{"title":"More questions than answers: insights into potential cysteine-rich receptor-like kinases redox signalling in Arabidopsis","authors":"Sergio Martin-Ramirez, Jente Stouthamer, Elwira Smakowska-Luzan","doi":"10.1111/tpj.70176","DOIUrl":null,"url":null,"abstract":"<p>Over the past few decades, significant advancements have been made in understanding how plasma-membrane localised receptor kinases (RKs) detect signals and activate responses to various stimuli. Numerous examples of ligand-induced receptor activation mechanisms and their downstream consequences have been characterised in detail. The crucial role of post-translational modifications (PTMs), such as the phosphorylation of receptor kinases, has been demonstrated concerning different cellular responses. Given the diverse structures and architectures of the extracellular domains (ECDs) of RKs, it is probable that various forms of PTMs also play an essential role in receptor activation, including cysteine oxidative modifications triggered by reactive oxygen species (ROS). The function of cysteine oxidative modifications as functional redox switches that modulate protein structure and function has been extensively studied across various multicellular organisms. Based on biochemical and structural characteristics, the family of cysteine-rich receptor-like kinases (CRK) emerges as excellent candidates for proteins regulated in a redox-dependent manner. This review provides a concise overview of cysteine's biochemical and structural properties in its role as a molecular redox switch. Drawing on the currently available literature, we describe how cysteine-redox signalling is maintained, particularly in plant cells. We further focus on extracellular ROS perception and the role of CRKs as promising candidates for ROS sensors in <i>Arabidopsis thaliana</i>. We discuss the structural and biochemical properties of CRKs, their involvement in plant growth and defence processes, and our perspective on why CRKs could be key components of the ROS sensing machinery or ROS sensors, especially regarding the dimerization abilities of CRKs. Finally, we highlight the current challenges in identifying and quantifying cysteine oxidative modifications and propose methods for detecting ROS-modified cysteines that may be promising for investigating the role of CRKs in extracellular ROS perception and signalling.</p>","PeriodicalId":233,"journal":{"name":"The Plant Journal","volume":"122 2","pages":""},"PeriodicalIF":6.2000,"publicationDate":"2025-04-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/tpj.70176","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Plant Journal","FirstCategoryId":"2","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1111/tpj.70176","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"PLANT SCIENCES","Score":null,"Total":0}
引用次数: 0
Abstract
Over the past few decades, significant advancements have been made in understanding how plasma-membrane localised receptor kinases (RKs) detect signals and activate responses to various stimuli. Numerous examples of ligand-induced receptor activation mechanisms and their downstream consequences have been characterised in detail. The crucial role of post-translational modifications (PTMs), such as the phosphorylation of receptor kinases, has been demonstrated concerning different cellular responses. Given the diverse structures and architectures of the extracellular domains (ECDs) of RKs, it is probable that various forms of PTMs also play an essential role in receptor activation, including cysteine oxidative modifications triggered by reactive oxygen species (ROS). The function of cysteine oxidative modifications as functional redox switches that modulate protein structure and function has been extensively studied across various multicellular organisms. Based on biochemical and structural characteristics, the family of cysteine-rich receptor-like kinases (CRK) emerges as excellent candidates for proteins regulated in a redox-dependent manner. This review provides a concise overview of cysteine's biochemical and structural properties in its role as a molecular redox switch. Drawing on the currently available literature, we describe how cysteine-redox signalling is maintained, particularly in plant cells. We further focus on extracellular ROS perception and the role of CRKs as promising candidates for ROS sensors in Arabidopsis thaliana. We discuss the structural and biochemical properties of CRKs, their involvement in plant growth and defence processes, and our perspective on why CRKs could be key components of the ROS sensing machinery or ROS sensors, especially regarding the dimerization abilities of CRKs. Finally, we highlight the current challenges in identifying and quantifying cysteine oxidative modifications and propose methods for detecting ROS-modified cysteines that may be promising for investigating the role of CRKs in extracellular ROS perception and signalling.
期刊介绍:
Publishing the best original research papers in all key areas of modern plant biology from the world"s leading laboratories, The Plant Journal provides a dynamic forum for this ever growing international research community.
Plant science research is now at the forefront of research in the biological sciences, with breakthroughs in our understanding of fundamental processes in plants matching those in other organisms. The impact of molecular genetics and the availability of model and crop species can be seen in all aspects of plant biology. For publication in The Plant Journal the research must provide a highly significant new contribution to our understanding of plants and be of general interest to the plant science community.