Identification of the recipient lysine residues on ubiquitinated ARIH2 induced by Lug14.

<p>Protein bands representing ubiquitinated ARIH2 were excised and digested with trypsin. The peptides characteristic of ubiquitination bearing the diGly remnant were detected and the modified lysine residues were mapped by LC/MS analysis. The spectra of fragments harboring K295 and K306 were...

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Bibliographic Details
Main Author:	Shuxin Liu (2792104) (author)
Other Authors:	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)
Published:	2025
Subjects:	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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Identification of the recipient lysine residues on ubiquitinated ARIH2 induced by Lug14.

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