Protein Phosphatase 5 Promotes SUMM2-Mediated Immunity by Facilitating Its Protein Accumulation

Protein Phosphatase 5 (PP5) is an evolutionarily conserved serine/threonine phosphatase with a unique tetratricopeptide domain. It has been implicated in a wide range of cellular processes in mammals, but its function in plants is unknown. Here, we uncovered that Arabidopsis PP5 is required for immunity mediated by the nucleotide-binding leucine-rich repeat immune receptor protein SUMM2. Loss-of-function mutations in PP5 suppress the autoimmune phenotypes caused by the activation of SUMM2 due to the disruption of the MEKK1-MKK1/MKK2-MPK4 kinase cascade. Further biochemical analysis revealed that SUMM2 interacts with Heat Shock Protein 90 (HSP90) and PP5, and SUMM2 level is reduced in pp5 knockout mutant plants, suggesting that PP5 promotes the accumulation of SUMM2, likely through its association with the HSP90 chaperone complex.

Authors

Institutions

Publication Details

Journal
Plants
Published
2026-06-17
DOI
https://doi.org/10.3390/plants15121875
Primary Topic
Protein Tyrosine Phosphatases
Type
article
Field-Weighted Citation Impact
0.00

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Protein Phosphatase 5 Promotes SUMM2-Mediated Immunity by Facilitating Its Protein Accumulation

Xingchuan Huang, Y ZHANG, Yanan Liu
Plants
Protein Tyrosine Phosphatases
article

Protein Phosphatase 5 Promotes SUMM2-Mediated Immunity by Facilitating Its Protein Accumulation

Xingchuan Huang, Y ZHANG, Yanan Liu
article en

Abstract

Protein Phosphatase 5 (PP5) is an evolutionarily conserved serine/threonine phosphatase with a unique tetratricopeptide domain. It has been implicated in a wide range of cellular processes in mammals, but its function in plants is unknown. Here, we uncovered that Arabidopsis PP5 is required for immunity mediated by the nucleotide-binding leucine-rich repeat immune receptor protein SUMM2. Loss-of-function mutations in PP5 suppress the autoimmune phenotypes caused by the activation of SUMM2 due to the disruption of the MEKK1-MKK1/MKK2-MPK4 kinase cascade. Further biochemical analysis revealed that SUMM2 interacts with Heat Shock Protein 90 (HSP90) and PP5, and SUMM2 level is reduced in pp5 knockout mutant plants, suggesting that PP5 promotes the accumulation of SUMM2, likely through its association with the HSP90 chaperone complex.

PlantsVol. 15(12)
University of British Columbia (CA), Sichuan University (CN), Neijiang Normal University (CN)
Canada Foundation for Innovation, China Postdoctoral Science Foundation, Neijiang Normal University, Natural Sciences and Engineering Research Council of Canada
Openalex Percentile: Top 12%
Protein Tyrosine Phosphatases
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.