S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation

Abstract Small peptides modulate multiple processes in plant cells, but their regulation by post-translational modification remains unclear. ROT4 (ROTUNDIFOLIA4) belongs to a family of Arabidopsis non-secreted small peptides, but knowledge on its molecular function and how it is regulated is limited...
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Autor*in:	Li, Wenliang [verfasserIn] Ye, Tushu Ye, Weixian Liang, Jieyi Wang, Wen Han, Danlu Liu, Xiaoshi Huang, Liting Ouyang, Youwei Liao, Jianwei Chen, Tongsheng Yang, Chengwei Lai, Jianbin

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2024

Schlagwörter:	Arabidopsis Plant Immunity Protein S-acylation ROT4 Small Peptide

Anmerkung:	© The Author(s) 2024

Übergeordnetes Werk:	Enthalten in: EMBO Reports - Nature Publishing Group UK, 2023, 25(2024), 2 vom: 02. Jan., Seite 489-505
Übergeordnetes Werk:	volume:25 ; year:2024 ; number:2 ; day:02 ; month:01 ; pages:489-505

Links:	Volltext

DOI / URN:	10.1038/s44319-023-00029-x

Katalog-ID:	SPR054761395

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520			\|a Abstract Small peptides modulate multiple processes in plant cells, but their regulation by post-translational modification remains unclear. ROT4 (ROTUNDIFOLIA4) belongs to a family of Arabidopsis non-secreted small peptides, but knowledge on its molecular function and how it is regulated is limited. Here, we find that ROT4 is S-acylated in plant cells. S-acylation is an important form of protein lipidation, yet so far it has not been reported to regulate small peptides in plants. We show that this modification is essential for the plasma membrane association of ROT4. Overexpression of S-acylated ROT4 results in a dramatic increase in immune gene expression. S-acylation of ROT4 enhances its interaction with BSK5 (BRASSINOSTEROID-SIGNALING KINASE 5) to block the association between BSK5 and PEPR1 (PEP RECEPTOR1), a receptor kinase for secreted plant elicitor peptides (PEPs), thereby activating immune signaling. Phenotype analysis indicates that S-acylation is necessary for ROT4 functions in pathogen resistance, PEP response, and the regulation of development. Collectively, our work reveals an important role for S-acylation in the cross-talk of non-secreted and secreted peptide signaling in plant immunity.
520			\|a Synopsis S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. S-acylation is important for the plasma membrane localization of the non-secreted plant peptide ROT4.The upregulation of plant immune genes mediated by ROT4 requires its S-acylation.S-acylation of ROT4 increases its association with BSK5 for activation of plant elicitor peptide signaling.S-acylation is necessary for the function of ROT4 in plant immunity and in pathogen resistance.
520			\|a S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides.
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allfields	10.1038/s44319-023-00029-x doi (DE-627)SPR054761395 (SPR)s44319-023-00029-x-e DE-627 ger DE-627 rakwb eng Li, Wenliang verfasserin (orcid)0009-0002-5593-5615 aut S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2024 Abstract Small peptides modulate multiple processes in plant cells, but their regulation by post-translational modification remains unclear. ROT4 (ROTUNDIFOLIA4) belongs to a family of Arabidopsis non-secreted small peptides, but knowledge on its molecular function and how it is regulated is limited. Here, we find that ROT4 is S-acylated in plant cells. S-acylation is an important form of protein lipidation, yet so far it has not been reported to regulate small peptides in plants. We show that this modification is essential for the plasma membrane association of ROT4. Overexpression of S-acylated ROT4 results in a dramatic increase in immune gene expression. S-acylation of ROT4 enhances its interaction with BSK5 (BRASSINOSTEROID-SIGNALING KINASE 5) to block the association between BSK5 and PEPR1 (PEP RECEPTOR1), a receptor kinase for secreted plant elicitor peptides (PEPs), thereby activating immune signaling. Phenotype analysis indicates that S-acylation is necessary for ROT4 functions in pathogen resistance, PEP response, and the regulation of development. Collectively, our work reveals an important role for S-acylation in the cross-talk of non-secreted and secreted peptide signaling in plant immunity. Synopsis S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. S-acylation is important for the plasma membrane localization of the