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First published online September 19, 2007
doi: 10.1242/10.1242/jcs.014191
Research Article |
1 Division of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands
2 Department of Cell Biology and Physiology, Washington University School of Medicine, St Louis, MO 63110, USA
* Author for correspondence (e-mail: a.sonnenberg{at}nki.nl)
Accepted 30 July 2007
The outer nuclear membrane proteins nesprin-1 and nesprin-2 are retained at the nuclear envelope through an interaction of their klarsicht/ANC-1/syne homology (KASH) domain with Sun proteins present at the inner nuclear membrane. We investigated the requirements for the localization of nesprin-3
at the outer nuclear membrane and show that the mechanism by which its localization is mediated is similar to that reported for the localization of nesprin-1 and nesprin-2: the last four amino acids of the nesprin-3 KASH domain are essential for its interaction with Sun1 and Sun2. Moreover, deletion of these amino acids or knockdown of the Sun proteins results in a redistribution of nesprin-3 away from the nuclear envelope and into the endoplasmic reticulum (ER), where it becomes colocalized with the cytoskeletal crosslinker protein plectin. Both nesprin-3 and plectin can form dimers, and dimerization of plectin is required for its interaction with nesprin-3 at the nuclear envelope, which is mediated by its N-terminal actin-binding domain. Additionally, overexpression of the plectin actin-binding domain stabilizes the actin cytoskeleton and prevents the recruitment of endogenous plectin to the nuclear envelope. Our studies support a model in which the actin cytoskeleton influences the binding of plectin dimers to dimers of nesprin-3, which in turn are retained at the nuclear envelope through an interaction with Sun proteins.
Key words: Nuclear envelope, Nesprin, Sun, Plectin, Intermediate filaments
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