PMID:26688217

Citation	Nie, S, Ke, H, Gao, F, Ren, J, Wang, M, Huo, L, Gong, W and Feng, W (2016) Coiled-Coil Domains of SUN Proteins as Intrinsic Dynamic Regulators. Structure 24:80-91
Abstract	SUN proteins are the core components of LINC complexes that span across the nuclear envelope for nuclear positioning and migration. SUN proteins contain at least one predicted coiled-coil domain preceding the SUN domain. Here, we found that the two coiled-coil domains (CC1 and CC2) of SUN2 exhibit distinct oligomeric states. CC2 is a monomer in solution. The structure of the CC2-SUN monomer revealed that CC2 unexpectedly folds as a three-helix bundle that interacts with the SUN domain and locks it in an inactive conformation. In contrast, CC1 is a trimer. The structure of the CC1 trimer demonstrated that CC1 is an imperfect coiled coil for the trimerization and activation of the SUN domain. Modulations of CC1 and CC2 dictate different oligomeric states of CC1-CC2-SUN, which is essential for LINC complex formation. Thus, the two coiled-coil domains of SUN2 act as the intrinsic dynamic regulators for controlling the SUN domain activity.
Links	PubMed Online version:10.1016/j.str.2015.10.024
Keywords	Amino Acid Sequence; Animals; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Mice; Molecular Dynamics Simulation; Molecular Sequence Data; Protein Binding; Protein Multimerization; Protein Structure, Tertiary; Telomere-Binding Proteins/chemistry; Telomere-Binding Proteins/metabolism
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
MOUSE:SUN2	enables	GO:0042802: identical protein binding	ECO:0000353: physical interaction evidence used in manual assertion	UniProtKB:Q8BJS4-3	F		Seeded From UniProt	complete

References

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