The maize ZmVPS23-like protein relocates the nucleotide-binding leucine-rich repeat protein Rp1-D21 to endosomes and suppresses the defense response
文献类型： 外文期刊
作者： Sun, Yang 1 ; Ma, Shijun 1 ; Liu, Xiangguo 2 ; Wang, Guan-Feng 1 ;
作者机构： 1.Shandong Univ, Sch Life Sci, Key Lab Plant Dev & Environm Adaptat Biol, Minist Educ, Qingdao 266237, Shandong, Peoples R China
2.Jilin Acad Agr Sci, Inst Agr Biotechnol, Changchun 130033, Jilin, Peoples R China
期刊名称：PLANT CELL （ 影响因子：11.6； 五年影响因子：12.9 ）
ISSN： 1040-4651
年卷期： 2023 年
页码：
收录情况： SCI
摘要： Plants often utilize nucleotide-binding leucine-rich repeat (NLR) proteins to perceive pathogen infections and trigger a hypersensitive response (HR). The endosomal sorting complex required for transport (ESCRT) machinery is a conserved multisubunit complex that is essential for the biogenesis of multivesicular bodies and cargo protein sorting. VPS23 is a key component of ESCRT-I and plays important roles in plant development and abiotic stresses. ZmVPS23L, a homolog of VPS23-like in maize (Zea mays), was previously identified as a candidate gene in modulating HR mediated by the autoactive NLR protein Rp1-D21 in different maize populations. Here, we demonstrate that ZmVPS23L suppresses Rp1-D21-mediated HR in maize and Nicotiana benthamiana. Variation in the suppressive effect of HR by different ZmVPS23L alleles was correlated with variation in their expression levels. ZmVPS23 also suppressed Rp1-D21-mediated HR. ZmVPS23L and ZmVPS23 predominantly localized to endosomes, and they physically interacted with the coiled-coil domain of Rp1-D21 and mediated the relocation of Rp1-D21 from the nucleo-cytoplasm to endosomes. In summary, we demonstrate that ZmVPS23L and ZmVPS23 are negative regulators of Rp1-D21-mediated HR, likely by sequestrating Rp1-D21 in endosomes via physical interaction. Our findings reveal the role of ESCRT components in controlling plant NLR-mediated defense responses. Maize ZmVPS23-like, a component of the ESCRT-I complex, interacts with the NLR protein Rp1-D21 and mediates its relocation to endosomes to suppress the defense response.
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