Phytosulfokine Regulates Growth in Arabidopsis through a Response Module at the Plasma Membrane That Includes CYCLIC NUCLEOTIDE-GATED CHANNEL17, H+-ATPase, and BAK1
Phytosulfokine Regulates Growth in Arabidopsis through a Response Module at the Plasma Membrane That Includes CYCLIC NUCLEOTIDE-GATED CHANNEL17, H+-ATPase, and BAK1
复制标题
DOI：
10.1105/tpc.15.00306
复制
发表时间：
2015-06-01
期刊：
影响因子：
11.6
通讯作者：
Sauter, Margret
中科院分区：
文献类型：
--
作者：
Ladwig, Friederike;Dahlke, Renate I.;Sauter, Margret
植物磺因子（PSK）被富含亮氨酸的重复序列受体激酶PSKR 1感知，并促进拟南芥的生长。PSKR 1与环核苷酸门控通道基因CNGC 17共表达。PSK在野生型中促进原生质体扩增，但在cngc 17中不促进。cGMP也以CNGC 17依赖性方式促进原生质体扩增。此外，PSKR 1缺陷型原生质体不响应PSK而扩增，但仍响应cGMP，表明cGMP在PSKR 1下游起作用。突变PSKR 1鸟苷酸环化酶中心损害幼苗生长，支持PSKR 1通过cGMP在植物中信号传导的作用。虽然PSKR 1不直接与CNGC 17相互作用，但它与质膜定位的H+-ATP酶AHA 1和AHA 2以及BRI相关受体激酶1（BAK 1）相互作用。CNGC 17同样与AHA 1、AHA 2和BAK 1相互作用，表明PSKR 1、BAK 1、CNGC 17和AHA组装成功能复合物。去黄化的bak 1 -3和bak 1 -4幼苗的根对PSK无反应，而bak 1 -3和bak 1 -4原生质体对PSK反应较小，但对cGMP反应完全，表明BAK 1在PSK信号通路中位于cGMP的上游。我们假设CNGC 17和AHAs形成了一个功能性阳离子转运单位，该单位被PSKR 1/BAK 1和可能的其他BAK 1/RLK复合物激活。
Phytosulfokine (PSK) is perceived by the leucine-rich repeat receptor kinase PSKR1 and promotes growth in Arabidopsis thaliana. PSKR1 is coexpressed with the CYCLIC NUCLEOTIDE-GATED CHANNEL gene CNGC17. PSK promotes protoplast expansion in the wild type but not in cngc17. Protoplast expansion is likewise promoted by cGMP in a CNGC17-dependentmanner. Furthermore, PSKR1-deficient protoplasts do not expand in response to PSK but are still responsive to cGMP, suggesting that cGMP acts downstream of PSKR1. Mutating the guanylate cyclase center of PSKR1 impairs seedling growth, supporting a role for PSKR1 signaling via cGMP in planta. While PSKR1 does not interact directly with CNGC17, it interacts with the plasma membrane-localized H+-ATPases AHA1 and AHA2 and with the BRI-associated receptor kinase 1 (BAK1). CNGC17 likewise interacts with AHA1, AHA2, and BAK1, suggesting that PSKR1, BAK1, CNGC17, and AHA assemble in a functional complex. Roots of deetiolated bak1-3 and bak1-4 seedlings were unresponsive to PSK, and bak1-3 and bak1-4 protoplasts expanded less in response to PSK but were fully responsive to cGMP, indicating that BAK1 acts in the PSK signal pathway upstream of cGMP. We hypothesize that CNGC17 and AHAs form a functional cation-translocating unit that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes.