LINC'ing form and function at the nuclear envelope

被引:49
作者
Meinke, Peter [1 ]
Schirmer, Eric C. [1 ]
机构
[1] Univ Edinburgh, Wellcome Trust Ctr Cell Biol, Kings Bldg,Michael Swann Bldg,Room 5-21, Edinburgh EH9 3BF, Midlothian, Scotland
基金
英国惠康基金;
关键词
LINC complex; Nuclear envelope; SUN protein; Nesprin protein; Nuclear envelope transmembrane protein; DREIFUSS MUSCULAR-DYSTROPHY; A-TYPE; MEMBRANE PROTEIN; INTERMEDIATE-FILAMENTS; EMERIN EXPRESSION; LAMIN PROTEINS; SUN PROTEINS; TAN LINES; IDENTIFICATION; MUTATIONS;
D O I
10.1016/j.febslet.2015.06.011
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The nuclear envelope is an amazing piece of engineering. On one hand it is built like a mediaeval fortress with filament systems reinforcing its membrane walls and its double membrane structure forming a lumen like a castle moat. On the other hand its structure can adapt while maintaining its integrity like a reed bending in a river. Like a fortress it has guarded drawbridges in the nuclear pore complexes, but also has other mechanical means of communication. All this is enabled largely because of the LINC complex, a multi-protein structure that connects the intermediate filament nucleoskeleton across the lumen of the double membrane nuclear envelope to multiple cytoplasmic filament systems that themselves could act simultaneously both like mediaeval buttresses and like lines on a suspension bridge. Although many details of the greater LINC structure remain to be discerned, a number of recent findings are giving clues as to how its structural organization can yield such striking dynamic yet stable properties. Combining double- and triple-helical coiled-coils, intrinsic disorder and order, tissue-specific components, and intermediate filaments enables these unique properties. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:2514 / 2521
页数:8
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