Details

Autor(en) / Beteiligte

• Sato, Seiichi
• Li, Kai
• Sakurai, Nozomi
• Hashizume, Mei
• Baidya, Sunanda
• Nonaka, Hirotaka
• Noguchi, Koki
• Ishikawa, Kozo
• Obuse, Chikashi
• Takaoka, Akinori

Titel

Regulation of an adaptor protein STING by Hsp90β to enhance innate immune responses against microbial infections

Ist Teil von

• Cellular immunology, 2020-10, Vol.356, p.104188-104188, Article 104188

Ort / Verlag

Netherlands: Elsevier Inc

Erscheinungsjahr

2020

Quelle

MEDLINE

Beschreibungen/Notizen

• •Hsp90s were identified as novel STING interacting proteins.•STING is a stable protein in immune cells.•Inhibition of Hsp90 resulted in the reduction of STING at protein level and innate responses in immune cells.•Stabilization of STING by Hsp90β enhances innate immune response in immune cells. Stimulator of interferon genes (STING) plays important roles in the DNA-mediated innate immune responses. However, the regulatory mechanism of STING in terms of stabilization is not fully understood. Here, we identified the chaperone protein Hsp90s as novel STING interacting proteins. Treatment with an Hsp90 inhibitor 17-AAG and knockdown of Hsp90β but not Hsp90α reduced STING at protein level, resulted in the suppression of IFN induction in response to stimulation with cGAMP, and infections with HSV-1 and Listeria monocytogenes. Collectively, our results suggest that the control of STING protein by Hsp90β is a critical biological process in the DNA sensing pathways.