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Published online August 27, 2007
doi:10.1083/jcb.200704108
The Journal of Cell Biology, Vol. 178, No. 5, 785-798
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Liu et al.
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Article

 Functional association of Sun1 with nuclear pore complexes

Qian Liu1, Nelly Pante2, Tom Misteli3, Mohamed Elsagga1, Melissa Crisp1, Didier Hodzic4, Brian Burke1, and Kyle J. Roux1

1 Department of Anatomy and Cell Biology, University of Florida, Gainesville, FL 32610
2 Department of Zoology, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada
3 National Cancer Institute, National Institutes of Health, Bethesda, MD 20892
4 Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110

Correspondence to Brian Burke: burke{at}ufl.edu

Sun1 and 2 are A-type lamin-binding proteins that, in association with nesprins, form a link between the inner nuclear membranes (INMs) and outer nuclear membranes of mammalian nuclear envelopes. Both immunofluorescence and immunoelectron microscopy reveal that Sun1 but not Sun2 is intimately associated with nuclear pore complexes (NPCs). Topological analyses indicate that Sun1 is a type II integral protein of the INM. Localization of Sun1 to the INM is defined by at least two discrete regions within its nucleoplasmic domain. However, association with NPCs is dependent on the synergy of both nucleoplasmic and lumenal domains. Cells that are either depleted of Sun1 by RNA interference or that overexpress dominant-negative Sun1 fragments exhibit clustering of NPCs. The implication is that Sun1 represents an important determinant of NPC distribution across the nuclear surface.

Abbreviations used in this paper: INM, inner nuclear membrane; LINC, linker of nucleoskeleton and cytoskeleton; MEF, mouse embryonic fibroblast; NE, nuclear envelope; NES, nuclear export sequence; PC, nuclear pore complex; ONM, outer nuclear membrane; PDI, protein disulfide isomerase; PNS, perinuclear space; TM, transmembrane; TX-100, Triton X-100.


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