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- 저자 : Gautam Shirsekar (검색결과 2 건)
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Role of Ubiquitination in Plant Innate Immunity and Pathogen Virulence
Gautam Shirsekar,Liangying Dai,Yajun Hu,Xuejun Wang,Lirong Zeng,Guo-Liang Wang 한국식물학회 2010 Journal of Plant Biology Vol.53 No.1
Plant diseases are a major constraint for stable crop production in the world. Plants are constantly threatened by different pathogens and have developed an array of mechanisms to defend themselves. A growing body of evidence indicates that ubiquitination, which is one of the most important cellular processes for protein modification in eukaryotic organisms, is involved in the regulation of host defense signaling. Pathogens also exploit ubiquitination to block or interfere with plant defenses. Recent studies in a few model plants have demonstrated that ubiquitination plays a critical role in plant–pathogen interactions that lead either to plant resistance or to successful pathogen invasion of the plant host. This review discusses recent findings about the functions of ubiquitination in host defense and pathogen invasion.
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The Monocot-Specific Receptor-like Kinase SDS2 Controls Cell Death and Immunity in Rice
Fan, Jiangbo,Bai, Pengfei,Ning, Yuese,Wang, Jiyang,Shi, Xuetao,Xiong, Yehui,Zhang, Kai,He, Feng,Zhang, Chongyang,Wang, Ruyi,Meng, Xiangzong,Zhou, Jinggeng,Wang, Mo,Shirsekar, Gautam,Park, Chan Ho,Bell Elsevier 2018 Cell host & microbe Vol.23 No.4
<P><B>Summary</B></P> <P>Programmed cell death (PCD) plays critical roles in plant immunity but must be regulated to prevent excessive damage. The E3 ubiquitin ligase SPL11 negatively regulates PCD and immunity in plants. We show that <I>S</I>PL11 cell-<I>d</I>eath <I>s</I>uppressor <I>2</I> (SDS2), an S-domain receptor-like kinase, positively regulates PCD and immunity in rice by engaging and regulating SPL11 and related kinases controlling defense responses. An <I>sds2</I> mutant shows reduced immune responses and enhanced susceptibility to the blast fungus <I>Magnaporthe oryzae</I>. Conversely, <I>SDS2</I> over-expression induces constitutive PCD accompanied by elevated immune responses and enhanced resistance to <I>M. oryzae</I>. SDS2 interacts with and phosphorylates SPL11, which in turn ubiquitinates SDS2, leading to its degradation. In addition, SDS2 interacts with related receptor-like cytoplasmic kinases, OsRLCK118/176, that positively regulate immunity by phosphorylating the NADPH oxidase OsRbohB to stimulate ROS production. Thus, a plasma membrane-resident protein complex consisting of SDS2, SPL11, and OsRLCK118/176 controls PCD and immunity in rice.</P> <P><B>Highlights</B></P> <P> <UL> <LI> The RLK SDS2 positively regulates plant cell death and immunity in rice </LI> <LI> SDS2 phosphorylates E3 ligase SPL11, which in turn ubiquitinates SDS2 for degradation </LI> <LI> SDS2 phosphorylates receptor-like cytoplasmic kinases RLCK118 </LI> <LI> RLCK118 interacts with and phosphorylates the NADPH oxidase OsRbohB </LI> </UL> </P> <P><B>Graphical Abstract</B></P> <P>[DISPLAY OMISSION]</P>
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