STING dimerization

Stable Identifier
R-HSA-3134800
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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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
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
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