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FEBS Lett. 2015 Sep 14;589(19 Pt A):2514-21. doi: 10.1016/j.febslet.2015.06.011. Epub 2015 Jun 19.

LINC'ing form and function at the nuclear envelope.

Author information

1
Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, UK. Electronic address: pmeinke@staffmail.ed.ac.uk.
2
Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.

Abstract

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.

KEYWORDS:

LINC complex; Nesprin protein; Nuclear envelope; Nuclear envelope transmembrane protein; SUN protein

PMID:
26096784
DOI:
10.1016/j.febslet.2015.06.011
[Indexed for MEDLINE]
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