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学者姓名：林文伟
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Abstract ：
Magnaporthe oryzae is a devastating fungal pathogen that causes the rice blast disease worldwide. The post-translational modification of ADP-ribosylation holds significant importance in various fundamental biological processes. However, the specific function of this modification in M. oryzae remains unknown. This study revealed that Poly(ADP-ribosyl)ation (PARylation) executes a critical function in M. oryzae. M. oryzae Poly(ADP-ribose) polymerase 1 (PARP1) exhibits robust PARylation activity. Disruption of PARylation by PARP1 knock-out or chemical inhibition reveals its involvement in M. oryzae virulence, particularly in appressorium formation. Furthermore, we identified two M. oryzae 14-3-3 proteins, GRF1 and GRF2, as substrates of PARP1. Deletion of GRF1 or GRF2 results in delayed and dysfunctional appressorium, diminished plant penetration, and reduced virulence of the fungus. Biochemical and genetic evidence suggest that PARylation of 14-3-3s is essential for its function in M. oryzae virulence. Moreover, PARylation regulates 14-3-3 dimerization and is required for the activation of the mitogen-activated protein kinases (MAPKs), Pmk1 and Mps1. GRF1 interacts with both Mst7 and Pmk1, and bridges their interaction in a PARylation-dependent manner. This study unveils a distinctive mechanism that PARylation of 14-3-3 proteins controls appressorium formation through MAPK activation, and could facilitate the development of new strategies of rice blast disease control.
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| GB/T 7714 | Gao, Xiuqin , Gao, Gaigai , Zheng, Weifeng et al. PARylation of 14-3-3 proteins controls the virulence of Magnaporthe oryzae [J]. | NATURE COMMUNICATIONS , 2024 , 15 (1) . |
| MLA | Gao, Xiuqin et al. "PARylation of 14-3-3 proteins controls the virulence of Magnaporthe oryzae" . | NATURE COMMUNICATIONS 15 . 1 (2024) . |
| APA | Gao, Xiuqin , Gao, Gaigai , Zheng, Weifeng , Liu, Haibing , Pan, Wenbo , Xia, Xi et al. PARylation of 14-3-3 proteins controls the virulence of Magnaporthe oryzae . | NATURE COMMUNICATIONS , 2024 , 15 (1) . |
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Extracellular perception of auxin, an essential phytohormone in plants, has been debated for decades. Auxin binding protein 1 (ABP1) physically interacts with quintessential transmembrane kinases (TMKs) and was proposed to act as an extracellular auxin receptor, but its role was disputed because abp1 knockout mutants lack obvious morphological phenotypes. Here, we identified two new auxin-binding proteins, ABL1 and ABL2, that are localized to the apoplast and directly interact with the extracellular domain of TMKs in an auxin-dependent manner. Furthermore, functionally redundant ABL1 and ABL2 genetically interact with TMKs and exhibit functions that overlap with those of ABP1 as well as being independent of ABP1. Importantly, the extracellular domain of TMK1 itself binds auxin and synergizes with either ABP1 or ABL1 in auxin binding. Thus, our findings discovered auxin receptors ABL1 and ABL2 having functions overlapping with but distinct from ABP1 and acting together with TMKs as co-receptors for extracellular auxin.
