarbonNitrogenSNARE Proteinstrans-Golgi NetworkUbiquitinUbiquitin-Protein LigasesArabidopsis ProteinsCarbonNitrogenSNARE ProteinsUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID35089338
PMCPMC8972251
OpenAlexW4210284048

What OpenQuestion holds

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Registered trials

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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.