Sec14-nodulin proteins and the patterning of phosphoinositide landmarks for developmental control of membrane morphogenesis.

Sec14-nodulin proteins and the patterning of phosphoinositide landmarks for developmental control of membrane morphogenesis.
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DOI:
10.1091/mbc.e14-10-1475
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发表时间:
2015-05-01
影响因子:
3.3
通讯作者:
Bankaitis VA
Bankaitis VA
中科院分区:
生物学3区
文献类型:
--
作者:
Ghosh R;de Campos MK;Huang J;Huh SK;Orlowski A;Yang Y;Tripathi A;Nile A;Lee HC;Dynowski M;Schäfer H;Róg T;Lete MG;Ahyayauch H;Alonso A;Vattulainen I;Igumenova TI;Schaaf G;Bankaitis VA

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一个Sec 14-Esculin蛋白模型被用来确定Esculin域作为一个新的磷酸肌醇效应模块,在控制磷酸肌醇的横向组织的作用。Sec 14-Esculin蛋白的结构域组织表明了将膜表面的位映射到高清晰度脂质信号屏幕的通用原理。极化膜形态发生是真核细胞的一项基本活动。这个过程对于细胞和组织的生物学是必不可少的,并且其执行需要具有高空间分辨率的功能多样的膜信号传导反应的精致的时间协调。此外,必须存在的机制,以建立和维护这样的组织在面对随机化的力量,将diffuse it. In这里,我们确定保守的AtSfh 1 Sec 14-acetulin蛋白作为一种新的效应的磷酸肌醇信号在极端极化膜生长程序所表现出的拟南芥根毛。这些数据与Sec 14-白藜芦醇蛋白控制植物中极化膜形态发生的磷脂酰肌醇4,5-二磷酸(PtdIns(4,5)P2)地标的侧向组织一致。这种模式化的活动需要PtdIns(4,5)P2的结合和同源寡聚化活动的AtSfh 1蛋白结构域,是一个重要方面的极性信号程序在根毛。最后,这些数据提出了一个一般原则,即磷酸肌醇信号转导景观如何在物理上进行位映射,以便真核细胞能够将膜表面转化为高清晰度的脂质信号转导屏幕。
A Sec14-nodulin protein model is used to identify the nodulin domain as a novel phosphoinositide effector module with a role in controlling lateral organization of phosphoinositide. The domain organization of Sec14-nodulin proteins suggests a versatile principle for the bit mapping of membrane surfaces into high-definition lipid-signaling screens. Polarized membrane morphogenesis is a fundamental activity of eukaryotic cells. This process is essential for the biology of cells and tissues, and its execution demands exquisite temporal coordination of functionally diverse membrane signaling reactions with high spatial resolution. Moreover, mechanisms must exist to establish and preserve such organization in the face of randomizing forces that would diffuse it. Here we identify the conserved AtSfh1 Sec14-nodulin protein as a novel effector of phosphoinositide signaling in the extreme polarized membrane growth program exhibited by growing Arabidopsis root hairs. The data are consistent with Sec14-nodulin proteins controlling the lateral organization of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) landmarks for polarized membrane morphogenesis in plants. This patterning activity requires both the PtdIns(4,5)P2 binding and homo-oligomerization activities of the AtSfh1 nodulin domain and is an essential aspect of the polarity signaling program in root hairs. Finally, the data suggest a general principle for how the phosphoinositide signaling landscape is physically bit mapped so that eukaryotic cells are able to convert a membrane surface into a high-definition lipid-signaling screen.