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Article ; Online: Degradation of nuclear Ubc9 induced by listeriolysin O is dependent on K

Li, Jiexin / Lam, Wendy Wai-Ling / Lai, Tsz-Wah / Au, Shannon Wing-Ngor

Biochemical and biophysical research communications

2017  Volume 493, Issue 2, Page(s) 1115–1121

Abstract: Listeriolysin O (LLO) is a pore-forming toxin produced by L. monocytogenes, and is belonged to a protein family of cholesterol-dependent cytolysins (CDCs). Previous studies have demonstrated that LLO triggers Ubc9 degradation and disrupts host ... ...

Abstract Listeriolysin O (LLO) is a pore-forming toxin produced by L. monocytogenes, and is belonged to a protein family of cholesterol-dependent cytolysins (CDCs). Previous studies have demonstrated that LLO triggers Ubc9 degradation and disrupts host SUMOylation to facilitate bacterial infection. However, the underlying mechanism of Ubc9 degradation is unclear. Here we show that LLO-induced down-regulation of Ubc9 is independent of Ubc9-SUMO interaction, however, it may involve phosphorylation signaling. Additionally, LLO exerts its effects primarily on nuclear Ubc9 and this process is mediated by K
MeSH term(s) Bacterial Toxins/metabolism ; Cations, Monovalent/metabolism ; HeLa Cells ; Heat-Shock Proteins/metabolism ; Hemolysin Proteins/metabolism ; Host-Pathogen Interactions ; Humans ; Listeria monocytogenes/physiology ; Listeriosis/metabolism ; Listeriosis/microbiology ; Phosphorylation ; Potassium/metabolism ; Proteolysis ; Sumoylation ; Ubiquitin-Conjugating Enzymes/metabolism
Chemical Substances Bacterial Toxins ; Cations, Monovalent ; Heat-Shock Proteins ; Hemolysin Proteins ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; ubiquitin-conjugating enzyme UBC9 (EC 6.3.2.-) ; hlyA protein, Listeria monocytogenes (R06ZRQ1YX9) ; Potassium (RWP5GA015D)
Language English
Publishing date 2017-09-12
Publishing country United States
Document type Journal Article
ZDB-ID 205723-2
ISSN 1090-2104 ; 0006-291X ; 0006-291X
ISSN (online) 1090-2104 ; 0006-291X
ISSN 0006-291X
DOI 10.1016/j.bbrc.2017.09.051
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