Lug14 promotes NLRP3 inflammasome activation by inhibiting the E3 ligase activity of ARIH2.

<p>A. Lug14-catalyzed ubiquitination inhibits the E3 ligase activity of ARIH2 toward NLRP3. Flag-NLRP3 and Flag-ARIH2 or Flag-ARIH2<sub>K295RK306R</sub> transiently expressed in HEK293T cells were precipitated with beads coated with the Flag antibody. Eluted proteins were used to d...

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التفاصيل البيبلوغرافية
المؤلف الرئيسي:	Shuxin Liu (2792104) (author)
مؤلفون آخرون:	Chunlin He (839438) (author), Yong Zhang (5893) (author), Siyao Liu (1942489) (author), Tao-Tao Chen (22250898) (author), Chunxiuli Li (19645108) (author), Dong Chen (448284) (author), Songying Ouyang (564927) (author), Lei Song (30203) (author), Jiaqi Fu (1525549) (author), Zhao-Qing Luo (227963) (author)
منشور في:	2025
الموضوعات:	Biochemistry Microbiology Cell Biology Evolutionary Biology Ecology Immunology Mental Health Infectious Diseases Virology Environmental Sciences not elsewhere classified Biological Sciences not elsewhere classified virulence factors interfere proximity labeling method one salient feature legionnaires ’ disease artificial water systems e3 ubiquitin ligases e3 ubiquitin ligase subvert host defense host signaling involved utilize catalysis mechanisms lug14 targets arih2 host ubiquitination machinery legionella pneumophila </ least thirteen dot canonical one found host ubiquitin network novel ubiquitin ligase ubiquitin network pneumophila </ host cells distinct mechanisms catalyze ubiquitination lug14 works effector lug14 host immunity seven deubiquitinases nlrp3 inflammasome increased activation icm transporter human health exists ubiquitously e2 ubch5c cysteine residue common target chemically distinct causative agent
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Lug14 promotes NLRP3 inflammasome activation by inhibiting the E3 ligase activity of ARIH2.

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