Abstract：
: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-3alpha 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-3alpha 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-3alpha away from the nuclear envelope and into the endoplasmic reticulum (ER), where it becomes colocalized with the cytoskeletal crosslinker protein plectin. Both nesprin-3alpha and plectin can form dimers, and dimerization of plectin is required for its interaction with nesprin-3alpha 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-3alpha, which in turn are retained at the nuclear envelope through an interaction with Sun proteins.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Ketema M,Wilhelmsen K,Kuikman I,Janssen H,Hodzic D,Sonnenberg Adoi
10.1242/jcs.014191subject
Has Abstractpub_date
2007-10-01 00:00:00pages
3384-94issue
Pt 19eissn
0021-9533issn
1477-9137pii
120/19/3384journal_volume
120pub_type
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