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| GB/T 7714 | Yu, Yongqiang , Tang, Wenxin , Lin, Wenwei et al. ABLs and TMKs are co-receptors for extracellular auxin [J]. | CELL , 2023 , 186 (25) . |
| MLA | Yu, Yongqiang et al. "ABLs and TMKs are co-receptors for extracellular auxin" . | CELL 186 . 25 (2023) . |
| APA | Yu, Yongqiang , Tang, Wenxin , Lin, Wenwei , Li, Wei , Zhou, Xiang , Li, Ying et al. ABLs and TMKs are co-receptors for extracellular auxin . | CELL , 2023 , 186 (25) . |
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Spatial partitioning is a propensity of biological systems orchestrating cell activities in space and time. The dynamic regulation of plasma membrane nano-environments has recently emerged as a key fundamental aspect of plant signaling, but the molecular components governing it are still mostly unclear. The receptor kinase FERONIA (FER) controls ligand-induced complex formation of the immune receptor kinase FLAGELLIN SENSING 2 (FLS2) with its co-receptor BRASSINOSTEROID-INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1), and perception of the endogenous peptide hormone RAPID ALKALANIZATION FACTOR 23 (RALF23) by FER inhibits immunity. Here, we show that FER regulates the plasma membrane nanoscale organization of FLS2 and BAK1. Our study demonstrates that akin to FER, leucine-rich repeat (LRR) extensin proteins (LRXs) contribute to RALF23 responsiveness and regulate BAK1 nanoscale organization and immune signaling. Furthermore, RALF23 perception leads to rapid modification of FLS2 and BAK1 nanoscale organization, and its inhibitory activity on immune signaling relies on FER kinase activity. Our results suggest that perception of RALF peptides by FER and LRXs actively modulates plasma membrane nanoscale organization to regulate cell surface signaling by other ligand-binding receptor kinases.
Keyword ：
A A innate immunity innate immunity nanoscale organization nanoscale organization peptide hormones peptide hormones plasma membrane plasma membrane receptor kinase receptor kinase signaling signaling thaliana thaliana
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| GB/T 7714 | Gronnier, Julien , Franck, Christina M. , Stegmann, Martin et al. Regulation of immune receptor kinase plasma membrane nanoscale organization by a plant peptide hormone and its receptors [J]. | ELIFE , 2022 , 11 . |
| MLA | Gronnier, Julien et al. "Regulation of immune receptor kinase plasma membrane nanoscale organization by a plant peptide hormone and its receptors" . | ELIFE 11 (2022) . |
| APA | Gronnier, Julien , Franck, Christina M. , Stegmann, Martin , DeFalco, Thomas A. , Abarca, Alicia , von Arx, Michelle et al. Regulation of immune receptor kinase plasma membrane nanoscale organization by a plant peptide hormone and its receptors . | ELIFE , 2022 , 11 . |
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Sclerotinia sclerotiorum is a devastating pathogen that infects a broad range of host plants. The mechanism underlying plant defence against fungal invasion is still not well characterized. Here, we report that ANGUSTIFOLIA (AN), a CtBP family member, plays a role in the defence against S. sclerotiorum attack. Arabidopsis an mutants exhibited stronger resistance to S. sclerotiorum at the early stage of infection than wild-type plants. Accordingly, an mutants exhibited stronger activation of pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) responses, including mitogen-activated protein kinase activation, reactive oxygen species accumulation, callose deposition, and the expression of PTI-responsive genes, upon treatment with PAMPs/microbe-associated molecular patterns. Moreover, Arabidopsis lines overexpressing AN were more susceptible to S. sclerotiorum and showed defective PTI responses. Our luminometry, bimolecular fluorescence complementation, coimmunoprecipitation, and in vitro pull-down assays indicate that AN interacts with allene oxide cyclases (AOC), essential enzymes involved in jasmonic acid (JA) biosynthesis, negatively regulating JA biosynthesis in response to S. sclerotiorum infection. This work reveals AN is a negative regulator of the AOC-mediated JA signalling pathway and PTI activation.
