Redox-Mediated Endocytosis of a Receptor-Like Kinase during Distal Stem Cell Differentiation Depends on Its Tumor Necrosis Factor Receptor Domain
Redox-Mediated Endocytosis of a Receptor-Like Kinase during Distal Stem Cell Differentiation Depends on Its Tumor Necrosis Factor Receptor Domain
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DOI：
10.1104/pp.19.00616
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发表时间：
2019-11-01
期刊：
影响因子：
7.4
通讯作者：
Gong，Zhizhong
中科院分区：
文献类型：
--
作者：
Qin，Yingying;Yang，Li;Gong，Zhizhong
细胞的氧化还原状态在细胞分裂和分化中起着关键作用，但其内在机制尚不清楚。在这里，我们探讨了氧化还原状态对拟南芥（拟南芥）根的远端干细胞（DSC）的干细胞身份的影响。用还原剂谷胱甘肽和氧化剂H2 O2处理抑制DSC分化，通过各种突变内源性改变活性氧的产生。这表明高度还原和氧化环境都抑制干细胞身份的特化。在我们对CLAVATA 3/胚乳包围区40（CLE 40）-拟南芥CRINKLY 4（ACR 4）/CLAVATA 1（CLV 1）-WUSCHEL相关同源框5（WOX 5）模块的突变体组分的观察中，还原剂和氧化剂都影响wox 5 - 1和clv 1 -1的DSC分化，但不影响inacr 4 - 2或CLE 40突变体植物。受体样激酶ACR 4的稳定性通过根尖中的内吞作用由氧化还原状态调节。在肿瘤坏死因子受体（TNFR）胞外结构域中具有多个Cys突变的ACR 4未能进行内吞作用。具有TNFR结构域的完全缺失的ACR 4直接定位于内体，绕过质膜。这两个突变影响DSC分化，但不影响种子灌浆。相反，ACR 4蛋白的细胞内结构域是种子灌浆所需的部分结构域，但不是DSC分化所需的。我们的研究揭示了一个重要的生物学作用的TNFR结构域在氧化还原介导的内吞作用的ACR 4根DSC分化。
Cellular redox status plays critical roles in cell division and differentiation, but the underlying mechanism is unclear. Here we explored the effect of redox status on stem cell identity in distal stem cells (DSCs) of Arabidopsis (Arabidopsis thaliana) roots. Treatment with the reductive reagent glutathione and the oxidative reagent H2O2inhibited DSC differentiation, as did endogenously altering reactive oxygen species production via various mutations. This suggests that both highly reductive and oxidative environments inhibit specification of stem cell identity. In our observations of mutant components of the CLAVATA3/ENDOSPERM SURROUNDING REGION 40 (CLE40)-ARABIDOPSIS CRINKLY4 (ACR4)/CLAVATA1 (CLV1)-WUSCHEL RELATED HOMEOBOX5 (WOX5) module, both reductive and oxidative reagents influenced DSC differentiation inwox5-1andclv1-1, but not inacr4-2orcle40mutant plants. The stability of the receptor-like kinase ACR4 is modulated by redox status through endocytosis in root tips. ACR4 with multiple Cys mutations in the tumor necrosis factor receptor (TNFR) extracellular domain failed to undergo endocytosis. ACR4 with a complete deletion of the TNFR domain was localized directly to endosomes, bypassing the plasma membrane. Both mutations affected DSC differentiation, but not seed filling. Conversely, the intracellular domain of the ACR4 protein is partially required for seed filling, but not for DSC differentiation. Our study uncovers an important biological role of the TNFR domain in redox-mediated endocytosis of ACR4 in root DSC differentiation.