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Cytoskeletal interactions at the nuclear envelope mediated by Nesprins

Taranum, S.; Sur, I.; Muller, R.; Lu, W.; Rashmi, R.N.; Munch, M.; Neumann, S.; Karakesisoglou, I.; Noegel, A.A.

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Authors

S. Taranum

I. Sur

R. Muller

W. Lu

R.N. Rashmi

M. Munch

S. Neumann

A.A. Noegel



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.

Citation

Taranum, S., Sur, I., Muller, R., Lu, W., Rashmi, R., Munch, M., …Noegel, A. (2012). Cytoskeletal interactions at the nuclear envelope mediated by Nesprins. International Journal of Cell Biology, 2012, Article 736524. https://doi.org/10.1155/2012/736524

Journal Article Type Article
Publication Date Feb 1, 2012
Deposit Date Apr 24, 2012
Publicly Available Date Jun 6, 2012
Journal International Journal of Cell Biology
Print ISSN 1687-8876
Electronic ISSN 1687-8884
Publisher Hindawi
Peer Reviewed Peer Reviewed
Volume 2012
Article Number 736524
DOI https://doi.org/10.1155/2012/736524

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Copyright 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.







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