Evidence map›Paper›PMID 36854476›Full record

ReviewAnnual review of plant biology2023

Proximity Labeling in Plants.

Shou-Ling Xu, Ruben Shrestha, Sumudu S Karunadasa, Pei-Qiao Xie

Open access · hybridAbstract readReview
In one paragraph

Review in Annual review of plant biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
11.9field-weighted citation impact, top 1% 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

36 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Mapping the architecture of protein complexes inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. TurboID-Based Proximity Labeling in Plants.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  12. Article
  13. Article
  14. A plant-specific cytochromeScience advances · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

4 authors at 2 institutions in 1 country.

Shou-Ling XuDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California, USA; email: slxu@stanford.edu.
Ruben ShresthaDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California, USA; email: slxu@stanford.edu.
Sumudu S KarunadasaDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California, USA; email: slxu@stanford.edu.
Pei-Qiao XieDepartment of Plant Biology, Carnegie Institution for Science, Stanford, California, USA; email: slxu@stanford.edu.
Carnegie Institution for Science · USDepartment of Plant Biology · US

Funding

Nutrient regulation of Alternative splicing and transcription by O-GlcNAcylationR01GM135706 · NIGMS · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI XU, SHOULING · 2020 to 2024
$1.8M
Thermo Orbitrap Eclipse Tribrid with ETD and an Ultimate 3000 RSLCnano SystemS10OD030441 · OD · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI XU, SHOULING · 2022 to 2022
$600k
NIGMS NIH HHS R01 GM135706NIH HHS S10 OD030441
6 · The paper itself

Abstract

Proteins are workhorses in the cell; they form stable and more often dynamic, transient protein-protein interactions, assemblies, and networks and have an intimate interplay with DNA and RNA. These network interactions underlie fundamental biological processes and play essential roles in cellular function. The proximity-dependent biotinylation labeling approach combined with mass spectrometry (PL-MS) has recently emerged as a powerful technique to dissect the complex cellular network at the molecular level. In PL-MS, by fusing a genetically encoded proximity-labeling (PL) enzyme to a protein or a localization signal peptide, the enzyme is targeted to a protein complex of interest or to an organelle, allowing labeling of proximity proteins within a zoom radius. These biotinylated proteins can then be captured by streptavidin beads and identified and quantified by mass spectrometry. Recently engineered PL enzymes such as TurboID have a much-improved enzymatic activity, enabling spatiotemporal mapping with a dramatically increased signal-to-noise ratio. PL-MS has revolutionized the way we perform proteomics by overcoming several hurdles imposed by traditional technology, such as biochemical fractionation and affinity purification mass spectrometry. In this review, we focus on biotin ligase-based PL-MS applications that have been, or are likely to be, adopted by the plant field. We discuss the experimental designs and review the different choices for engineered biotin ligases, enrichment, and quantification strategies. Lastly, we review the validation and discuss future perspectives.

Indexed as

BiotinOrganellesPlantsProteinsStreptavidinBiotinProteinsStreptavidincell type–specific proteomeprotein–nucleotide interactionprotein–protein interactionproximity labelingquantificationsubcellular proteome

Identifiers

PMID36854476
PMCPMC10576617
OpenAlexW4322615509

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.