检索结果-南通市图书馆

Structural and biochemical basis of FLS2-mediated signal activation and transduction in rice

Plant Communications 2024年第3期5卷 216-231页

作者： Qiaoqiao Zhao Jinlin Bao Huailong Li Wei Hu Yanqiong Kong Yifeng Zhong Qiang Fu Guolyu Xu Fenmei Liu Xi Jiao Jian Jin Zhenhua Ming State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources College of Life Science and TechnologyGuangxi Key Laboratory for Sugarcane BiologyGuangxi UniversityNanning 530004P.R.China

The receptor-like kinase FLAGELLIN-SENSITIVE 2(FLS2)functions as a bacterialflagellin receptor local-ized on the cell membrane of *** Arabidopsis,the co-receptor BRI1-ASSOCIATED RECEPTOR KI-NASE 1(BAK1)cooperates with FLS2 to detect theflagellin epitopeflg22,resulting in formation of a signaling complex that triggers plant defense ***,the co-receptor responsible for recog-nizing and signaling theflg22 epitope in rice remains to be determined,and the precise structural mecha-nism underlying FLS2-mediated signal activation and transduction has not been *** study pre-sents the structural characterization of a kinase-dead mutant of the intracellular kinase domain of OsFLS2(OsFLS2-KDD1013A)in complex with ATP or ADP,resolved at resolutions of 1.98 A˚and 2.09 A˚,*** analysis revealed that OsFLS2 can adopt an active conformation in the absence of phosphorylation,although it exhibits only weak basal catalytic activity for ***-quent investigations demonstrated that OsSERK2 effectively phosphorylates OsFLS2,which reciprocally phosphorylates OsSERK2,leading to complete activation of OsSERK2 and rapid phosphorylation of the downstream substrate receptor-like cytoplasmic kinases OsRLCK176 and *** mass spectrometry experiments,we successfully identied critical autophosphorylation sites on OsSERK2,as well as sites transphosphorylated by ***,we demonstrated the interaction between OsSERK2 and OsFLS2,which is enhanced in the presence *** evidence suggests that OsRLCK176 and OsRLCK185 may function downstream of the OsFLS2-mediated signaling *** study reveals the molecular mechanism by which OsFLS2 mediates signal transduction pathways in rice and provides a valuable example for understanding RLK-mediated signaling pathways in plants.

关键词： FLS2 active conformation kinase activation transphosphorylation signal transduction

来源：

维普期刊数据库评论

在线全文

维普期刊数据库

学校读者我要写书评

暂无评论

Src Is Dephosphorylated at Tyrosine 530 in Human Colon Carcinomas

引用

Chinese Journal of Cancer Research 2011年第3期23卷 229-231页

作者： Jeffrey D Bjorge Donald J Fujita Department of Biochemistry and Molecular Biology and Southern Alberta Cancer Research InstituteUniversity of Calgary

Objective：Src is a protein tyrosine kinase that plays important roles in cancer development,and Src kinase activity has been found to be elevated in several types of ***,the cause of the elevation of Src kinase activity in the majority of human colon carcinomas is still largely *** aim at finding the cause of elevated Src kinase activity in human colon ***：We employed normal colon epithelial FHC cells and examined Src activation in human colon carcinoma specimens from 8 *** expression levels were determined by Western blotting,and the activity of Src kinase by kinase ***：Actin levels were different between tumor and normal tissues,demonstrating the complexities and inhomogeneities of the tissue *** kinase activities were increased in the majority of the colon carcinomas as compared with normal colon epithelial cells （range 13-29）.Src protein levels were reduced in the colon *** Y530 phosphorylation levels were reduced to a higher extent than protein levels in the ***：The results suggest that Src specific activities were highly increased in human colon carcinomas;phosphorylation at Src Y530 was reduced,contributing to the highly elevated Src specific activity and Src kinase activity.

关键词： Src kinase activation Dephosphorylation Colon carcinoma

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

欢迎您,

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

请选择保存的检索档案：

请选择收藏分类：

通借通还

欢迎您,

建议与咨询 留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

请选择保存的检索档案： 新增检索档案 确定 取消

请选择收藏分类： 新增自定义分类 确定 取消

通借通还

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

请选择保存的检索档案：

请选择收藏分类：