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第一作者:Matouš Glanc
第一单位:奥地利科学技术研究所
通讯作者:Jiří Friml
Abstract
背景回顾:Polar subcellular localization of the PINexporters of the phytohormone auxin is a key determinant of directional, intercellular auxin transport and thus a central topic of both plant cell and developmental biology.
提出问题:Arabidopsis mutants lacking PID, a kinase that phosphorylates PINs, or the MAB4/MELproteins of unknown molecular function display PIN polarity defects and phenocopy pin mutants, but mechanistic insights into how these factors convey PIN polarity are missing.
结果1-互作复合体:Here, by combining protein biochemistry with quantitative live-cell imaging, we demonstrate that PINs, MAB4/MELs, and AGC kinases interact in the same complex at the plasma membrane.
结果2-PIN招募MAB4/MELs:MAB4/MELs are recruited to the plasma membrane by the PINs and in concert with the AGC kinases maintain PIN polarity through limiting lateral diffusion-based escape of PINs from the polar domain.
结果3-正反馈调节:The PIN-MAB4/MEL-PID protein complex has self-reinforcing properties thanks to positive feedback between AGC kinase-mediated PIN phosphorylation and MAB4/MEL recruitment.
结论:We thus uncover the molecular mechanism by which AGC kinases and MAB4/MEL proteins regulate PIN localization and plant development.
摘 要
生长素外运载体PIN蛋白在细胞中的极性定位是决定细胞间方向性生长素流的关键因素,因此在植物细胞和发育生物学领域备受关注。拟南芥中,PID能够磷酸化PINs,而MAB4/MEL蛋白还未知其生物学功能,但是二者的突变体均表现出PIN蛋白的极性定位缺陷,出现类似于pin突变体的表型,但是这两种蛋白具体如何作用于PINs的极性还不清楚。本文中,作者结合了蛋白生物化学和定量活细胞成像,发现PINs、MAB4/MELs和AGC激酶在质膜上的同一个复合体中发生互作。MAB4/MELs被PINs招募到质膜,并在此与AGC激酶一起通过限制PIN在极性域中的侧向扩散,来维持PIN的极性。PIN-MAB4/MEL-PID蛋白复合体具有自我增强的特性,这是由AGC激酶介导的PIN磷酸化和MAB4/MEL招募形成的正向反馈所介导的。因此,本文的研究揭示了一个AGC激酶和MAB4/MEL蛋白作用于PIN蛋白的极性定位, 从而调控植物发育的分子机制。
通讯作者
** Jiří Friml **
个人简介:
1995年,马萨里克大学,化学学士;
1997年,马萨里克大学,生物化学学士;
2000年,科隆大学,生物学博士;
2002年,马萨里克大学,生物化学博士。
研究方向:生长素的极性运输;细胞极性;细胞内吞与再循环;信号转导的非转录机制。
doi: https://doi.org/10.1016/j.cub.2021.02.028
Journal: Current Biology
Published date: Mar 10, 2021
p.s. 往期Jiří Friml通讯研究链接:
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