non-secreted plant peptide ROT4.The upregulation of plant immune genes mediated by ROT4 requires its S-acylation.S-acylation of ROT4 increases its association with BSK5 for activation of plant elicitor peptide signaling.S-acylation is necessary for the function of ROT4 in plant immunity and in pathogen resistance. S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. Arabidopsis (dpeaa)DE-He213 Plant Immunity (dpeaa)DE-He213 Protein S-acylation (dpeaa)DE-He213 ROT4 (dpeaa)DE-He213 Small Peptide (dpeaa)DE-He213 Ye, Tushu aut Ye, Weixian aut Liang, Jieyi aut Wang, Wen (orcid)0009-0009-8695-1803 aut Han, Danlu (orcid)0000-0002-9828-371X aut Liu, Xiaoshi (orcid)0000-0002-2851-7330 aut Huang, Liting aut Ouyang, Youwei aut Liao, Jianwei aut Chen, Tongsheng aut Yang, Chengwei (orcid)0000-0002-2648-3181 aut Lai, Jianbin (orcid)0000-0002-9269-9052 aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 25(2024), 2 vom: 02. Jan., Seite 489-505 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:25 year:2024 number:2 day:02 month:01 pages:489-505 https://dx.doi.org/10.1038/s44319-023-00029-x kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_22 GBV_ILN_24 GBV_ILN_62 GBV_ILN_63 GBV_ILN_120 GBV_ILN_150 GBV_ILN_168 GBV_ILN_211 GBV_ILN_252 GBV_ILN_266 GBV_ILN_2005 GBV_ILN_2010 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2037 GBV_ILN_2064 GBV_ILN_2108 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2336 GBV_ILN_2472 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 25 2024 2 02 01 489-505
spelling	10.1038/s44319-023-00029-x doi (DE-627)SPR054761395 (SPR)s44319-023-00029-x-e DE-627 ger DE-627 rakwb eng Li, Wenliang verfasserin (orcid)0009-0002-5593-5615 aut S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2024 Abstract Small peptides modulate multiple processes in plant cells, but their regulation by post-translational modification remains unclear. ROT4 (ROTUNDIFOLIA4) belongs to a family of Arabidopsis non-secreted small peptides, but knowledge on its molecular function and how it is regulated is limited. Here, we find that ROT4 is S-acylated in plant cells. S-acylation is an important form of protein lipidation, yet so far it has not been reported to regulate small peptides in plants. We show that this modification is essential for the plasma membrane association of ROT4. Overexpression of S-acylated ROT4 results in a dramatic increase in immune gene expression. S-acylation of ROT4 enhances its interaction with BSK5 (BRASSINOSTEROID-SIGNALING KINASE 5) to block the association between BSK5 and PEPR1 (PEP RECEPTOR1), a receptor kinase for secreted plant elicitor peptides (PEPs), thereby activating immune signaling. Phenotype analysis indicates that S-acylation is necessary for ROT4 functions in pathogen resistance, PEP response, and the regulation of development. Collectively, our work reveals an important role for S-acylation in the cross-talk of non-secreted and secreted peptide signaling in plant immunity. Synopsis S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. S-acylation is important for the plasma membrane localization of the non-secreted plant peptide ROT4.The upregulation of plant immune genes mediated by ROT4 requires its S-acylation.S-acylation of ROT4 increases its association with BSK5 for activation of plant elicitor peptide signaling.S-acylation is necessary for the function of ROT4 in plant immunity and in pathogen resistance. S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. Arabidopsis (dpeaa)DE-He213 Plant Immunity (dpeaa)DE-He213 Protein S-acylation (dpeaa)DE-He213 ROT4 (dpeaa)DE-He213 Small Peptide (dpeaa)DE-He213 Ye, Tushu aut Ye, Weixian aut Liang, Jieyi aut Wang, Wen (orcid)0009-0009-8695-1803 aut Han, Danlu (orcid)0000-0002-9828-371X aut Liu, Xiaoshi (orcid)0000-0002-2851-7330 aut Huang, Liting aut Ouyang, Youwei aut Liao, Jianwei aut Chen, Tongsheng aut Yang, Chengwei (orcid)0000-0002-2648-3181 aut Lai, Jianbin (orcid)0000-0002-9269-9052 aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 25(2024), 2 vom: 02. Jan., Seite 489-505 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:25 year:2024 number:2 day:02 month:01 pages:489-505 https://dx.doi.org/10.1038/s44319-023-00029-x kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_22 GBV_ILN_24 GBV_ILN_62 GBV_ILN_63 GBV_ILN_120 GBV_ILN_150 GBV_ILN_168 GBV_ILN_211 GBV_ILN_252 GBV_ILN_266 GBV_ILN_2005 GBV_ILN_2010 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2037 GBV_ILN_2064 GBV_ILN_2108 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2336 GBV_ILN_2472 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 25 2024 2 02 01 489-505
