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  1. Article ; Online: BRASSINOSTEROID-SIGNALING KINASE1 associates with and is required for cysteine protease RESPONSE TO DEHYDRATION 19-mediated disease resistance in Arabidopsis.

    Li, Qiuyi / Shao, Jing / Luo, Mingyu / Chen, Desheng / Tang, Dingzhong / Shi, Hua

    Plant science : an international journal of experimental plant biology

    2024  Volume 342, Page(s) 112033

    Abstract: The receptor-like cytoplasmic kinase BRASSINOSTEROID-SIGNALING KINASE1 (BSK1) interacts with pattern recognition receptor (PRR) FLAGELLIN SENSING2 (FLS2) and positively regulates plant innate immunity in Arabidopsis thaliana. However, the molecular ... ...

    Abstract The receptor-like cytoplasmic kinase BRASSINOSTEROID-SIGNALING KINASE1 (BSK1) interacts with pattern recognition receptor (PRR) FLAGELLIN SENSING2 (FLS2) and positively regulates plant innate immunity in Arabidopsis thaliana. However, the molecular components involved in BSK1-mediated immune signaling remain largely unknown. To further explore the molecular mechanism underlying BSK1-mediated disease resistance, we screened two cysteine proteases, RESPONSE TO DEHYDRATION 19 (RD19) and RD19-LIKE 2 (RDL2), as BSK1-binding partners. Overexpression of RD19, but not RDL2, displayed an autoimmune phenotype, presenting programmed cell death and enhanced resistance to multiple pathogens. Interestingly, RD19-mediated immune activation depends on BSK1, as knockout of BSK1 in RD19-overexpressing plants rescued their autoimmunity and abolished the increased resistance. Furthermore, we found that BSK1 plays a positive role in maintaining RD19 protein abundance in Arabidopsis. Our results provide new insights into BSK1-mediated immune signaling and reveal a potential mechanism by which BSK1 stabilizes RD19 to promote effective immune output.
    MeSH term(s) Arabidopsis/metabolism ; Arabidopsis Proteins/genetics ; Arabidopsis Proteins/metabolism ; Brassinosteroids/metabolism ; Cysteine Proteases/genetics ; Cysteine Proteases/metabolism ; Dehydration ; Disease Resistance/genetics ; Plant Immunity/genetics ; Protein Serine-Threonine Kinases/genetics
    Chemical Substances Arabidopsis Proteins ; brassinosteroid-signaling kinase1, Arabidopsis (EC 2.7.11.1) ; Brassinosteroids ; Cysteine Proteases (EC 3.4.-) ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2024-02-12
    Publishing country Ireland
    Document type Journal Article
    ZDB-ID 742010-9
    ISSN 1873-2259 ; 0168-9452
    ISSN (online) 1873-2259
    ISSN 0168-9452
    DOI 10.1016/j.plantsci.2024.112033
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    Z 77/717: Show issues

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  2. Article ; Online: The Role of Ubiquitination in Plant Immunity: Fine-Tuning Immune Signaling and Beyond.

    Gao, Chenyang / Tang, Dingzhong / Wang, Wei

    Plant & cell physiology

    2022  Volume 63, Issue 10, Page(s) 1405–1413

    Abstract: Ubiquitination is an essential posttranslational modification and plays a crucial role in regulating plant immunity by modulating protein activity, stability, abundance and interaction. Recently, major breakthroughs have been made in understanding the ... ...

    Abstract Ubiquitination is an essential posttranslational modification and plays a crucial role in regulating plant immunity by modulating protein activity, stability, abundance and interaction. Recently, major breakthroughs have been made in understanding the mechanisms associated with the regulation of immune signaling by ubiquitination. In this mini review, we highlight the recent advances in the role of ubiquitination in fine-tuning the resistance activated by plant pattern recognition receptors (PRRs) and intracellular nucleotide-binding site and leucine-rich repeat domain receptors (NLRs). We also discuss current understanding of the positive regulation of plant immunity by ubiquitination, including the modification of immune negative regulators and of the guardee proteins monitored by NLRs.
    MeSH term(s) Plant Immunity/physiology ; Ubiquitination ; Signal Transduction ; Protein Processing, Post-Translational ; Plants
    Language English
    Publishing date 2022-07-20
    Publishing country Japan
    Document type Review ; Journal Article
    ZDB-ID 208907-5
    ISSN 1471-9053 ; 0032-0781
    ISSN (online) 1471-9053
    ISSN 0032-0781
    DOI 10.1093/pcp/pcac105
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  3. Article ; Online: NUA positively regulates plant immunity by coordination with ESD4 to deSUMOylate TPR1 in Arabidopsis

