STING dimerization

Stable Identifier
Reaction [binding]
Homo sapiens
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STING dimerization is 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). The de‑ubiquitinating enzyme, severe acute respiratory syndrome coronavirus type 1 (SARS‑CoV-1) 1a‑encoded papain‑like protease (PLPro or nsp3), inhibits the ubiquitination of STING (Chen X et al. 2014).

Literature References
PubMed ID Title Journal Year
22728658 Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system

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

Nat. Struct. Mol. Biol. 2012
22579474 Structural Analysis of the STING Adaptor Protein Reveals a Hydrophobic Dimer Interface and Mode of Cyclic di-GMP Binding

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

Immunity 2012
This event is regulated
Orthologous Events
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