期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 287, 期 8, 页码 5317-5326出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M111.304543
关键词
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资金
- National Cancer Institute
- Abramson Family Cancer Research Institute at the University of Pennsylvania
- Samuel Oschin Comprehensive Cancer Institute
- Women's Guild Lung Institute of the Cedars-Sinai Medical Center
- National Natural Science Foundation of China [30970566, 10979005]
- National Institutes of Health [GM15847]
- Barnett Institute [992]
The SUN (Sad1-UNC-84 homology) domain is conserved in a number of nuclear envelope proteins involved in nuclear migration, meiotic telomere tethering, and antiviral responses. The LINC (linker of nucleoskeleton and cytoskeleton) complex, formed by the SUN and the nesprin proteins at the nuclear envelope, serves as a mechanical linkage across the nuclear envelope. Here we report the crystal structure of the SUN2 protein SUN domain, which reveals a homotrimer. The SUN domain is sufficient to mediate binding to the KASH (Klarsicht, ANC-1, and Syne homology) domain of nesprin 2, and the regions involved in the interaction have been identified. Binding of the SUN domain to the KASH domain is abolished by deletion of a region important for trimerization or by point mutations associated with nuclear migration failure. We propose a model of the LINC complex, where the SUN and the KASH domains form a higher ordered oligomeric network in the nuclear envelope. These findings provide the structural basis for understanding the function and the regulation of the LINC complex.
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