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The danger of "multi-tasking"

机译：“多任务”的危险

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The nuclear envelope (NE) is a barrier that separates nuclear from cytoplasmic processes. It is composed of an inner and outer nuclear membrane (INM, ONM), separated by the perinuclear space (PNS). The ONM is contiguous with the endoplasmic reticulum (ER), and thus, the lumen of the NE and that of the ER constitute one compartment. The lamin B receptor (LBR) is a NE protein that has a central structural role as a linker of the INM, the lamina and chromatin, and a less well characterized functional role as a sterol reductase. In a recent study, we reported that the forced expression of mutant variants of LBR in some cell types induces a separation of the INM from the outer nuclear envelope concomitantly with a separation of ER membranes, whereas in other cells no separation is observed. In this extra view, we speculate about the mechanism that leads to this fundamental disruption of NE and ER structure. Our observations furthermore raise the question to what extent LBR contributes to the establishment or maintenance of the ER and PNS luminal compartment, and how a single mutant protein can so drastically interfere with its regular organization.
机译：核被膜（NE）是将核与细胞质过程分开的屏障。它由一个内核膜和一个外核膜（INM，ONM）组成，被核周空间（PNS）隔开。 ONM与内质网（ER）相邻，因此，NE的腔和ER的腔构成一个腔室。薄层蛋白B受体（LBR）是一种NE蛋白，具有作为INM，薄层和染色质的连接子的中心结构作用，而作为甾醇还原酶的功能则不太明确。在最近的一项研究中，我们报道了在某些细胞类型中强迫表达LBR突变体会诱导INM从外核被膜中分离，并伴有ER膜的分离，而在其他细胞中则未观察到分离。从这个额外的角度来看，我们推测导致NE和ER结构发生根本性破坏的机制。我们的观察进一步提出了一个问题，即LBR在多大程度上有助于ER和PNS腔室的建立或维持，以及单个突变蛋白如何如此剧烈地干扰其正常组织。

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