Institute of Botany, Heinrich-Heine University, Düsseldorf 40225, Germany.
Institute of Plant Biology and Biotechnology, University of Münster, Münster 48149, Germany.
Dev Cell. 2019 Mar 11;48(5):726-740.e10. doi: 10.1016/j.devcel.2019.01.006. Epub 2019 Jan 31.
Nutrient acquisition is entangled with growth and stress in sessile organisms. The bHLH transcription factor FIT is a key regulator of Arabidopsis iron (Fe) acquisition and post-translationally activated upon low Fe. We identified CBL-INTERACTING PROTEIN KINASE CIPK11 as a FIT interactor. Cytosolic Ca concentration and CIPK11 expression are induced by Fe deficiency. cipk11 mutant plants display compromised root Fe mobilization and seed Fe content. Fe uptake is dependent on CBL1/CBL9. CIPK11 phosphorylates FIT at Ser272, and mutation of this target site modulates FIT nuclear accumulation, homo-dimerization, interaction with bHLH039, and transcriptional activity and affects the plant's Fe-uptake ability. We propose that Ca-triggered CBL1/9-mediated activation of CIPK11 and subsequent phosphorylation of FIT shifts inactive into active FIT, allowing regulatory protein interactions in the nucleus. This biochemical link between Fe deficiency and the cellular Ca decoding machinery represents an environment-sensing mechanism to adjust nutrient uptake.
养分获取与固着生物的生长和应激交织在一起。bHLH 转录因子 FIT 是拟南芥铁(Fe)获取的关键调节剂,在低铁时被翻译后激活。我们鉴定出 CBL-INTERACTING PROTEIN KINASE CIPK11 是 FIT 的相互作用蛋白。细胞溶质 Ca 浓度和 CIPK11 的表达受 Fe 缺乏诱导。cipk11 突变体植物表现出根铁动员和种子铁含量受损。Fe 摄取依赖于 CBL1/CBL9。CIPK11 在 Ser272 处磷酸化 FIT,并且该靶位点的突变调节 FIT 核积累、同二聚化、与 bHLH039 的相互作用以及转录活性,并影响植物的 Fe 摄取能力。我们提出,Ca 触发的 CBL1/9 介导的 CIPK11 激活以及随后的 FIT 磷酸化将非活性 FIT 转变为活性 FIT,从而允许核内调节蛋白相互作用。这种 Fe 缺乏与细胞内 Ca 解码机制之间的生化联系代表了一种环境感应机制,以调节养分摄取。