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Cytoskeletal interactions at the nuclear envelope mediated by Nesprins.

Taranum, S. and Sur, I. and Muller, R. and Lu, W. and Rashmi, R.N. and Munch, M. and Neumann, S. and Karakesisoglou, I. and Noegel, A.A. (2012) 'Cytoskeletal interactions at the nuclear envelope mediated by Nesprins.', International journal of cell biology., 2012 . p. 736524.

Abstract

Nesprin-1 is a giant tail-anchored nuclear envelope protein composed of an N-terminal F-actin binding domain, a long linker region formed by multiple spectrin repeats and a C-terminal transmembrane domain. Based on this structure, it connects the nucleus to the actin cytoskeleton. Earlier reports had shown that Nesprin-1 binds to nuclear envelope proteins emerin and lamin through C-terminal spectrin repeats. These repeats can also self-associate. We focus on the N-terminal Nesprin-1 sequences and show that they interact with Nesprin-3, a further member of the Nesprin family, which connects the nucleus to the intermediate filament network. We show that upon ectopic expression of Nesprin-3 in COS7 cells, which are nearly devoid of Nesprin-3 in vitro, vimentin filaments are recruited to the nucleus and provide evidence for an F-actin interaction of Nesprin-3 in vitro. We propose that Nesprins through interactions amongst themselves and amongst the various Nesprins form a network around the nucleus and connect the nucleus to several cytoskeletal networks of the cell.

Item Type:Article
Full text:PDF - Published Version (2295Kb)
Status:Peer-reviewed
Publisher Web site:http://dx.doi.org/10.1155/2012/736524
Publisher statement:Copyright © 2012 Surayya Taranum et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Record Created:01 Jun 2012 11:50
Last Modified:06 Jun 2012 12:30

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