    Xie, Bao / Luo, Mingyu / Li, Qiuyi / Shao, Jing / Chen, Desheng / Somers, David E. / Tang, Dingzhong / Shi, Hua

    New Phytologist. 2024 Jan., v. 241, no. 1 p.363-377

    2024  

    Abstract: Nuclear pore complex (NPC) is composed of multiple nucleoporins (Nups). A plethora of studies have highlighted the significance of NPC in plant immunity. However, the specific roles of individual Nups are poorly understood. NUCLEAR PORE ANCHOR (NUA) is a ...

    Abstract Nuclear pore complex (NPC) is composed of multiple nucleoporins (Nups). A plethora of studies have highlighted the significance of NPC in plant immunity. However, the specific roles of individual Nups are poorly understood. NUCLEAR PORE ANCHOR (NUA) is a component of NPC. Loss of NUA leads to an increase in SUMO conjugates and pleiotropic developmental defects in Arabidopsis thaliana. Herein, we revealed that NUA is required for plant defense against multiple pathogens. NUCLEAR PORE ANCHOR associates with the transcriptional corepressor TOPLESS‐RELATED1 (TPR1) and contributes to TPR1 deSUMOylation. Significantly, NUA‐interacting protein EARLY IN SHORT DAYS 4 (ESD4), a SUMO protease, specifically deSUMOylates TPR1. It has been previously established that the SUMO E3 ligase SAP AND MIZ1 DOMAIN‐CONTAINING LIGASE 1 (SIZ1)‐mediated SUMOylation of TPR1 represses the immune‐related function of TPR1. Consistent with this notion, the hyper‐SUMOylated TPR1 in nua‐3 leads to upregulated expression of TPR1 target genes and compromised TPR1‐mediated disease resistance. Taken together, our work uncovers a mechanism by which NUA positively regulates plant defense responses by coordination with ESD4 to deSUMOylate TPR1. Our findings, together with previous studies, reveal a regulatory module in which SIZ1 and NUA/ESD4 control the homeostasis of TPR1 SUMOylation to maintain proper immune output.
    Keywords Arabidopsis thaliana ; disease resistance ; homeostasis ; immunity ; nuclear pore ; nucleoporins ; proteinases ; sumoylation ; transcription (genetics) ; ubiquitin-protein ligase
    Language English
    Dates of publication 2024-01
    Size p. 363-377.
    Publishing place John Wiley & Sons, Ltd
    Document type Article ; Online
    Note JOURNAL ARTICLE
    ZDB-ID 208885-x
    ISSN 1469-8137 ; 0028-646X
    ISSN (online) 1469-8137
    ISSN 0028-646X
    DOI 10.1111/nph.19287
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  4. Article ; Online: The RECEPTOR-LIKE PROTEIN53 immune complex associates with LLG1 to positively regulate plant immunity.

    Chen, Renjie / Sun, Pengwei / Zhong, Guitao / Wang, Wei / Tang, Dingzhong

    Journal of integrative plant biology

    2022  Volume 64, Issue 9, Page(s) 1833–1846

    Abstract: Pattern recognition receptors (PRRs) sense ligands in pattern-triggered immunity (PTI). Plant PRRs include numerous receptor-like proteins (RLPs), but many RLPs remain functionally uncharacterized. Here, we examine an Arabidopsis thaliana RLP, RLP53, ... ...