allfields_unstemmed	10.1038/s44319-023-00029-x doi (DE-627)SPR054761395 (SPR)s44319-023-00029-x-e DE-627 ger DE-627 rakwb eng Li, Wenliang verfasserin (orcid)0009-0002-5593-5615 aut S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2024 Abstract Small peptides modulate multiple processes in plant cells, but their regulation by post-translational modification remains unclear. ROT4 (ROTUNDIFOLIA4) belongs to a family of Arabidopsis non-secreted small peptides, but knowledge on its molecular function and how it is regulated is limited. Here, we find that ROT4 is S-acylated in plant cells. S-acylation is an important form of protein lipidation, yet so far it has not been reported to regulate small peptides in plants. We show that this modification is essential for the plasma membrane association of ROT4. Overexpression of S-acylated ROT4 results in a dramatic increase in immune gene expression. S-acylation of ROT4 enhances its interaction with BSK5 (BRASSINOSTEROID-SIGNALING KINASE 5) to block the association between BSK5 and PEPR1 (PEP RECEPTOR1), a receptor kinase for secreted plant elicitor peptides (PEPs), thereby activating immune signaling. Phenotype analysis indicates that S-acylation is necessary for ROT4 functions in pathogen resistance, PEP response, and the regulation of development. Collectively, our work reveals an important role for S-acylation in the cross-talk of non-secreted and secreted peptide signaling in plant immunity. Synopsis S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. S-acylation is important for the plasma membrane localization of the non-secreted plant peptide ROT4.The upregulation of plant immune genes mediated by ROT4 requires its S-acylation.S-acylation of ROT4 increases its association with BSK5 for activation of plant elicitor peptide signaling.S-acylation is necessary for the function of ROT4 in plant immunity and in pathogen resistance. S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. Arabidopsis (dpeaa)DE-He213 Plant Immunity (dpeaa)DE-He213 Protein S-acylation (dpeaa)DE-He213 ROT4 (dpeaa)DE-He213 Small Peptide (dpeaa)DE-He213 Ye, Tushu aut Ye, Weixian aut Liang, Jieyi aut Wang, Wen (orcid)0009-0009-8695-1803 aut Han, Danlu (orcid)0000-0002-9828-371X aut Liu, Xiaoshi (orcid)0000-0002-2851-7330 aut Huang, Liting aut Ouyang, Youwei aut Liao, Jianwei aut Chen, Tongsheng aut Yang, Chengwei (orcid)0000-0002-2648-3181 aut Lai, Jianbin (orcid)0000-0002-9269-9052 aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 25(2024), 2 vom: 02. Jan., Seite 489-505 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:25 year:2024 number:2 day:02 month:01 pages:489-505 https://dx.doi.org/10.1038/s44319-023-00029-x kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_22 GBV_ILN_24 GBV_ILN_62 GBV_ILN_63 GBV_ILN_120 GBV_ILN_150 GBV_ILN_168 GBV_ILN_211 GBV_ILN_252 GBV_ILN_266 GBV_ILN_2005 GBV_ILN_2010 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2037 GBV_ILN_2064 GBV_ILN_2108 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2336 GBV_ILN_2472 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 25 2024 2 02 01 489-505
allfieldsGer	10.1038/s44319-023-00029-x doi (DE-627)SPR054761395 (SPR)s44319-023-00029-x-e DE-627 ger DE-627 rakwb eng Li, Wenliang verfasserin (orcid)0009-0002-5593-5615 aut S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2024 Abstract Small peptides modulate multiple processes in plant cells, but their regulation by post-translational modification remains unclear. ROT4 (ROTUNDIFOLIA4) belongs to a family of Arabidopsis non-secreted small peptides, but knowledge on its molecular function and how it is regulated is limited. Here, we find that ROT4 is S-acylated in plant cells. S-acylation is an important form of protein lipidation, yet so far it has not been reported to regulate small peptides in plants. We show that this modification is essential for the plasma membrane association of ROT4. Overexpression of S-acylated ROT4 results in a dramatic increase in immune gene expression. S-acylation of ROT4 enhances its interaction with BSK5 (BRASSINOSTEROID-SIGNALING KINASE 5) to block the association between BSK5 and PEPR1 (PEP RECEPTOR1), a receptor kinase for secreted plant elicitor peptides (PEPs), thereby activating immune signaling. Phenotype analysis indicates that S-acylation is necessary for ROT4 functions in pathogen resistance, PEP response, and the regulation of development. Collectively, our work reveals an