التفاصيل البيبلوغرافية
| العنوان: |
Bacteria make surgical strikes on host ubiquitin signaling. |
| المؤلفون: |
Franklin, Tyler G.1 (AUTHOR), Pruneda, Jonathan N.1 (AUTHOR) pruneda@ohsu.edu |
| المصدر: |
PLoS Pathogens. 3/18/2021, Vol. 17 Issue 3, p1-6. 6p. |
| مصطلحات موضوعية: |
*UBIQUITIN, *UBIQUITIN ligases, *TRIM proteins, *BACTERIAL proteins, *BACTERIA, *PATTERN perception receptors |
| مستخلص: |
The NELs IpaH1.4 and IpaH2.5 attach Lys48-linked poly-ubiquitin to the catalytic subunit of LUBAC, targeting it for proteasomal degradation and thereby preventing Met1 poly-ubiquitin chain formation and subsequent inflammatory signaling [[32]]. Typhimurium, I Legionella pneumophila i , and enterohemorrhagic I Escherichia coli i (EHEC) have all acquired E3 ligases that transfer ubiquitin through a cysteine-based mechanism and can dictate poly-ubiquitin chain specificity [[7]-[10]]. Using IpaH9.8, a separate NEL effector, I Shigella i also targets the Met1 poly-ubiquitin sensor protein NEMO for ubiquitin-dependent proteasomal degradation, thus blocking activation of the I B kinase complex required for NF- B signaling [[23]]. Bacterial ligases destroy key targets Poly-ubiquitin signals linked through Lys48 are the canonical message for proteasomal degradation, and bacterial E3 ligases frequently take advantage of this process to selectively degrade target host proteins [[1]]. [Extracted from the article] |
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