    Abstract Pattern recognition receptors (PRRs) sense ligands in pattern-triggered immunity (PTI). Plant PRRs include numerous receptor-like proteins (RLPs), but many RLPs remain functionally uncharacterized. Here, we examine an Arabidopsis thaliana RLP, RLP53, which positively regulates immune signaling. Our forward genetic screen for suppressors of enhanced disease resistance1 (edr1) identified a point mutation in RLP53 that fully suppresses disease resistance and mildew-induced cell death in edr1 mutants. The rlp53 mutants showed enhanced susceptibility to virulent pathogens, including fungi, oomycetes, and bacteria, indicating that RLP53 is important for plant immunity. The ectodomain of RLP53 contains leucine-rich repeat (LRR) motifs. RLP53 constitutively associates with the LRR receptor-like kinase SUPPRESSOR OF BRASSINOSTEROID INSENSITIVE1-ASSOCIATED KINASE (BAK1)-INTERACTING RECEPTOR KINASE1 (SOBIR1) and interacts with the co-receptor BAK1 in a pathogen-induced manner. The double mutation sobir1-12 bak1-5 suppresses edr1-mediated disease resistance, suggesting that EDR1 negatively regulates PTI modulated by the RLP53-SOBIR1-BAK1 complex. Moreover, the glycosylphosphatidylinositol (GPI)-anchored protein LORELEI-LIKE GPI-ANCHORED PROTEIN1 (LLG1) interacts with RLP53 and mediates RLP53 accumulation in the plasma membrane. We thus uncovered the role of a novel RLP and its associated immune complex in plant defense responses and revealed a potential new mechanism underlying regulation of RLP immune function by a GPI-anchored protein.
    MeSH term(s) Antigen-Antibody Complex/genetics ; Antigen-Antibody Complex/metabolism ; Arabidopsis/metabolism ; Arabidopsis Proteins/genetics ; Arabidopsis Proteins/metabolism ; Cell Membrane/metabolism ; Disease Resistance/genetics ; GPI-Linked Proteins ; Gene Expression Regulation, Plant ; Glycosylphosphatidylinositols/metabolism ; Plant Diseases/microbiology ; Plant Immunity/genetics ; Plants/metabolism ; Protein Kinases/genetics ; Protein Kinases/metabolism ; Protein Serine-Threonine Kinases/genetics ; Receptors, Pattern Recognition/metabolism
    Chemical Substances Antigen-Antibody Complex ; Arabidopsis Proteins ; EDR1 protein, Arabidopsis ; GPI-Linked Proteins ; Glycosylphosphatidylinositols ; LLG1 protein, Arabidopsis ; Receptors, Pattern Recognition ; Protein Kinases (EC 2.7.-) ; Protein Serine-Threonine Kinases (EC 2.7.11.1)
    Language English
    Publishing date 2022-08-18
    Publishing country China (Republic : 1949- )
    Document type Journal Article
    ZDB-ID 2130095-1
    ISSN 1744-7909 ; 1672-9072
    ISSN (online) 1744-7909
    ISSN 1672-9072
    DOI 10.1111/jipb.13327
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  5. Article ; Online: Fimbrin associated with Pmk1 to regulate the actin assembly during Magnaporthe oryzae hyphal growth and infection.

    Li, Yuan-Bao / Shen, Ningning / Deng, Xianya / Liu, Zixuan / Zhu, Shuai / Liu, Chengyu / Tang, Dingzhong / Han, Li-Bo

    Stress biology

    2024  Volume 4, Issue 1, Page(s) 5

    Abstract: The dynamic assembly of the actin cytoskeleton is vital for Magnaporthe oryzae development and host infection. The actin-related protein MoFim1 is a key factor for organizing the M. oryzae actin cytoskeleton. Currently, how MoFim1 is regulated in M. ... ...

    Abstract The dynamic assembly of the actin cytoskeleton is vital for Magnaporthe oryzae development and host infection. The actin-related protein MoFim1 is a key factor for organizing the M. oryzae actin cytoskeleton. Currently, how MoFim1 is regulated in M. oryzae to precisely rearrange the actin cytoskeleton is unclear. In this study, we found that MoFim1 associates with the M. oryzae mitogen-activated protein (MAP) kinase Pmk1 to regulate actin assembly. MoFim1 directly interacted with Pmk1, and the phosphorylation level of MoFim1 was decreased in Δpmk1, which led to a change in the subcellular distribution of MoFim1 in the hyphae of Δpmk1. Moreover, the actin cytoskeleton was aberrantly organized at the hyphal tip in the Δpmk1, which was similar to what was observed in the Δmofim1 during hyphal growth. Furthermore, phosphorylation analysis revealed that Pmk1 could phosphorylate MoFim1 at serine 94. Loss of phosphorylation of MoFim1 at serine 94 decreased actin bundling activity. Additionally, the expression of the site mutant of MoFim1 S94D (in which serine 94 was replaced with aspartate to mimic phosphorylation) in Δpmk1 could reverse the defects in actin organization and hyphal growth in Δpmk1. It also partially rescues the formation of appressorium failure in Δpmk1. Taken together, these findings suggest a regulatory mechanism in which Pmk1 phosphorylates MoFim1 to regulate the assembly of the actin cytoskeleton during hyphal development and pathogenesis.
    Language English
    Publishing date 2024-01-22
    Publishing country Switzerland
    Document type Journal Article
    ISSN 2731-0450
    ISSN (online) 2731-0450
    DOI 10.1007/s44154-023-00147-5
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  6. Article ; Online: Mechanism of plant immune activation and signaling: Insight from the first solved plant resistosome structure.

