The Golgi complex comprises a connected ribbon of stacked cisternal membranes localized to the perinuclear region in most vertebrate cells. The position and morphology of this organelle depends upon interactions with microtubules and the actin cytoskeleton. In contrast, we know relatively little about the relationship of the Golgi complex with intermediate filaments (IFs). In this study, we show that the Golgi is in close physical proximity to vimentin IFs in cultured mouse and human cells. We also show that the trans-Golgi network coiled-coil protein GORAB can physically associate with vimentin IFs. Loss of vimentin and/or GORAB had a modest effect upon Golgi structure at the steady state. The Golgi underwent more rapid disassembly upon chemical disruption with brefeldin A or nocodazole, and slower reassembly upon drug washout, in vimentin knockout cells. Moreover, loss of vimentin caused reduced Golgi ribbon integrity when cells were cultured on high-stiffness hydrogels, which was exacerbated by loss of GORAB. These results indicate that vimentin IFs contribute to the structural stability of the Golgi complex and suggest a role for GORAB in this process.

中文翻译：

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波形蛋白中间丝为哺乳动物高尔基复合体提供结构稳定性。

高尔基复合体由位于大多数脊椎动物细胞核周区域的堆叠的池膜连接带组成。该细胞器的位置和形态取决于与微管和肌动蛋白细胞骨架的相互作用。相比之下，我们对高尔基复合体与中间丝（IF）的关系知之甚少。在这项研究中，我们表明，在培养的小鼠和人类细胞中，高尔基体与波形蛋白 IF 的物理位置非常接近。我们还表明，跨高尔基体网络卷曲螺旋蛋白 GORAB 可以与波形蛋白 IF 物理结合。波形蛋白和/或 GORAB 的损失对稳定状态下的高尔基体结构影响不大。在波形蛋白敲除细胞中，用布雷菲德菌素 A 或诺考达唑进行化学破坏后，高尔基体会经历更快速的分解，而在药物冲洗后，高尔基体会经历更慢的重新组装。此外，当细胞在高硬度水凝胶上培养时，波形蛋白的缺失会导致高尔基带完整性降低，而GORAB的缺失会加剧这种情况。这些结果表明波形蛋白 IF 有助于高尔基复合体的结构稳定性，并表明 GORAB 在此过程中的作用。