important role for S-acylation in the cross-talk of non-secreted and secreted peptide signaling in plant immunity. Synopsis S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. S-acylation is important for the plasma membrane localization of the non-secreted plant peptide ROT4.The upregulation of plant immune genes mediated by ROT4 requires its S-acylation.S-acylation of ROT4 increases its association with BSK5 for activation of plant elicitor peptide signaling.S-acylation is necessary for the function of ROT4 in plant immunity and in pathogen resistance. S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. Arabidopsis (dpeaa)DE-He213 Plant Immunity (dpeaa)DE-He213 Protein S-acylation (dpeaa)DE-He213 ROT4 (dpeaa)DE-He213 Small Peptide (dpeaa)DE-He213 Ye, Tushu aut Ye, Weixian aut Liang, Jieyi aut Wang, Wen (orcid)0009-0009-8695-1803 aut Han, Danlu (orcid)0000-0002-9828-371X aut Liu, Xiaoshi (orcid)0000-0002-2851-7330 aut Huang, Liting aut Ouyang, Youwei aut Liao, Jianwei aut Chen, Tongsheng aut Yang, Chengwei (orcid)0000-0002-2648-3181 aut Lai, Jianbin (orcid)0000-0002-9269-9052 aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 25(2024), 2 vom: 02. Jan., Seite 489-505 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:25 year:2024 number:2 day:02 month:01 pages:489-505 https://dx.doi.org/10.1038/s44319-023-00029-x kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_22 GBV_ILN_24 GBV_ILN_62 GBV_ILN_63 GBV_ILN_120 GBV_ILN_150 GBV_ILN_168 GBV_ILN_211 GBV_ILN_252 GBV_ILN_266 GBV_ILN_2005 GBV_ILN_2010 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2037 GBV_ILN_2064 GBV_ILN_2108 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2336 GBV_ILN_2472 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 25 2024 2 02 01 489-505
allfieldsSound	10.1038/s44319-023-00029-x doi (DE-627)SPR054761395 (SPR)s44319-023-00029-x-e DE-627 ger DE-627 rakwb eng Li, Wenliang verfasserin (orcid)0009-0002-5593-5615 aut S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation 2024 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2024 Abstract Small peptides modulate multiple processes in plant cells, but their regulation by post-translational modification remains unclear. ROT4 (ROTUNDIFOLIA4) belongs to a family of Arabidopsis non-secreted small peptides, but knowledge on its molecular function and how it is regulated is limited. Here, we find that ROT4 is S-acylated in plant cells. S-acylation is an important form of protein lipidation, yet so far it has not been reported to regulate small peptides in plants. We show that this modification is essential for the plasma membrane association of ROT4. Overexpression of S-acylated ROT4 results in a dramatic increase in immune gene expression. S-acylation of ROT4 enhances its interaction with BSK5 (BRASSINOSTEROID-SIGNALING KINASE 5) to block the association between BSK5 and PEPR1 (PEP RECEPTOR1), a receptor kinase for secreted plant elicitor peptides (PEPs), thereby activating immune signaling. Phenotype analysis indicates that S-acylation is necessary for ROT4 functions in pathogen resistance, PEP response, and the regulation of development. Collectively, our work reveals an important role for S-acylation in the cross-talk of non-secreted and secreted peptide signaling in plant immunity. Synopsis S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. S-acylation is important for the plasma membrane localization of the non-secreted plant peptide ROT4.The upregulation of plant immune genes mediated by ROT4 requires its S-acylation.S-acylation of ROT4 increases its association with BSK5 for activation of plant elicitor peptide signaling.S-acylation is necessary for the function of ROT4 in plant immunity and in pathogen resistance. S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. Arabidopsis (dpeaa)DE-He213 Plant Immunity (dpeaa)DE-He213 Protein S-acylation (dpeaa)DE-He213 ROT4 (dpeaa)DE-He213 Small Peptide (dpeaa)DE-He213 Ye, Tushu aut Ye, Weixian aut Liang, Jieyi aut Wang, Wen (orcid)0009-0009-8695-1803 aut Han, Danlu (orcid)0000-0002-9828-371X aut Liu, Xiaoshi (orcid)0000-0002-2851-7330 aut Huang, Liting aut Ouyang, Youwei aut Liao, Jianwei aut Chen, Tongsheng aut Yang, Chengwei (orcid)0000-0002-2648-3181 aut Lai, Jianbin (orcid)0000-0002-9269-9052 aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 25(2024), 2 vom: 02. Jan., Seite 489-505 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:25 year:2024 number:2 day:02 month:01 pages:489-505 https://dx.doi.org/10.1038/s44319-023-00029-x kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_22 GBV_ILN_24 GBV_ILN_62 GBV_ILN_63 GBV_ILN_120 GBV_ILN_150 GBV_ILN_168 GBV_ILN_211 GBV_ILN_252 GBV_ILN_266 GBV_ILN_2005 GBV_ILN_2010 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2037 GBV_ILN_2064 GBV_ILN_2108 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2336 GBV_ILN_2472 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 25 2024 2 02 01 489-505
