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Insights into the complexity and functionality of plant virus protein phosphorylation.
Wu, Yuansheng; Liu, Na; Zheng, Chengxu; Li, Dongyuan; Li, Shanshan; Wu, Jianguo; Zhao, Shanshan.
Affiliation
  • Wu Y; Fuzhou, China; 18314433155@163.com.
  • Liu N; Fuzhou, China; liuna_js@163.com.
  • Zheng C; Fuzhou, China; 1733064195@QQ.com.
  • Li D; Fuzhou, China; ldyljr@163.com.
  • Li S; Fuzhou, China; lishanshangw@163.com.
  • Wu J; Vector-borne Virus Research Center, Fujian Agriculture and Forestry University, Fuzhou, Fujian, China, 350002; wujianguo81@126.com.
  • Zhao S; Fuzhou, China; sszhao88@163.com.
Article in En | MEDLINE | ID: mdl-38814574
ABSTRACT
Phosphorylation, the most extensive and pleiotropic form of protein post-translation modification, is central to cellular signal transduction. Throughout the extensive co-evolution of plant hosts and viruses, modifications to phosphorylation have served multiple purposes. Such modifications highlight the evolutionary trajectories of viruses and their hosts, with pivotal roles in regulation and refinement of host-virus interactions. In plant hosts, protein phosphorylation orchestrates immune responses, enhancing the activities of defense-related proteins such as kinases and transcription factors, thereby strengthening pathogen resistance in plants. Moreover, phosphorylation influences the interactions between host and viral proteins, altering viral spread and replication within host plants. In the context of plant viruses, protein phosphorylation controls key aspects of the infection cycle, including viral protein functionality and the interplay between viruses and host plant cells, leading to effects on viral accumulation and dissemination within plant tissues. Explorations of the nuances of protein phosphorylation in plant hosts and their interactions with viruses are particularly important. This review provides a systematic summary of the biological roles of the proteins of plant viruses carrying diverse genomes in regulating infection and host responses through changes in the phosphorylation status.

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Mol Plant Microbe Interact Journal subject: BIOLOGIA MOLECULAR / BOTANICA / MICROBIOLOGIA Year: 2024 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: Mol Plant Microbe Interact Journal subject: BIOLOGIA MOLECULAR / BOTANICA / MICROBIOLOGIA Year: 2024 Document type: Article
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