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核纤层蛋白、核纤层病及疾病发生机制:蛋白酶体对关键调节蛋白的降解作用可能与之相关。

Lamins, laminopathies and disease mechanisms: possible role for proteasomal degradation of key regulatory proteins.

机构信息

Centre for Cellular and Molecular Biology (CSIR), Hyderabad 500 007, India.

出版信息

J Biosci. 2011 Aug;36(3):471-9. doi: 10.1007/s12038-011-9085-2.

DOI:10.1007/s12038-011-9085-2
PMID:21799258
Abstract

Lamins are major structural proteins of the nucleus and are essential for nuclear integrity and organization of nuclear functions. Mutations in the human lamin genes lead to highly degenerative genetic diseases that affect a number of different tissues such as muscle, adipose or neuronal tissues, or cause premature ageing syndromes. New findings on the role of lamins in cellular signalling pathways, as well as in ubiquitin-mediated proteasomal degradation, have given important insights into possible mechanisms of pathogenesis.

摘要

核纤层蛋白是细胞核的主要结构蛋白,对于核的完整性和核功能的组织至关重要。人类核纤层蛋白基因突变可导致多种组织(如肌肉、脂肪或神经组织)发生退行性遗传疾病,或引起早衰综合征。核纤层蛋白在细胞信号通路以及泛素介导的蛋白酶体降解中的作用的新发现,为发病机制的可能机制提供了重要的见解。

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本文引用的文献

1
Lamin C and chromatin organization in Drosophila.果蝇中的核纤层蛋白C与染色质组织
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2
Lamin A rod domain mutants target heterochromatin protein 1alpha and beta for proteasomal degradation by activation of F-box protein, FBXW10.核纤层蛋白 A 杆状结构域突变体通过激活 F-box 蛋白 FBXW10,将异染色质蛋白 1α 和β靶向到蛋白酶体降解。
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Lamin-binding Proteins.层粘连蛋白结合蛋白。
利用非洲爪蟾无细胞提取物研究亚细胞结构的大小调控。
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Recent advances in understanding nuclear size and shape.核大小与形态认知的最新进展
Nucleus. 2016 Apr 25;7(2):167-86. doi: 10.1080/19491034.2016.1162933. Epub 2016 Mar 10.
5
Sustained accumulation of prelamin A and depletion of lamin A/C both cause oxidative stress and mitochondrial dysfunction but induce different cell fates.前层粘连蛋白A的持续积累和层粘连蛋白A/C的耗竭都会导致氧化应激和线粒体功能障碍,但会诱导不同的细胞命运。
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When lamins go bad: nuclear structure and disease.当核纤层蛋白出现异常:核结构与疾病。
Cell. 2013 Mar 14;152(6):1365-75. doi: 10.1016/j.cell.2013.02.015.
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Breaking down protein degradation mechanisms in cardiac muscle.解析心肌蛋白降解机制。
Trends Mol Med. 2013 Apr;19(4):239-49. doi: 10.1016/j.molmed.2013.01.005. Epub 2013 Feb 27.
8
Lamin A/C haploinsufficiency modulates the differentiation potential of mouse embryonic stem cells.核纤层蛋白 A/C 杂合不足调节小鼠胚胎干细胞的分化潜能。
PLoS One. 2013;8(2):e57891. doi: 10.1371/journal.pone.0057891. Epub 2013 Feb 25.
9
Ubiquitin ligase RNF123 mediates degradation of heterochromatin protein 1α and β in lamin A/C knock-down cells.泛素连接酶 RNF123 介导 lamin A/C 敲低细胞中异染色质蛋白 1α 和 1β 的降解。
PLoS One. 2012;7(10):e47558. doi: 10.1371/journal.pone.0047558. Epub 2012 Oct 15.
10
Lamin misexpression upregulates three distinct ubiquitin ligase systems that degrade ATR kinase in HeLa cells.层粘连蛋白表达上调了三个不同的泛素连接酶系统,导致 HeLa 细胞中的 ATR 激酶降解。
Mol Cell Biochem. 2012 Jun;365(1-2):323-32. doi: 10.1007/s11010-012-1272-4. Epub 2012 Mar 1.
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4
Genome-nuclear lamina interactions and gene regulation.基因组-核层板相互作用与基因调控。
Curr Opin Cell Biol. 2010 Jun;22(3):320-5. doi: 10.1016/j.ceb.2010.04.002. Epub 2010 May 3.
5
An accumulation of non-farnesylated prelamin A causes cardiomyopathy but not progeria.未酰化的前层粘连蛋白 A 的积累会导致心肌病,但不会导致早衰症。
Hum Mol Genet. 2010 Jul 1;19(13):2682-94. doi: 10.1093/hmg/ddq158. Epub 2010 Apr 26.
6
Abnormal development of the cerebral cortex and cerebellum in the setting of lamin B2 deficiency.脑皮质和小脑在核层蛋白 B2 缺乏症的情况下发育异常。
Proc Natl Acad Sci U S A. 2010 Mar 16;107(11):5076-81. doi: 10.1073/pnas.0908790107. Epub 2010 Feb 9.
7
A progeria mutation reveals functions for lamin A in nuclear assembly, architecture, and chromosome organization.早衰症突变揭示了核组装、结构和染色体组织中核纤层蛋白 A 的功能。
Proc Natl Acad Sci U S A. 2009 Dec 8;106(49):20788-93. doi: 10.1073/pnas.0911895106. Epub 2009 Nov 19.
8
Reduced expression of lamin A/C results in modified cell signaling and metabolism coupled with changes in expression of structural proteins. lamin A/C 的表达减少导致细胞信号转导和代谢发生改变,同时结构蛋白的表达也发生变化。
J Proteome Res. 2009 Nov;8(11):5196-211. doi: 10.1021/pr900549a.
9
Novel roles for A-type lamins in telomere biology and the DNA damage response pathway.A型核纤层蛋白在端粒生物学和DNA损伤反应途径中的新作用。
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10
A nuclear-envelope bridge positions nuclei and moves chromosomes.核膜桥定位细胞核并移动染色体。
J Cell Sci. 2009 Mar 1;122(Pt 5):577-86. doi: 10.1242/jcs.037622.