Evidence map›Paper›PMID 35166439›Full record

ArticleEMBO reports2022

Deubiquitinating enzymes UBP12 and UBP13 stabilize the brassinosteroid receptor BRI1.

Yongming Luo, Junpei Takagi, Lucas Alves Neubus Claus, Chao Zhang, Shigetaka Yasuda, Yoko Hasegawa, Junji Yamaguchi, Libo Shan, Eugenia Russinova, Takeo Sato

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Ubiquitin-specific protease UBP14 stabilizes HY5 by deubiquitination to promote photomorphogenesis inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Arabidopsis proteinProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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

10 authors at 4 institutions in 3 countries.

Yongming LuoGraduate School of Life Science, Hokkaido University, Sapporo, Japan.ORCID 0000-0002-0474-060X
Junpei TakagiFaculty of Science, Hokkaido University, Sapporo, Japan.ORCID 0000-0002-2409-1205
Lucas Alves Neubus ClausDepartment of Plant Biotechnology and Bioinformatics, Ghent University, Ghent, Belgium.
Chao ZhangDepartment of Plant Pathology & Microbiology, Texas A&M University, College Station, TX, USA.
Shigetaka YasudaFaculty of Science, Hokkaido University, Sapporo, Japan.ORCID 0000-0002-4602-6404
Yoko HasegawaGraduate School of Life Science, Hokkaido University, Sapporo, Japan.ORCID 0000-0002-2541-9364
Junji YamaguchiFaculty of Science, Hokkaido University, Sapporo, Japan.ORCID 0000-0002-8023-8507
Libo ShanDepartment of Biochemistry & Biophysics, Texas A&M University, College Station, TX, USA.
Eugenia RussinovaDepartment of Plant Biotechnology and Bioinformatics, Ghent University, Ghent, Belgium.ORCID 0000-0002-0569-1977
Takeo SatoFaculty of Science, Hokkaido University, Sapporo, Japan.ORCID 0000-0001-6707-0706
Hokkaido University of Science · JPGhent University · BEHokkaido University · JPTexas A&M University · US

Funding

Phosphorylation and ubiquitination of immune sensory complexes in innate immune signalingR01GM097247 · NIGMS · TEXAS A&M UNIVERSITY · PI SHAN, LIBO · 2011 to 2021
$2.4M
Immune signal perception and integration by cell surface receptors and peptide ligandsR35GM144275 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Libo Shan · 2022 to 2026
$2.2M
NIGMS NIH HHS R01 GM097247NIGMS NIH HHS R35 GM144275
6 · The paper itself

Abstract

Protein ubiquitination is a dynamic and reversible post-translational modification that controls diverse cellular processes in eukaryotes. Ubiquitin-dependent internalization, recycling, and degradation are important mechanisms that regulate the activity and the abundance of plasma membrane (PM)-localized proteins. In plants, although several ubiquitin ligases are implicated in these processes, no deubiquitinating enzymes (DUBs), have been identified that directly remove ubiquitin from membrane proteins and limit their vacuolar degradation. Here, we discover two DUB proteins, UBP12 and UBP13, that directly target the PM-localized brassinosteroid (BR) receptor BR INSENSITIVE1 (BRI1) in Arabidopsis. BRI1 protein abundance is decreased in the ubp12i/ubp13 double mutant that displayed severe growth defects and reduced sensitivity to BRs. UBP13 directly interacts with and effectively removes K63-linked polyubiquitin chains from BRI1, thereby negatively modulating its vacuolar targeting and degradation. Our study reveals that UBP12 and UBP13 play crucial roles in governing BRI1 abundance and BR signaling activity to regulate plant growth.

Indexed as

ArabidopsisArabidopsis ProteinsEndopeptidasesBrassinosteroidsDeubiquitinating EnzymesArabidopsis ProteinsBrassinosteroidsDeubiquitinating EnzymesEndopeptidasesUBP12 protein, ArabidopsisUBP13 protein, Arabidopsisendocytosismembrane proteinphytohormonereceptorubiquitination

Identifiers

PMID35166439
PMCPMC8982535
OpenAlexW4213278354

What Socratic 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 Socratic graph.