期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 69, 期 20, 页码 3493-3509出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-012-1034-1
关键词
Actin binding domain; Cytoskeleton; KASH-domain; LINC complex; Nesprin; Nuclear envelope; Nuclear shape; SUN-domain
资金
- Deutsche Forschungsgemeinschaft (DFG) [KA 2778/1-1]
- Wellcome Trust
- Biotechnology and Biological Sciences Research Council [1096654] Funding Source: researchfish
Nesprins-1/-2/-3/-4 are nuclear envelope proteins, which connect nuclei to the cytoskeleton. The largest nesprin-1/-2 isoforms (termed giant) tether F-actin through their N-terminal actin binding domain (ABD). Nesprin-3, however, lacks an ABD and associates instead to plectin, which binds intermediate filaments. Nesprins are integrated into the outer nuclear membrane via their C-terminal KASH-domain. Here, we show that nesprin-1/-2 ABDs physically and functionally interact with nesprin-3. Thus, both ends of nesprin-1/-2 giant are integrated at the nuclear surface: via the C-terminal KASH-domain and the N-terminal ABD-nesprin-3 association. Interestingly, nesprin-2 ABD or KASH-domain overexpression leads to increased nuclear areas. Conversely, nesprin-2 mini (contains the ABD and KASH-domain but lacks the massive nesprin-2 giant rod segment) expression yields smaller nuclei. Nuclear shrinkage is further enhanced upon nesprin-3 co-expression or microfilament depolymerization. Our findings suggest that multivariate intermolecular nesprin interactions with the cytoskeleton form a lattice-like filamentous network covering the outer nuclear membrane, which determines nuclear size.
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