Keyword ：
ANGUSTIFOLIA gene ANGUSTIFOLIA gene Arabidopsis thaliana Arabidopsis thaliana JA signalling pathway JA signalling pathway PAMP-triggered immunity PAMP-triggered immunity Sclerotinia sclerotiorum Sclerotinia sclerotiorum
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| GB/T 7714 | Gao, Xiuqin , Dang, Xie , Yan, Fengting et al. ANGUSTIFOLIA negatively regulates resistance to Sclerotinia sclerotiorum via modulation of PTI and JA signalling pathways in Arabidopsis thaliana [J]. | MOLECULAR PLANT PATHOLOGY , 2022 , 23 (8) : 1091-1106 . |
| MLA | Gao, Xiuqin et al. "ANGUSTIFOLIA negatively regulates resistance to Sclerotinia sclerotiorum via modulation of PTI and JA signalling pathways in Arabidopsis thaliana" . | MOLECULAR PLANT PATHOLOGY 23 . 8 (2022) : 1091-1106 . |
| APA | Gao, Xiuqin , Dang, Xie , Yan, Fengting , Li, Yuhua , Xu, Jing , Tian, Shifu et al. ANGUSTIFOLIA negatively regulates resistance to Sclerotinia sclerotiorum via modulation of PTI and JA signalling pathways in Arabidopsis thaliana . | MOLECULAR PLANT PATHOLOGY , 2022 , 23 (8) , 1091-1106 . |
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During growth and morphogenesis, plant cells respond to mechanical stresses resulting from spatiotemporal changes in the cell wall that bear high internal turgor pressure. Microtubule (MT) arrays are reorganized to align in the direction of maximal tensile stress, presumably reinforcing the local cell wall by guiding the synthesis of cellulose. However, how mechanical forces regulate MT reorganization remains largely unknown. Here, we demonstrate that mechanical signaling that is based on the Catharanthus roseus RLK1-like kinase (CrRLK1L) subfamily receptor kinase FERONIA (FER) regulates the reorganization of cortical MT in cotyledon epidermal pavement cells (PCs) in Arabidopsis. Recessive mutations in FER compromised MT responses to mechanical perturbations, such as single-cell ablation, compression, and isoxaben treatment, in these PCs. These perturbations promoted the activation of ROP6 guanosine triphosphatase (GTPase) that acts directly downstream of FER. Furthermore, defects in the ROP6 signaling pathway negated the reorganization of cortical MTs induced by these stresses. Finally, reduction in highly demethylesterified pectin, which binds the extracellular malectin domains of FER and is required for FER-mediated ROP6 activation, also impacted mechanical induction of cortical MT reorganization. Taken together, our results suggest that the FER-pectin complex senses and/or transduces mechanical forces to regulate MT organization through activating the ROP6 signaling pathway in Arabidopsis.
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| GB/T 7714 | Tang, Wenxin , Lin, Wenwei , Zhou, Xiang et al. Mechano-transduction via the pectin-FERONIA complex activates ROP6 GTPase signaling in Arabidopsis pavement cell morphogenesis [J]. | CURRENT BIOLOGY , 2022 , 32 (3) : 508-, . |
| MLA | Tang, Wenxin et al. "Mechano-transduction via the pectin-FERONIA complex activates ROP6 GTPase signaling in Arabidopsis pavement cell morphogenesis" . | CURRENT BIOLOGY 32 . 3 (2022) : 508-, . |
| APA | Tang, Wenxin , Lin, Wenwei , Zhou, Xiang , Guo, Jingzhe , Dang, Xie , Li, Binqi et al. Mechano-transduction via the pectin-FERONIA complex activates ROP6 GTPase signaling in Arabidopsis pavement cell morphogenesis . | CURRENT BIOLOGY , 2022 , 32 (3) , 508-, . |
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The phytohormone auxin controls many processes in plants, at least in part through its regulation of cell expansion(1). The acid growth hypothesis has been proposed to explain auxin-stimulated cell expansion for five decades, but the mechanism that underlies auxin-induced cell-wall acidification is poorly characterized. Auxin induces the phosphorylation and activation of the plasma membrane H+-ATPase that pumps protons into the apoplast(2), yet how auxin activates its phosphorylation remains unclear. Here we show that the transmembrane kinase (TMK) auxin-signalling proteins interact with plasma membrane H+-ATPases, inducing their phosphorylation, and thereby promoting cell-wall acidification and hypocotyl cell elongation in Arabidopsis. Auxin induced interactions between TMKs and H+-ATPases in the plasma membrane within seconds, as well as TMK-dependent phosphorylation of the penultimate threonine residue on the H+-ATPases. Our genetic, biochemical and molecular evidence demonstrates that TMKs directly phosphorylate plasma membrane H+-ATPase and are required for auxin-induced H+-ATPase activation, apoplastic acidification and cell expansion. Thus, our findings reveal a crucial connection between auxin and plasma membrane H+-ATPase activation in regulating apoplastic pH changes and cell expansion through TMK-based cell surface auxin signalling.
