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Phylogenetic analysis of plant multi-domain SEC14-like phosphatidylinositol transfer proteins and structure-function properties of PATELLIN2.
Plant Molecular Biology ( IF 3.9 ) Pub Date : 2020-09-11 , DOI: 10.1007/s11103-020-01067-y
Karolin Montag 1 , Jannik Hornbergs 1 , Rumen Ivanov 1 , Petra Bauer 1
Affiliation  

Key message

SEC14L-PITPs guide membrane recognition and signaling. An increasingly complex modular structure of SEC14L-PITPs evolved in land plants compared to green algae. SEC14/CRAL-TRIO and GOLD domains govern membrane binding specificity.

Abstract

SEC14-like phosphatidylinositol transfer proteins (SEC14L-PITPs) provide cues for membrane identity by exchanging lipophilic substrates, ultimately governing membrane signaling. Flowering plant SEC14L-PITPs often have modular structure and are associated with cell division, development, and stress responses. Yet, structure–function relationships for biochemical–cellular interactions of SEC14L-PITPs are rather enigmatic. Here, we evaluate the phylogenetic relationships of the SEC14L-PITP superfamily in the green lineage. Compared to green algae, land plants have an extended set of SEC14L-PITPs with increasingly complex modular structure. SEC14-GOLD PITPs, present in land plants but not Chara, diverged to three functional subgroups, represented by the six PATELLIN (PATL) proteins in Arabidopsis. Based on the example of Arabidopsis PATL2, we dissect the functional domains for in vitro binding to phosphoinositides and liposomes and for plant cell membrane association. While the SEC14 domain and its CRAL-TRIO-N-terminal extension serve general membrane attachment of the protein, the C-terminal GOLD domain directs it to the plasma membrane by recognizing specific phosphoinositides. We discuss that the different domains of SEC14L-PITPs integrate developmental and environmental signals to control SEC14L-PITP-mediated membrane identity, important to initiate dynamic membrane events.



中文翻译:

植物多结构域 SEC14 样磷脂酰肌醇转移蛋白的系统发育分析和 PATELLIN2 的结构功能特性。

关键信息

SEC14L-PITPs 指导膜识别和信号传导。与绿藻相比,陆地植物中进化出的 SEC14L-PITP 模块化结构越来越复杂。SEC14/CRAL-TRIO 和 GOLD 结构域控制膜结合特异性。

抽象的

SEC14 样磷脂酰肌醇转移蛋白 (SEC14L-PITP) 通过交换亲脂性底物为膜身份提供线索,最终控制膜信号传导。开花植物 SEC14L-PITPs 通常具有模块化结构,并与细胞分裂、发育和应激反应有关。然而,SEC14L-PITPs 的生化-细胞相互作用的结构-功能关系相当神秘。在这里,我们评估了绿色谱系中 SEC14L-PITP 超家族的系统发育关系。与绿藻相比,陆地植物具有扩展的 SEC14L-PITP 集,其模块化结构越来越复杂。SEC14-GOLD PITPs 存在于陆地植物中,但不存在于 Chara 中,分化为三个功能亚群,以拟南芥中的六种 PATELLIN (PATL) 蛋白为代表。以拟南芥 PATL2 为例,我们剖析了体外与磷酸肌醇和脂质体结合以及植物细胞膜结合的功能域。虽然 SEC14 结构域及其 CRAL-TRIO-N 末端延伸服务于蛋白质的一般膜附着,但 C 末端 GOLD 结构域通过识别特定的磷酸肌醇将其引导至质膜。我们讨论了 SEC14L-PITPs 的不同结构域整合了发育和环境信号来控制 SEC14L-PITP 介导的膜特性,这对于启动动态膜事件很重要。C 末端 GOLD 结构域通过识别特定的磷酸肌醇将其引导至质膜。我们讨论了 SEC14L-PITPs 的不同结构域整合了发育和环境信号来控制 SEC14L-PITP 介导的膜特性,这对于启动动态膜事件很重要。C 末端 GOLD 结构域通过识别特定的磷酸肌醇将其引导至质膜。我们讨论了 SEC14L-PITPs 的不同结构域整合了发育和环境信号来控制 SEC14L-PITP 介导的膜特性,这对于启动动态膜事件很重要。

更新日期:2020-09-11
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