language	English
source	Enthalten in EMBO Reports 25(2024), 2 vom: 02. Jan., Seite 489-505 volume:25 year:2024 number:2 day:02 month:01 pages:489-505
sourceStr	Enthalten in EMBO Reports 25(2024), 2 vom: 02. Jan., Seite 489-505 volume:25 year:2024 number:2 day:02 month:01 pages:489-505
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Arabidopsis Plant Immunity Protein S-acylation ROT4 Small Peptide
isfreeaccess_bool	true
container_title	EMBO Reports
authorswithroles_txt_mv	Li, Wenliang @@aut@@ Ye, Tushu @@aut@@ Ye, Weixian @@aut@@ Liang, Jieyi @@aut@@ Wang, Wen @@aut@@ Han, Danlu @@aut@@ Liu, Xiaoshi @@aut@@ Huang, Liting @@aut@@ Ouyang, Youwei @@aut@@ Liao, Jianwei @@aut@@ Chen, Tongsheng @@aut@@ Yang, Chengwei @@aut@@ Lai, Jianbin @@aut@@
publishDateDaySort_date	2024-01-02T00:00:00Z
hierarchy_top_id	320645622
id	SPR054761395
language_de	englisch
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author	Li, Wenliang
spellingShingle	Li, Wenliang misc Arabidopsis misc Plant Immunity misc Protein S-acylation misc ROT4 misc Small Peptide S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation
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topic_title	S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation Arabidopsis (dpeaa)DE-He213 Plant Immunity (dpeaa)DE-He213 Protein S-acylation (dpeaa)DE-He213 ROT4 (dpeaa)DE-He213 Small Peptide (dpeaa)DE-He213
topic	misc Arabidopsis misc Plant Immunity misc Protein S-acylation misc ROT4 misc Small Peptide
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title	S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation
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title_full	S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation
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author_browse	Li, Wenliang Ye, Tushu Ye, Weixian Liang, Jieyi Wang, Wen Han, Danlu Liu, Xiaoshi Huang, Liting Ouyang, Youwei Liao, Jianwei Chen, Tongsheng Yang, Chengwei Lai, Jianbin
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doi_str_mv	10.1038/s44319-023-00029-x
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title_sort	s-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation
title_auth	S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation
abstract	Abstract Small peptides modulate multiple processes in plant cells, but their regulation by post-translational modification remains unclear. ROT4 (ROTUNDIFOLIA4) belongs to a family of Arabidopsis non-secreted small peptides, but knowledge on its molecular function and how it is regulated is limited. Here, we find that ROT4 is S-acylated in plant cells. S-acylation is an important form of protein lipidation, yet so far it has not been reported to regulate small peptides in plants. We show that this modification is essential for the plasma membrane association of ROT4. Overexpression of S-acylated ROT4 results in a dramatic increase in immune gene expression. S-acylation of ROT4 enhances its interaction with BSK5 (BRASSINOSTEROID-SIGNALING KINASE 5) to block the association between BSK5 and PEPR1 (PEP RECEPTOR1), a receptor kinase for secreted plant elicitor peptides (PEPs), thereby activating immune signaling. Phenotype analysis indicates that S-acylation is necessary for ROT4 functions in pathogen resistance, PEP response, and the regulation of development. Collectively, our work reveals an important role for S-acylation in the cross-talk of non-secreted and secreted peptide signaling in plant immunity. Synopsis S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. S-acylation is important for the plasma membrane localization of the non-secreted plant peptide ROT4.The upregulation of plant immune genes mediated by ROT4 requires its S-acylation.S-acylation of ROT4 increases its association with BSK5 for activation of plant elicitor peptide signaling.S-acylation is necessary for the function of ROT4 in plant immunity and in pathogen resistance. S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. © The Author(s) 2024