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| GB/T 7714 | Lin, Wenwei , Zhou, Xiang , Tang, Wenxin et al. TMK-based cell-surface auxin signalling activates cell-wall acidification [J]. | NATURE , 2021 , 599 (7884) : 278-, . |
| MLA | Lin, Wenwei et al. "TMK-based cell-surface auxin signalling activates cell-wall acidification" . | NATURE 599 . 7884 (2021) : 278-, . |
| APA | Lin, Wenwei , Zhou, Xiang , Tang, Wenxin , Takahashi, Koji , Pan, Xue , Dai, Jiawei et al. TMK-based cell-surface auxin signalling activates cell-wall acidification . | NATURE , 2021 , 599 (7884) , 278-, . |
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Invasive or penetrative growth is critical for developmental and reproductive processes (e.g., pollen tube penetration of pistils) and disease progression (e.g., cancer metastasis and fungal hyphae invasion). The invading or penetrating cells experience drastic changes in mechanical pressure from the surroundings and must balance growth with cell integrity. Here, we show that Arabidopsis pollen tubes sense and/or respond to mechanical changes via a cell-surface receptor kinase Buddha's Paper Seal 1 (BUPS1) while emerging from compressing female tissues. BUPS1-defective pollen tubes fail to maintain cell integrity after emergence from these tissues. The mechano-transduction function of BUPS1 is established by using a microfluidic channel device mimicking the mechanical features of the in vivo growth path. BUPS1-based mechano-transduction activates Rho-like GTPase from Plant 1 (ROP1) GTPase to promote exocytosis that facilitates secretion of BUPS1's ligands for mechanical signal amplification and cell wall rigidification in pollen tubes. These findings uncover a membrane receptor-based mechano-transduction system for cells to cope with the physical challenges during invasive or penetrative growth.
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| GB/T 7714 | Zhou, Xiang , Lu, Jun , Zhang, Yuqin et al. Membrane receptor-mediated mechano-transduction maintains cell integrity during pollen tube growth within the pistil [J]. | DEVELOPMENTAL CELL , 2021 , 56 (7) : 1030-, . |
| MLA | Zhou, Xiang et al. "Membrane receptor-mediated mechano-transduction maintains cell integrity during pollen tube growth within the pistil" . | DEVELOPMENTAL CELL 56 . 7 (2021) : 1030-, . |
| APA | Zhou, Xiang , Lu, Jun , Zhang, Yuqin , Guo, Jingzhe , Lin, Wenwei , Van Norman, Jaimie M. et al. Membrane receptor-mediated mechano-transduction maintains cell integrity during pollen tube growth within the pistil . | DEVELOPMENTAL CELL , 2021 , 56 (7) , 1030-, . |
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Cell polarity is fundamental to the development of both eukaryotes and prokaryotes, yet the mechanisms behind its formation are not well understood. Here we found that, phytohormone auxin-induced, sterol-dependent nanoclustering of cell surface transmembrane receptor kinase 1 (TMK1) is critical for the formation of polarized domains at the plasma membrane (PM) during the morphogenesis of cotyledon pavement cells (PC) in Arabidopsis. Auxin-induced TMK1 nanoclustering stabilizes flotillin1-associated ordered nanodomains, which in turn promote the nanoclustering of ROP6 GTPase that acts downstream of TMK1 to regulate cortical microtubule organization. In turn, cortical microtubules further stabilize TMK1- and flotillin1-containing nanoclusters at the PM. Hence, we propose a new paradigm for polarity formation: A diffusive signal triggers cell polarization by promoting cell surface receptor-mediated nanoclustering of signaling components and cytoskeleton-mediated positive feedback that reinforces these nanodomains into polarized domains. The significance of protein nanoclustering in cell polarization is unclear. Here Pan et al. show that auxin-induced TMK1/sterol nanoclustering as well as microtubule-based positive feedback regulation of the TMK1/sterol nanoclusters is critical for cell polarity formation in Arabidopsis.
