Evidence map›Paper›PMID 41880509›Full record

ArticleScience advances2026

Comparative proteomic profiling of receptor kinase signaling reveals key trafficking components enforcing plant stomatal development.

Pengfei Bai, Minh Huy Vu, Chiaki Komatsu, Ophelia Papoulas, Kazuo Ebine, Akira Nozawa, Tatsuya Sawasaki, Takashi Ueda, Edward M Marcotte, Keiko U Torii

Abstract read
In one paragraph

Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. ERECTA-family receptor kinases: versatile regulators of plant developmental signaling.The Plant journal : for cell and molecular biology · 2026
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Pengfei BaiHoward Hughes Medical Institute, The University of Texas, Austin, TX 78712, USA.ORCID 0000-0002-2281-2881
Minh Huy VuHoward Hughes Medical Institute, The University of Texas, Austin, TX 78712, USA.ORCID 0000-0002-1963-2759
Chiaki KomatsuHoward Hughes Medical Institute, The University of Texas, Austin, TX 78712, USA.ORCID 0009-0002-6316-6078
Ophelia PapoulasDepartment of Molecular Biosciences, The University of Texas, Austin, TX 78712, USA.ORCID 0000-0002-6370-0616
Kazuo EbineDivision of Cellular Dynamics, National Institute for Basic Biology, Okazaki, Aichi 444-0867, Japan.ORCID 0000-0003-3020-7208
Akira NozawaProteoScience Center, Ehime University, Matsuyama, Ehime 790-8577, Japan.ORCID 0000-0003-4886-0213
Tatsuya SawasakiProteoScience Center, Ehime University, Matsuyama, Ehime 790-8577, Japan.ORCID 0000-0002-7952-0556
Takashi UedaDivision of Cellular Dynamics, National Institute for Basic Biology, Okazaki, Aichi 444-0867, Japan.ORCID 0000-0002-5190-892X
Edward M MarcotteDepartment of Molecular Biosciences, The University of Texas, Austin, TX 78712, USA.ORCID 0000-0001-8808-180X
Keiko U ToriiHoward Hughes Medical Institute, The University of Texas, Austin, TX 78712, USA.ORCID 0000-0002-6168-427X

Funding

Proteomics and model organism humanization to decode human geneticsR35GM122480 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI EDWARD M MARCOTTE · 2017 to 2026
$5.4M
NIGMS NIH HHS R35 GM122480
6 · The paper itself

Abstract

Receptor kinases are pivotal for growth, development, and environmental response of plants. Yet, their regulatory mechanisms and spatial dynamics remain underexplored. The ERECTA-family receptor kinases coordinate diverse developmental processes, including stomatal development. To understand the proteomic landscape of the ERECTA-mediated signaling pathways, we report comparative analyses of the ERECTA interactome and proximitome by epitope-tagged affinity-purification (ET-AP) and TurboID-based proximity labeling (TbID-PL) mass spectrometry, respectively. While ET-AP recovered receptor complex components (e.g., TOO MANY MOUTHS), TbID-PL effectively captured transient associations with the components of endosomal trafficking, i.e., clathrin-mediated endocytosis machinery. We further identify that specific subfamily members of phosphatidylinositol-binding clathrin assembly proteins (PICALMs) interact with and synergistically regulate ERECTA internalization. Mutations in

Indexed as

ArabidopsisArabidopsis ProteinsPlant StomataProtein Serine-Threonine KinasesProteomeProteomicsReceptors, Cell SurfaceSignal TransductionEndocytosisMutationPhosphotransferasesProtein TransportArabidopsis ProteinsAt3g51550 protein, ArabidopsisPhosphotransferasesProtein Serine-Threonine KinasesProteomeReceptors, Cell Surface

Identifiers

PMID41880509
PMCPMC13015889

What OpenQuestion holds

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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.