STING dimerization

Stable Identifier
Reaction [binding]
Homo sapiens
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Several studies have demonstrated that human STING functions as a dimer and STING dimerization was essential for the induction of IFN response (Sun W et al. 2009; Burdette DL et al. 2011; Jin L et al. 2011; Ouyang S et al. 2012). Mouse Sting/Myps has been also reported to exist as a dimer constitutively [Jin L et al 2008]. Moreover, STING can function as a ROS sensor, which forms a disulfide-linked homodimer under conditions of oxidative stress in HEK293T cells [Jin L et al 2010]. Structural studies revealed that the strictly conserved cytosolic aa 153-173 region of STING participates in dimerization via hydrophobic interactions (Ouyang S et al. 2012).

STING was shown to undergo K63-linked ubiquitination, which may facilitate its dimerization (Tsuchid T et al. 2010; Zhang J et al. 2012)

Literature References
PubMed ID Title Journal Year
22579474 Structural Analysis of the STING Adaptor Protein Reveals a Hydrophobic Dimer Interface and Mode of Cyclic di-GMP Binding

Ouyang, S, Song, X, Wang, Y, Ru, H, Shaw, N, Jiang, Y, Niu, F, Zhu, Y, Qiu, W, Parvatiyar, K, Li, Y, Zhang, R, Cheng, G, Liu, ZJ

Immunity 2012
22728658 Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system

Shu, C, Yi, G, Watts, T, Kao, CC, Li, P

Nat. Struct. Mol. Biol. 2012
Participant Of
Orthologous Events
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