Beyond proteins: Ubiquitylation of lipopolysaccharide to fight bacteria

Mechanisms and functions of protein ubiquitylation and LPS ubiquitylation. LPS ubiquitylation serves as a scaffold to recruit E3 ligases for the ubiquitylation of the membrane of bacteria. Polyubiquitin coat on the bacterial cell surface is one type of “eat‐me” signal recognized by the host cells. T...

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Autores principales: Gong, Yanqiu, Nie, Litong, Dai, Lunzhi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Highlights
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8706746/
https://www.ncbi.nlm.nih.gov/pubmed/34977880
http://dx.doi.org/10.1002/mco2.86
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author Gong, Yanqiu
Nie, Litong
Dai, Lunzhi
author_facet Gong, Yanqiu
Nie, Litong
Dai, Lunzhi
author_sort Gong, Yanqiu
collection PubMed
description Mechanisms and functions of protein ubiquitylation and LPS ubiquitylation. LPS ubiquitylation serves as a scaffold to recruit E3 ligases for the ubiquitylation of the membrane of bacteria. Polyubiquitin coat on the bacterial cell surface is one type of “eat‐me” signal recognized by the host cells. The abbreviations used in the figure are Pro, Protein; Ub, Ubiquitin; E1, Ubiquitin‐activating enzymes; E2, Ubiquitin‐conjugating enzymes; E3, Ubiquitin‐ligating enzymes; LPS, lipopolysaccharide; RNF213, Ring Finger Protein 213; and LUBAC, linear ubiquitin chain assembly complex. [Image: see text]
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spelling pubmed-87067462021-12-30 Beyond proteins: Ubiquitylation of lipopolysaccharide to fight bacteria Gong, Yanqiu Nie, Litong Dai, Lunzhi MedComm (2020) Highlights Mechanisms and functions of protein ubiquitylation and LPS ubiquitylation. LPS ubiquitylation serves as a scaffold to recruit E3 ligases for the ubiquitylation of the membrane of bacteria. Polyubiquitin coat on the bacterial cell surface is one type of “eat‐me” signal recognized by the host cells. The abbreviations used in the figure are Pro, Protein; Ub, Ubiquitin; E1, Ubiquitin‐activating enzymes; E2, Ubiquitin‐conjugating enzymes; E3, Ubiquitin‐ligating enzymes; LPS, lipopolysaccharide; RNF213, Ring Finger Protein 213; and LUBAC, linear ubiquitin chain assembly complex. [Image: see text] John Wiley and Sons Inc. 2021-09-09 /pmc/articles/PMC8706746/ /pubmed/34977880 http://dx.doi.org/10.1002/mco2.86 Text en © 2021 The Authors. MedComm published by Sichuan International Medical Exchange & Promotion Association (SCIMEA) and John Wiley & Sons Australia, Ltd. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Highlights
Gong, Yanqiu
Nie, Litong
Dai, Lunzhi
Beyond proteins: Ubiquitylation of lipopolysaccharide to fight bacteria
title Beyond proteins: Ubiquitylation of lipopolysaccharide to fight bacteria
title_full Beyond proteins: Ubiquitylation of lipopolysaccharide to fight bacteria
title_fullStr Beyond proteins: Ubiquitylation of lipopolysaccharide to fight bacteria
title_full_unstemmed Beyond proteins: Ubiquitylation of lipopolysaccharide to fight bacteria
title_short Beyond proteins: Ubiquitylation of lipopolysaccharide to fight bacteria
title_sort beyond proteins: ubiquitylation of lipopolysaccharide to fight bacteria
topic Highlights
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8706746/
https://www.ncbi.nlm.nih.gov/pubmed/34977880
http://dx.doi.org/10.1002/mco2.86
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