Evidence map›Paper›PMID 41951888›Full record

ArticleNature plants2026

De-repression of protein phosphatase 5 by the chaperone organizer HOP1 activates plant NLR immunity.

Yan Yan, Zhixue Zhao, In-Cheol Yeo, Jun Liu, Luciano de Souza Vespoli, Guangchao Liu, Suji Ye, Jayakrishnan Nandakumar, Libo Shan, Ping He

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature plants, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
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.

Yan YanDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.ORCID http://orcid.org/0000-0003-2333-9456
Zhixue ZhaoDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX, USA.
In-Cheol YeoDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.
Jun LiuDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX, USA.
Luciano de Souza VespoliDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX, USA.
Guangchao LiuDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.
Suji YeDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.
Jayakrishnan NandakumarDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.
Libo ShanDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.ORCID http://orcid.org/0000-0002-4798-9907
Ping HeDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI, USA. pinghemi@umich.edu.ORCID http://orcid.org/0000-0002-5926-8349

Funding

Molecular mechanisms of intersecting human telomeric functionsR35GM148276 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Jayakrishnan Nandakumar · 2023 to 2026
$1.6M
Foundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.) R35GM144275Foundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.) R35GM148276Foundation for the National Institutes of Health (Foundation for the National Institutes of Health, Inc.) R35GM149197NIGMS NIH HHS R35 GM148276
6 · The paper itself

Abstract

Protein phosphatase 5 (PP5) is a conserved serine/threonine phosphatase regulating growth, stress responses, programmed cell death and immunity across eukaryotes. However, the mechanisms underlying its activation remain poorly understood. Here we demonstrate that the disruption of the plant MEKK1-MKK1/2-MPK4 cascade activates LET7, a plant homologue of PP5, triggering nucleotide-binding leucine-rich repeat (NLR) SUMM2-mediated autoimmunity in Arabidopsis. The binding of LET7 to the co-chaperone protein HOP1 disrupts the autoinhibitory interaction between the tetratricopeptide repeat and phosphatase domains of LET7 in releasing its phosphatase activity. Activated LET7 subsequently dephosphorylates CRCK3, a crucial kinase regulating SUMM2 autoimmunity. Furthermore, HOP1 and LET7 stabilize SUMM2 via their tetratricopeptide repeat domains, highlighting the dual role of the HOP1-LET7 module in dephosphorylating CRCK3 and stabilizing SUMM2 in NLR-mediated immunity. Our studies reveal a conserved mechanism of PP5 activation across plants and animals and elucidate a unique dephosphorylation cascade governing NLR activation.

Indexed as

ArabidopsisArabidopsis ProteinsMolecular ChaperonesNLR ProteinsPhosphoprotein PhosphatasesPlant ImmunityCarrier ProteinsNuclear ProteinsArabidopsis ProteinsCarrier ProteinsMolecular ChaperonesNLR ProteinsNuclear ProteinsPhosphoprotein Phosphatasesprotein phosphatase 5SUMM2 protein, Arabidopsis

Identifiers

PMID41951888
PMCPMC13106031

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.