    Feng, Baomin / Tang, Dingzhong

    Journal of integrative plant biology

    2019  Volume 61, Issue 8, Page(s) 902–907

    Abstract: This commentary introduces an exciting breakthrough: the first solved structure of a plant NLR immune receptor complex. The significance of this work, including the similarity between the activation of NLRs from plants and animals, and potentially novel ... ...

    Abstract This commentary introduces an exciting breakthrough: the first solved structure of a plant NLR immune receptor complex. The significance of this work, including the similarity between the activation of NLRs from plants and animals, and potentially novel mechanism of immune signaling in plants, were discussed and put into perspective.
    MeSH term(s) Plant Immunity/physiology ; Plants/immunology ; Plants/metabolism ; Signal Transduction/immunology ; Signal Transduction/physiology
    Language English
    Publishing date 2019-05-22
    Publishing country China (Republic : 1949- )
    Document type Journal Article
    ZDB-ID 2130095-1
    ISSN 1744-7909 ; 1672-9072
    ISSN (online) 1744-7909
    ISSN 1672-9072
    DOI 10.1111/jipb.12814
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  7. Article ; Online: The Microtubule End Binding Protein Mal3 Is Essential for the Dynamic Assembly of Microtubules during

    Shen, Ningning / Han, Libo / Liu, Zixuan / Deng, Xianya / Zhu, Shuai / Liu, Chengyu / Tang, Dingzhong / Li, Yuanbao

    International journal of molecular sciences

    2024  Volume 25, Issue 5

    Abstract: Cytoskeletal microtubules (MTs) play crucial roles in many aspects of life processes in eukaryotic organisms. They dynamically assemble physiologically important MT arrays under different cell conditions. Currently, aspects of MT assembly underlying the ... ...

    Abstract Cytoskeletal microtubules (MTs) play crucial roles in many aspects of life processes in eukaryotic organisms. They dynamically assemble physiologically important MT arrays under different cell conditions. Currently, aspects of MT assembly underlying the development and pathogenesis of the model plant pathogenic fungus
    MeSH term(s) Carrier Proteins/metabolism ; Magnaporthe/physiology ; Ascomycota/metabolism ; Microtubules/metabolism ; Oryza/metabolism ; Plant Diseases/microbiology ; Fungal Proteins/metabolism
    Chemical Substances Carrier Proteins ; Fungal Proteins
    Language English
    Publishing date 2024-02-26
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms25052672
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  8. Article: Wheat powdery mildew resistance: from gene identification to immunity deployment.

    Zou, Shenghao / Xu, Yang / Li, Qianqian / Wei, Yali / Zhang, Youlian / Tang, Dingzhong

    Frontiers in plant science

    2023  Volume 14, Page(s) 1269498

    Abstract: Powdery mildew is one of the most devastating diseases on wheat and is caused by the obligate biotrophic ... ...

    Abstract Powdery mildew is one of the most devastating diseases on wheat and is caused by the obligate biotrophic phytopathogen
    Language English
    Publishing date 2023-09-18
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2613694-6
    ISSN 1664-462X
    ISSN 1664-462X
    DOI 10.3389/fpls.2023.1269498
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  9. Article ; Online: MITOGEN-ACTIVATED PROTEIN KINASE3 enhances disease resistance of edr1 mutants by phosphorylating MAPKKK5.