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| GB/T 7714 | Pan, Xue , Fang, Linjing , Liu, Jianfeng et al. Auxin-induced signaling protein nanoclustering contributes to cell polarity formation [J]. | NATURE COMMUNICATIONS , 2020 , 11 (1) . |
| MLA | Pan, Xue et al. "Auxin-induced signaling protein nanoclustering contributes to cell polarity formation" . | NATURE COMMUNICATIONS 11 . 1 (2020) . |
| APA | Pan, Xue , Fang, Linjing , Liu, Jianfeng , Senay-Aras, Betul , Lin, Wenwei , Zheng, Shuan et al. Auxin-induced signaling protein nanoclustering contributes to cell polarity formation . | NATURE COMMUNICATIONS , 2020 , 11 (1) . |
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Abstract ：
Invasive growth is critical for developmental and reproductive processes (e.g., pollen tube penetration of pistils) and disease progression (e.g., cancer metastasis and fungal hyphae invasion). The invading cells experience drastic changes in mechanical pressure from the surroundings and must balance growth with cell integrity. Here we show that Arabidopsis pollen tubes sense mechanical changes via a cell-surface receptor kinase CUPID1 while penetrating compressing female tissues. Pollen tubes carrying cupid1 mutations fail to maintain cell integrity and burst after exiting these tissues. The mechanosensing function of CUPID1 is established in a microfluidic channel device that mimics the mechanical features of the in vivo growth path. CUPID1-based mechanosensing activates ROP1 GTPase signaling to promote exocytosis that facilitates the secretion of CUPID1's ligands for mechanical signal amplification and cell wall rigidification in pollen tubes. These findings uncover a membrane receptor-mediated mechanosensing system for cells to cope with the physical challenges during invasive growth. © 2020, The Authors. All rights reserved.
Keyword ：
Cell membranes Cell membranes Cell signaling Cell signaling Cytology Cytology Diseases Diseases Histology Histology Tissue Tissue Tubes (components) Tubes (components)
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| GB/T 7714 | Zhou, Xiang , Lu, Jun , Zhang, Yuqin et al. A Membrane Receptor-Mediated Mechanosensing System Maintains Cell Integrity during Invasive Growth [J]. | SSRN , 2020 . |
| MLA | Zhou, Xiang et al. "A Membrane Receptor-Mediated Mechanosensing System Maintains Cell Integrity during Invasive Growth" . | SSRN (2020) . |
| APA | Zhou, Xiang , Lu, Jun , Zhang, Yuqin , Guo, Jingzhe , Lin, Wenwei , van Norman, Jaimie M. et al. A Membrane Receptor-Mediated Mechanosensing System Maintains Cell Integrity during Invasive Growth . | SSRN , 2020 . |
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| GB/T 7714 | Lin, W. W. , Zhang, J. , Yang, W. T. et al. First Report of Bamboo mosaic virus Infecting Bamboo in the Mainland of China [J]. | PLANT DISEASE , 2015 , 99 (8) : 1189-1189 . |
| MLA | Lin, W. W. et al. "First Report of Bamboo mosaic virus Infecting Bamboo in the Mainland of China" . | PLANT DISEASE 99 . 8 (2015) : 1189-1189 . |
| APA | Lin, W. W. , Zhang, J. , Yang, W. T. , Liu, Y. Y. , Wan, B. J. , Xu, X. L. et al. First Report of Bamboo mosaic virus Infecting Bamboo in the Mainland of China . | PLANT DISEASE , 2015 , 99 (8) , 1189-1189 . |
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