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Sun1 forms immobile macromolecular assemblies at the nuclear envelope
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2008 (English)In: Biochimica et Biophysica Acta. Molecular Cell Research, ISSN 0167-4889, Vol. 1783, no 12, 2415-2426 p.Article in journal (Refereed) Published
Abstract [en]

SUN-domain proteins form a novel and conserved family of inner nuclear membrane (INM) proteins, which establish physical connections between the nucleoplasm and the cytoskeleton. In the current study, we provide evidence that within the nuclear envelope (NE) Stint proteins form highly immobile oligomeric complexes in interphase cells. By performing inverse fluorescence recovery after photobleaching analysis, we demonstrate in vivo that both perinuclear and nucleoplasmic Sun I segments are essential for maintenance of Sun I immobility at the NE. Our data in Particular underline the self-association properties of the C-terminal coiled-coil Sun I segment, the ability of which to form dimers and tetramers is demonstrated. Furthermore, the Sun1 tertiary Structure involves interchain disulfide bonds that might contribute to higher homo-oligomer formation, although the overall dynamics of the Sun1 C-terminus remains unaffected when the cysteins involved are mutated. While a major Sun1 pool colocalizes with nuclear pore complex proteins, a large fraction of the Sun1 protein assemblies colocalize with immunoreactive foci of Sun2, another SUN-domain paralogue at the NE. We demonstrate that the Sun1 coiled-coil domain permits these heterophilic associations with Sun2. Sun1 therefore provides a non-dynamic platform for the formation of different macromolecular assemblies at the INM Our data support a model in which SUN-protein-containing multivariate complexes may provide versatile outer nuclear membrane attachment sites for cytoskeletal filaments. Crown

Place, publisher, year, edition, pages
2008. Vol. 1783, no 12, 2415-2426 p.
Keyword [en]
SUN-domain, Sun1, Sun2, Nuclear envelope, Nesprin, KASH-domain, iFRAP, spindle pole body, membrane protein, lamin-a, caenorhabditis-elegans, actin cytoskeleton, domain proteins, pore complexes, fission yeast, living cells, in-vitro
URN: urn:nbn:se:kth:diva-18023DOI: 10.1016/j.bbamcr.2008.09.001ISI: 000261346100021ScopusID: 2-s2.0-55049087455OAI: diva2:336068
QC 20100525Available from: 2010-08-05 Created: 2010-08-05Bibliographically approved

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Uhlén, MathiasAl-Khalili Szigyarto, Cristina
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