Polarly localized WPR proteins interact with PAN receptors and the actin cytoskeleton during maize stomatal development

Polarly localized WPR proteins interact with PAN receptors and the actin cytoskeleton during maize stomatal development
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玉米气孔发育过程中极性定位的 WPR 蛋白与 PAN 受体和肌动蛋白细胞骨架相互作用

DOI:
10.1093/plcell/koac301
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发表时间:
2022
期刊:
The Plant Cell
影响因子:
--
通讯作者:
Facette, Michelle R.
Facette, Michelle R.
中科院分区:
--
文献类型:
--
作者:
Nan, Qiong;Char, Si Nian;Yang, Bing;Bennett, Eric J.;Yang, Bing;Facette, Michelle R.

文献摘要

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细胞不对称分裂前的极化对正确的细胞分裂、细胞命运和组织构型至关重要。在玉米(Zea Mays)气孔发育过程中,副母细胞(SMC)不对称分裂前的极化是由Brick(BRK)-Pangoss(PAN)-Rho家族GTP酶(ROP)途径控制的。两个催化失活的受体样激酶PAN2和PAN1是正确定位分裂平面所必需的。BRK-PAN-ROP途径中的蛋白质在SMC中是极化的,每个蛋白质的极化依赖于前一个蛋白质。由于这一途径中的大多数已知蛋白质都不存在物理上的相互作用,因此可能参与该途径的相互作用尚不清楚。我们发现在玉米SMC偏振过程中,蓝光下弱的叶绿体运动1(WEB1)/叶绿体运动受损2(PMI2)相关蛋白(WPR)是参与SMC偏振的蛋白。WPR在物理上与PAN受体相互作用,并在SMC中以极性方式积聚。WPR蛋白的极化定位依赖于PAN2,而不是PAN1。CRISPR-Cas9诱导的突变导致SMC分裂平面缺陷,而WPR-RFP的异位表达导致气孔缺陷和肌动蛋白细胞骨架的改变。我们发现某些WPR蛋白通过其N-末端直接与F-肌动蛋白相互作用。我们的数据暗示WPR蛋白可能调节肌动蛋白细丝,为了解它们的分子功能提供了线索。这些结果表明WPR蛋白在细胞极化过程中起着重要作用。
Polarization of cells prior to asymmetric cell division is crucial for correct cell divisions, cell fate, and tissue patterning. In maize (Zea mays) stomatal development, the polarization of subsidiary mother cells (SMCs) prior to asymmetric division is controlled by the BRICK (BRK)–PANGLOSS (PAN)–RHO FAMILY GTPASE (ROP) pathway. Two catalytically inactive receptor-like kinases, PAN2 and PAN1, are required for correct division plane positioning. Proteins in the BRK–PAN–ROP pathway are polarized in SMCs, with the polarization of each protein dependent on the previous one. As most of the known proteins in this pathway do not physically interact, possible interactors that might participate in the pathway are yet to be described. We identified WEAK CHLOROPLAST MOVEMENT UNDER BLUE LIGHT 1 (WEB1)/PLASTID MOVEMENT IMPAIRED 2 (PMI2)-RELATED (WPR) proteins as players during SMC polarization in maize. WPRs physically interact with PAN receptors and polarly accumulate in SMCs. The polarized localization of WPR proteins depends on PAN2 but not PAN1. CRISPR–Cas9-induced mutations result in division plane defects in SMCs, and ectopic expression of WPR-RFP results in stomatal defects and alterations to the actin cytoskeleton. We show that certain WPR proteins directly interact with F-actin through their N-terminus. Our data implicate WPR proteins as potentially regulating actin filaments, providing insight into their molecular function. These results demonstrate that WPR proteins are important for cell polarization.