The glycogen synthase kinase MoGsk1, regulated by Mps1 MAP kinase, is required for fungal development and pathogenicity in Magnaporthe oryzae

Abstract Magnaporthe oryzae, the causal agent of blast disease, is one of the most destructive plant pathogens, causing significant yield losses on staple crops such as rice and wheat. The fungus infects plants with a specialized cell called an appressorium, whose development is tightly regulated by...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Tengsheng Zhou, Yasin F. Dagdas, Xiaohan Zhu, Shiqin Zheng, Liqiong Chen, Zachary Cartwright, Nicholas J. Talbot, Zonghua Wang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5bb2f1d26bf248eebebda73de967720b
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:5bb2f1d26bf248eebebda73de967720b
record_format	dspace
spelling	oai:doaj.org-article:5bb2f1d26bf248eebebda73de967720b2021-12-02T16:07:00ZThe glycogen synthase kinase MoGsk1, regulated by Mps1 MAP kinase, is required for fungal development and pathogenicity in Magnaporthe oryzae10.1038/s41598-017-01006-w2045-2322https://doaj.org/article/5bb2f1d26bf248eebebda73de967720b2017-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01006-whttps://doaj.org/toc/2045-2322Abstract Magnaporthe oryzae, the causal agent of blast disease, is one of the most destructive plant pathogens, causing significant yield losses on staple crops such as rice and wheat. The fungus infects plants with a specialized cell called an appressorium, whose development is tightly regulated by MAPK signaling pathways following the activation of upstream sensors in response to environmental stimuli. Here, we show the expression of the Glycogen synthase kinase 3 (GSK3) MoGSK1 in M. oryzae is regulated by Mps1 MAP kinase, particularly under the stressed conditions. Thus, MoGSK1 is functionally characterized in this study. MoGsk1 is functionally homologues to the Saccharomyces cerevisiae GSK3 homolog MCK1. Gene replacement of MoGSK1 caused significant delay in mycelial growth, complete loss of conidiation and inability to penetrate the host surface by mycelia-formed appressorium-like structures, consequently resulting in loss of pathogenicity. However, the developmental and pathogenic defects of Δmogsk1 are recovered via the heterologous expression of Fusarium graminearum GSK3 homolog gene FGK3, whose coding products also shows the similar cytoplasmic localization as MoGsk1 does in M. oryzae. By contrast, overexpression of MoGSK1 produced deformed appressoria in M. oryzae. In summary, our results suggest that MoGsk1, as a highly conservative signal modulator, dictates growth, conidiation and pathogenicity of M. oryzae.Tengsheng ZhouYasin F. DagdasXiaohan ZhuShiqin ZhengLiqiong ChenZachary CartwrightNicholas J. TalbotZonghua WangNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Tengsheng Zhou Yasin F. Dagdas Xiaohan Zhu Shiqin Zheng Liqiong Chen Zachary Cartwright Nicholas J. Talbot Zonghua Wang The glycogen synthase kinase MoGsk1, regulated by Mps1 MAP kinase, is required for fungal development and pathogenicity in Magnaporthe oryzae
description	Abstract Magnaporthe oryzae, the causal agent of blast disease, is one of the most destructive plant pathogens, causing significant yield losses on staple crops such as rice and wheat. The fungus infects plants with a specialized cell called an appressorium, whose development is tightly regulated by MAPK signaling pathways following the activation of upstream sensors in response to environmental stimuli. Here, we show the expression of the Glycogen synthase kinase 3 (GSK3) MoGSK1 in M. oryzae is regulated by Mps1 MAP kinase, particularly under the stressed conditions. Thus, MoGSK1 is functionally characterized in this study. MoGsk1 is functionally homologues to the Saccharomyces cerevisiae GSK3 homolog MCK1. Gene replacement of MoGSK1 caused significant delay in mycelial growth, complete loss of conidiation and inability to penetrate the host surface by mycelia-formed appressorium-like structures, consequently resulting in loss of pathogenicity. However, the developmental and pathogenic defects of Δmogsk1 are recovered via the heterologous expression of Fusarium graminearum GSK3 homolog gene FGK3, whose coding products also shows the similar cytoplasmic localization as MoGsk1 does in M. oryzae. By contrast, overexpression of MoGSK1 produced deformed appressoria in M. oryzae. In summary, our results suggest that MoGsk1, as a highly conservative signal modulator, dictates growth, conidiation and pathogenicity of M. oryzae.
format	article
author	Tengsheng Zhou Yasin F. Dagdas Xiaohan Zhu Shiqin Zheng Liqiong Chen Zachary Cartwright Nicholas J. Talbot Zonghua Wang
author_facet	Tengsheng Zhou Yasin F. Dagdas Xiaohan Zhu Shiqin Zheng Liqiong Chen Zachary Cartwright Nicholas J. Talbot Zonghua Wang
author_sort	Tengsheng Zhou
title	The glycogen synthase kinase MoGsk1, regulated by Mps1 MAP kinase, is required for fungal development and pathogenicity in Magnaporthe oryzae
title_short	The glycogen synthase kinase MoGsk1, regulated by Mps1 MAP kinase, is required for fungal development and pathogenicity in Magnaporthe oryzae
title_full	The glycogen synthase kinase MoGsk1, regulated by Mps1 MAP kinase, is required for fungal development and pathogenicity in Magnaporthe oryzae
title_fullStr	The glycogen synthase kinase MoGsk1, regulated by Mps1 MAP kinase, is required for fungal development and pathogenicity in Magnaporthe oryzae
title_full_unstemmed	The glycogen synthase kinase MoGsk1, regulated by Mps1 MAP kinase, is required for fungal development and pathogenicity in Magnaporthe oryzae
title_sort	glycogen synthase kinase mogsk1, regulated by mps1 map kinase, is required for fungal development and pathogenicity in magnaporthe oryzae
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/5bb2f1d26bf248eebebda73de967720b
work_keys_str_mv	AT tengshengzhou theglycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT yasinfdagdas theglycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT xiaohanzhu theglycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT shiqinzheng theglycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT liqiongchen theglycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT zacharycartwright theglycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT nicholasjtalbot theglycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT zonghuawang theglycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT tengshengzhou glycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT yasinfdagdas glycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT xiaohanzhu glycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT shiqinzheng glycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT liqiongchen glycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT zacharycartwright glycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT nicholasjtalbot glycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae AT zonghuawang glycogensynthasekinasemogsk1regulatedbymps1mapkinaseisrequiredforfungaldevelopmentandpathogenicityinmagnaportheoryzae
_version_	1718384776995405824

The glycogen synthase kinase MoGsk1, regulated by Mps1 MAP kinase, is required for fungal development and pathogenicity in Magnaporthe oryzae

Ejemplares similares