cytoskeletal interactions at the nuclear envelope mediated by nesprins

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ID: 164288
2012
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Ranked #48 of 61 articles by views in Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases

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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.
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taranum2012internationalcytoskeletal Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Surayya Taranum;Ilknur Sur;Rolf Müller;Wenshu Lu;R. N. Rashmi;Martina Munck;Sascha Neumann;Iakowos Karakesisoglou;Angelika A. Noegel
Journal Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases
Year 2012
DOI
10.1155/2012/736524
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