Evidence map›Paper›PMID 38446628›Full record

ArticleThe Plant cell2024

Rapid depletion of target proteins in plants by an inducible protein degradation system.

Linzhou Huang, Marcela Rojas-Pierce

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.7field-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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. A Tradeoff Between the Escape fromPlants (Basel, Switzerland) · 2025
    Article
  7. Article
  8. An N-terminal domain specifies developmental control by the SMAX1-LIKE family of transcriptional regulators inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Review
  10. Article
  11. Review
  12. Focus on proteolysis.The Plant cell · 2024
    Article
  13. Article
  14. 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

2 authors at 1 institution in 1 country.

Linzhou HuangDepartment of Plant and Microbial Biology, North Carolina State University, Raleigh, NC 27695, USA.ORCID 0000-0002-3990-765X
Marcela Rojas-PierceDepartment of Plant and Microbial Biology, North Carolina State University, Raleigh, NC 27695, USA.ORCID 0000-0003-1051-1827
North Carolina State University · US

Funding

National Science Foundation
6 · The paper itself

Abstract

Inducible protein knockdowns are excellent tools to test the function of essential proteins in short time scales and to capture the role of proteins in dynamic events. Current approaches destroy or sequester proteins by exploiting plant biological mechanisms such as the activity of photoreceptors for optogenetics or auxin-mediated ubiquitination in auxin degrons. It follows that these are not applicable for plants as light and auxin are strong signals for plant cells. We describe here an inducible protein degradation system in plants named E3-DART for E3-targeted Degradation of Plant Proteins. The E3-DART system is based on the specific and well-characterized interaction between the Salmonella-secreted protein H1 (SspH1) and its human target protein kinase N1 (PKN1). This system harnesses the E3 catalytic activity of SspH1 and the SspH1-binding activity of the homology region 1b (HR1b) domain from PKN1. Using Nicotiana benthamiana and Arabidopsis (Arabidopsis thaliana), we show that a chimeric protein containing the leucine-rich repeat and novel E3 ligase domains of SspH1 efficiently targets protein fusions of varying sizes containing HR1b for degradation. Target protein degradation was induced by transcriptional control of the chimeric E3 ligase using a glucocorticoid transactivation system, and target protein depletion was detected as early as 3 h after induction. This system could be used to study the loss of any plant protein with high-temporal resolution and may become an important tool in plant cell biology.

Indexed as

ArabidopsisNicotianaProteolysisUbiquitin-Protein LigasesArabidopsis ProteinsBacterial ProteinsGene Expression Regulation, PlantPlant ProteinsPlants, Genetically ModifiedProtein Kinase CArabidopsis ProteinsBacterial ProteinsPlant ProteinsProtein Kinase Cprotein kinase NUbiquitin-Protein Ligases

Identifiers

PMID38446628
PMCPMC11371150
OpenAlexW4392519870

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.