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SPIKE1 Signals Originate from and Assemble Specialized Domains of the Endoplasmic Reticulum

机译：SPIKE1信号源自内质网的特定域并组装在内

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In the leaf epidermis, intricately lobed pavement cells use Rho of plants (ROP) small GTPases to integrate actin and microtubule organization with trafficking through the secretory pathway [1-5]. Cell signaling occurs because guanine nucleotide exchange factors (GEFs) promote ROP activation and their interactions with effector proteins that direct the cell growth machineries [6]. In Arabidopsis, SPIKE1 (SPK1) is the lone DOCK family GEF [7, 8]. SPK1 promotes polarized growth and cell-cell adhesion in the leaf epidermis; however, its mode of action in cells is not known. Vertebrate DOCK proteins are deployed at the plasma membrane [9, 10]. Likewise, current models place SPK1 activity and/or active ROP at the plant plasma membrane and invoke the localized patterning of the cortical cytoskeleton as the mechanism for shape control [1, 4, 6, 11]. In this paper, we find that SPK1 is a peripheral membrane protein that accumulates at, and promotes the formation of, a specialized domain of the endoplasmic reticulum (ER) termed the ER exit site (ERES). SPK1 signals are generated from a distributed network of ERES point sources and maintain the homeostasis of the early secretory pathway. The ERES is the location for cargo export from the ER [12]. Our findings open up unexpected areas of plant G protein biology and redefine the ERES as a subcellular location for signal integration during morphogenesis.
机译：在叶表皮中，复杂的叶状路面细胞利用植物的Rho（ROP）小GTP酶将肌动蛋白和微管组织整合在一起，并通过分泌途径进行转运[1-5]。发生细胞信号传导是因为鸟嘌呤核苷酸交换因子（GEF）促进ROP活化及其与指导细胞生长机制的效应蛋白的相互作用[6]。在拟南芥中，SPIKE1（SPK1）是唯一的DOCK家族GEF [7，8]。 SPK1促进叶片表皮中的极化生长和细胞粘附。然而，其在细胞中的作用方式尚不清楚。脊椎动物DOCK蛋白被部署在质膜上[9，10]。同样，当前的模型将SPK1活性和/或活性ROP置于植物质膜上，并调用皮质细胞骨架的局部模式作为形状控制的机制[1、4、6、11]。在本文中，我们发现SPK1是一种外围膜蛋白，其在称为ER出口位点（ERES）的内质网（ER）的专用域中积累并促进其形成。 SPK1信号从ERES点源的分布式网络生成，并维持早期分泌途径的稳态。 ERES是从ER出口货物的地点[12]。我们的发现打开了植物G蛋白生物学意想不到的领域，并将ERES重新定义为形态发生过程中信号整合的亚细胞位置。

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