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本文引用的文献

1
LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins.LINC 复合物通过三个 KASH 肽与三聚体 SUN 蛋白的结构域界面结合形成。
Cell. 2012 May 25;149(5):1035-47. doi: 10.1016/j.cell.2012.03.046.
2
Nuclear envelope budding enables large ribonucleoprotein particle export during synaptic Wnt signaling.核膜出芽使大核糖核蛋白颗粒在突触 Wnt 信号传导中输出。
Cell. 2012 May 11;149(4):832-46. doi: 10.1016/j.cell.2012.03.032.
3
Accumulation of the inner nuclear envelope protein Sun1 is pathogenic in progeric and dystrophic laminopathies.核内包膜蛋白 Sun1 的积累与早老性和营养不良性层粘连蛋白病的发病机制有关。
Cell. 2012 Apr 27;149(3):565-77. doi: 10.1016/j.cell.2012.01.059.
4
Trafficking to uncharted territory of the nuclear envelope.贩运至核膜的未知领域。
Curr Opin Cell Biol. 2012 Jun;24(3):341-9. doi: 10.1016/j.ceb.2012.01.009. Epub 2012 Feb 10.
5
A functional role for TorsinA in herpes simplex virus 1 nuclear egress.TorsinA 在单纯疱疹病毒 1 核输出中的功能作用。
J Virol. 2011 Oct;85(19):9667-79. doi: 10.1128/JVI.05314-11. Epub 2011 Jul 20.
6
The ESCRT pathway.外体分选复合体(ESCRT)途径。
Dev Cell. 2011 Jul 19;21(1):77-91. doi: 10.1016/j.devcel.2011.05.015.
7
Herpesviruses remodel host membranes for virus egress.疱疹病毒重塑宿主膜以促进病毒出芽。
Nat Rev Microbiol. 2011 May;9(5):382-94. doi: 10.1038/nrmicro2559.
8
Efficient induction of nuclear aggresomes by specific single missense mutations in the DNA-binding domain of a viral AP-1 homolog.特定的单错义突变在病毒 AP-1 同源物的 DNA 结合域中诱导核聚集物的有效诱导。
J Biol Chem. 2011 Mar 18;286(11):9748-62. doi: 10.1074/jbc.M110.198325. Epub 2011 Jan 13.
9
Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms.细胞质和内质网中的蛋白质质量控制:同仇敌忾的兄弟。
Mol Cell. 2010 Oct 22;40(2):238-52. doi: 10.1016/j.molcel.2010.10.001.
10
Membrane budding and scission by the ESCRT machinery: it's all in the neck.通过 ESCRT 机制进行膜出芽和分裂:一切都在颈部。
Nat Rev Mol Cell Biol. 2010 Aug;11(8):556-66. doi: 10.1038/nrm2937. Epub 2010 Jun 30.

细胞蛋白质量控制的替代核转运。

Alternative nuclear transport for cellular protein quality control.

机构信息

Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, P.O. Box 208114, Bass 236A, New Haven, CT 06520-8114, USA.

出版信息

Trends Cell Biol. 2012 Oct;22(10):509-14. doi: 10.1016/j.tcb.2012.07.003. Epub 2012 Jul 31.

DOI:10.1016/j.tcb.2012.07.003
PMID:22858153
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3462225/
Abstract

Herpesvirus capsids traverse the nuclear envelope (NE) by utilizing an unusual export pathway termed nuclear egress. In this process, the viral capsid is delivered into the perinuclear space (PNS), producing a vesicular intermediate after fission. After fusion with the outer nuclear membrane (ONM), the naked capsid is released into the cytosol. A recent study now suggests that this pathway might be an endogenous cellular pathway, co-opted by viruses, that serves to transport cellular cargo exceeding the size limit imposed by the nuclear pore complex (NPC). We propose that one function of this pathway is to transport nuclear protein aggregates to the cytosolic autophagy machinery. Our model has implications for our understanding of laminopathies and related diseases affecting proteins residing at the inner nuclear membrane (INM) and nuclear lamina.

摘要

疱疹病毒衣壳通过利用一种称为核输出的不寻常出口途径穿过核膜(NE)。在这个过程中,病毒衣壳被递送到核周空间(PNS),在分裂后产生囊泡中间体。与外核膜(ONM)融合后,裸露的衣壳被释放到细胞质中。最近的一项研究表明,该途径可能是一种被病毒采用的内源性细胞途径,用于运输超过核孔复合体(NPC)所施加的大小限制的细胞货物。我们提出,该途径的一个功能是将核蛋白聚集体运输到细胞质自噬机制中。我们的模型对于理解影响位于内核膜(INM)和核层的蛋白质的核纤层病和相关疾病具有重要意义。