    Wang, Wei / Chen, Shuling / Zhong, Guitao / Gao, Chenyang / Zhang, Qin / Tang, Dingzhong

    Plant physiology

    2023  Volume 194, Issue 1, Page(s) 578–591

    Abstract: Mitogen-activated protein kinase (MAPK/MPK) cascades are key signaling modules that regulate plant immunity. ENHANCED DISEASE RESISTANCE1 (EDR1) encodes a Raf-like MAPK kinase kinase (MAPKKK) that negatively regulates plant defense in Arabidopsis ( ... ...

    Abstract Mitogen-activated protein kinase (MAPK/MPK) cascades are key signaling modules that regulate plant immunity. ENHANCED DISEASE RESISTANCE1 (EDR1) encodes a Raf-like MAPK kinase kinase (MAPKKK) that negatively regulates plant defense in Arabidopsis (Arabidopsis thaliana). The enhanced resistance of edr1 requires MAPK KINASE4 (MKK4), MKK5, and MPK3. Although the edr1 mutant displays higher MPK3/6 activation, the mechanism by which plants increase MAPK cascade activation remains elusive. Our previous study showed that MAPKKK5 is phosphorylated at the Ser-90 residue in edr1 mutants. In this study, we demonstrated that the enhanced disease resistance of edr1 required MAPKKK5. Phospho-dead MAPKKK5S90A partially impaired the resistance of edr1, and the expression of phospho-mimetic MAPKKK5S90D in mapkkk5-2 resulted in enhanced resistance to the powdery mildew Golovinomyces cichoracearum strain UCSC1 and the bacterial pathogen Pseudomonas syringae pv. tomato (Pto) strain DC3000. Thus, Ser-90 phosphorylation in MAPKKK5 appears to play a crucial role in disease resistance. However, MAPKKK5-triggered cell death was not suppressed by EDR1. Furthermore, activated MPK3 phosphorylated the N terminus of MAPKKK5, and Ser-90 was one of the phosphorylated sites. Ser-90 phosphorylation increased MAPKKK5 stability, and EDR1 might negatively regulate MAPK cascade activation by suppressing the MPK3-mediated feedback regulation of MAPKKK5. Taken together, these results indicate that MPK3 phosphorylates MAPKKK5 to enhance MAPK cascade activation and disease resistance in edr1 mutants.
    MeSH term(s) Humans ; Disease Resistance/genetics ; Arabidopsis Proteins/metabolism ; MAP Kinase Kinase Kinase 5/metabolism ; Mitogens/metabolism ; Arabidopsis/metabolism ; Gene Expression Regulation, Plant ; Plant Diseases/microbiology
    Chemical Substances Arabidopsis Proteins ; MAP Kinase Kinase Kinase 5 (EC 2.7.11.25) ; Mitogens ; EDR1 protein, Arabidopsis
    Language English
    Publishing date 2023-08-24
    Publishing country United States
    Document type Journal Article
    ZDB-ID 208914-2
    ISSN 1532-2548 ; 0032-0889
    ISSN (online) 1532-2548
    ISSN 0032-0889
    DOI 10.1093/plphys/kiad472
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  10. Article: Mechanism of plant immune activation and signaling: Insight from the first solved plant resistosome structure

    Feng, Baomin / Tang, Dingzhong

    Journal of integrative plant biology. 2019 Aug., v. 61, no. 8

    2019  

    Abstract: This commentary introduces an exciting breakthrough: the first solved structure of a plant NLR immune receptor complex. The significance of this work, including the similarity between the activation of NLRs from plants and animals, and potentially novel ... ...

    Abstract This commentary introduces an exciting breakthrough: the first solved structure of a plant NLR immune receptor complex. The significance of this work, including the similarity between the activation of NLRs from plants and animals, and potentially novel mechanism of immune signaling in plants, were discussed and put into perspective.
    Keywords immunologic receptors ; plant proteins ; resistance mechanisms ; signal transduction
    Language English
    Dates of publication 2019-08
    Size p. 902-907.
    Publishing place John Wiley & Sons, Ltd
    Document type Article
    Note JOURNAL ARTICLE
    ZDB-ID 2130095-1
    ISSN 1744-7909 ; 1672-9072
    ISSN (online) 1744-7909
    ISSN 1672-9072
    DOI 10.1111/jipb.12814
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