abstractGer	Abstract Small peptides modulate multiple processes in plant cells, but their regulation by post-translational modification remains unclear. ROT4 (ROTUNDIFOLIA4) belongs to a family of Arabidopsis non-secreted small peptides, but knowledge on its molecular function and how it is regulated is limited. Here, we find that ROT4 is S-acylated in plant cells. S-acylation is an important form of protein lipidation, yet so far it has not been reported to regulate small peptides in plants. We show that this modification is essential for the plasma membrane association of ROT4. Overexpression of S-acylated ROT4 results in a dramatic increase in immune gene expression. S-acylation of ROT4 enhances its interaction with BSK5 (BRASSINOSTEROID-SIGNALING KINASE 5) to block the association between BSK5 and PEPR1 (PEP RECEPTOR1), a receptor kinase for secreted plant elicitor peptides (PEPs), thereby activating immune signaling. Phenotype analysis indicates that S-acylation is necessary for ROT4 functions in pathogen resistance, PEP response, and the regulation of development. Collectively, our work reveals an important role for S-acylation in the cross-talk of non-secreted and secreted peptide signaling in plant immunity. Synopsis S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. S-acylation is important for the plasma membrane localization of the non-secreted plant peptide ROT4.The upregulation of plant immune genes mediated by ROT4 requires its S-acylation.S-acylation of ROT4 increases its association with BSK5 for activation of plant elicitor peptide signaling.S-acylation is necessary for the function of ROT4 in plant immunity and in pathogen resistance. S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. © The Author(s) 2024
abstract_unstemmed	Abstract Small peptides modulate multiple processes in plant cells, but their regulation by post-translational modification remains unclear. ROT4 (ROTUNDIFOLIA4) belongs to a family of Arabidopsis non-secreted small peptides, but knowledge on its molecular function and how it is regulated is limited. Here, we find that ROT4 is S-acylated in plant cells. S-acylation is an important form of protein lipidation, yet so far it has not been reported to regulate small peptides in plants. We show that this modification is essential for the plasma membrane association of ROT4. Overexpression of S-acylated ROT4 results in a dramatic increase in immune gene expression. S-acylation of ROT4 enhances its interaction with BSK5 (BRASSINOSTEROID-SIGNALING KINASE 5) to block the association between BSK5 and PEPR1 (PEP RECEPTOR1), a receptor kinase for secreted plant elicitor peptides (PEPs), thereby activating immune signaling. Phenotype analysis indicates that S-acylation is necessary for ROT4 functions in pathogen resistance, PEP response, and the regulation of development. Collectively, our work reveals an important role for S-acylation in the cross-talk of non-secreted and secreted peptide signaling in plant immunity. Synopsis S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. S-acylation is important for the plasma membrane localization of the non-secreted plant peptide ROT4.The upregulation of plant immune genes mediated by ROT4 requires its S-acylation.S-acylation of ROT4 increases its association with BSK5 for activation of plant elicitor peptide signaling.S-acylation is necessary for the function of ROT4 in plant immunity and in pathogen resistance. S-acylation of the non-secreted peptide ROT4 is essential for its membrane localization and function in plant cells. S-acylation of ROT4 enhances its association with BSK5 to activate immune signaling mediated by plant elicitor peptides. © The Author(s) 2024
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_22 GBV_ILN_24 GBV_ILN_62 GBV_ILN_63 GBV_ILN_120 GBV_ILN_150 GBV_ILN_168 GBV_ILN_211 GBV_ILN_252 GBV_ILN_266 GBV_ILN_2005 GBV_ILN_2010 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2037 GBV_ILN_2064 GBV_ILN_2108 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2336 GBV_ILN_2472 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
container_issue	2
title_short	S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation
url	https://dx.doi.org/10.1038/s44319-023-00029-x
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author2	Ye, Tushu Ye, Weixian Liang, Jieyi Wang, Wen Han, Danlu Liu, Xiaoshi Huang, Liting Ouyang, Youwei Liao, Jianwei Chen, Tongsheng Yang, Chengwei Lai, Jianbin
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S-acylation of a non-secreted peptide controls plant immunity via secreted-peptide signal activation

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