ORCID Profile
0000-0002-3512-0200
Current Organisations
Wageningen University
,
Northwest A and F University
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Publisher: Elsevier BV
Date: 08-2018
DOI: 10.1016/J.MOLP.2018.05.009
Abstract: Phytophthora pathogens secrete a large arsenal of effectors that manipulate host processes to create an environment conducive to pathogen colonization. However, the underlying mechanisms by which Phytophthora effectors manipulate host plant cells still remain largely unclear. In this study, we report that PcAvr3a12, a Phytophthora capsici RXLR effector and a member of the Avr3a effector family, suppresses plant immunity by targeting and inhibiting host plant peptidyl-prolyl cis-trans isomerase (PPIase). Overexpression of PcAvr3a12 in Arabidopsis thaliana enhanced plant susceptibility to P. capsici. FKBP15-2, an endoplasmic reticulum (ER)-localized protein, was identified as a host target of PcAvr3a12 during early P. capsici infection. Analyses of A. thaliana T-DNA insertion mutant (fkbp15-2), RNAi, and overexpression lines consistently showed that FKBP15-2 positively regulates plant immunity in response to Phytophthora infection. FKBP15-2 possesses PPIase activity essential for its contribution to immunity but is directly suppressed by PcAvr3a12. Interestingly, we found that FKBP15-2 is involved in ER stress sensing and is required for ER stress-mediated plant immunity. Taken together, these results suggest that P. capsici deploys an RXLR effector, PcAvr3a12, to facilitate infection by targeting and suppressing a novel ER-localized PPIase, FKBP15-2, which is required for ER stress-mediated plant immunity.
Publisher: Wiley
Date: 12-09-2020
DOI: 10.1111/NPH.16861
Abstract: Pathogens secret a plethora of effectors into the host cell to modulate plant immunity. Analysing the role of effectors in altering the function of their host target proteins will reveal critical components of the plant immune system. Here we show that Phytophthora infestans RXLR effector PITG20303, a virulent variant of AVRblb2 (PITG20300) that escapes recognition by the resistance protein Rpi‐blb2, suppresses PAMP‐triggered immunity (PTI) and promotes pathogen colonization by targeting and stabilizing a potato MAPK cascade protein, StMKK1. Both PITG20300 and PITG20303 target StMKK1, as confirmed by multiple in vivo and in vitro assays, and StMKK1 was shown to be a negative regulator of plant immunity, as determined by overexpression and gene silencing. StMKK1 is a negative regulator of plant PTI, and the kinase activities of StMKK1 are required for its suppression of PTI and effector interaction. PITG20303 depends partially on MKK1, PITG20300 does not depend on MKK1 for suppression of PTI‐induced reactive oxygen species burst, while the full virulence activities of nuclear targeted PITG20303 and PITG20300 are dependent on MKK1. Our results show that PITG20303 and PITG20300 target and stabilize the plant MAPK cascade signalling protein StMKK1 to negatively regulate plant PTI response.
Publisher: Wiley
Date: 07-02-2023
DOI: 10.1111/NPH.18749
Abstract: Ubiquitin‐like domain‐containing proteins (UDPs) are involved in the ubiquitin‐proteasome system because of their ability to interact with the 26S proteasome. Here, we identified potato StUDP as a target of the Phytophthora infestans RXLR effector Pi06432 (PITG_06432), which supresses the salicylic acid (SA)‐related immune pathway. By overexpressing and silencing of StUDP in potato, we show that StUDP negatively regulates plant immunity against P. infestans . StUDP interacts with, and destabilizes, the 26S proteasome subunit that is referred to as REGULATORY PARTICLE TRIPLE‐A ATP‐ASE (RPT) subunit StRPT3b. This destabilization represses the proteasome activity. Proteomic analysis and Western blotting show that StUDP decreases the stability of the master transcription factor SYSTEMIC ACQUIRED RESISTANCE DEFICIENT 1 (SARD1) in SA biosynthesis. StUDP negatively regulates the SA signalling pathway by repressing the proteasome activity and destabilizing StSARD1, leading to a decreased expression of the SARD1‐targeted gene ISOCHORISMATE SYNTHASE 1 and thereby a decrease in SA content. Pi06432 stabilizes StUDP, and it depends on StUDP to destabilize StRPT3b and thereby supress the proteasome activity. Our study reveals that the P. infestans effector Pi06432 targets StUDP to h er the homeostasis of the proteasome by the degradation of the proteasome subunit StRPT3b and thereby suppresses SA‐related immunity.
Publisher: Wiley
Date: 04-01-2023
DOI: 10.1111/PBI.13979
Abstract: Phytophthora infestans causes severe losses in potato production. The MAPK kinase StMKK1 was previously found to negatively regulate potato immunity to P. infestans . Our results showed that StMKK1 interacts with a protein tyrosine phosphatase, referred to as StPTP1a, and StMKK1 directly phosphorylates StPTP1a at residues Ser‐99, Tyr‐223 and Thr‐290. StPTP1a is a functional phosphatase and the phosphorylation of StPTP1a at these three residues enhances its stability and catalytic activity. StPTP1a negatively regulates potato immunity and represses SA‐related gene expression. Furthermore, StPTP1a interacts with, and dephosphorylates, the StMKK1 downstream signalling targets StMPK4 and −7 at their Tyr‐203 residue resulting in the repression of salicylic acid (SA)‐related immunity. Silencing of NbPTP1a + NbMPK4 or NbPTP1a + NbMPK7 abolished the plant immunity to P. infestans caused by NbPTP1a silencing, indicating that PTP1a functions upstream of NbMPK4 and NbMPK7. StMKK1 requires StPTP1a to negatively regulate SA‐related immunity and StPTP1a is phosphorylated and stabilized during immune activation to promote the de‐phosphorylation of StMPK4 and −7. Our results reveal that potato StMKK1 activates and stabilizes the tyrosine phosphatase StPTP1a that in its turn de‐phosphorylates StMPK4 and −7, thereby repressing plant SA‐related immunity.
Publisher: Wiley
Date: 25-03-2021
DOI: 10.1111/MPP.13050
No related grants have been discovered for Yu Du.