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PMID: 18707898 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Roles of ubiquitination in pattern-recognition receptors and type I interferon receptor signaling.

Cytokine ·Vol. 43 ·No. 3 ·2008-09-00 ·Pages 359-67

Bibeau-Poirier A, Servant MJ

Abstract

Post-translational protein modifications are involved in all functions of living cells. This includes the ability of cells to recognize pathogens and regulate genes involved in their clearance, a concept known as innate immunity. While phosphorylation mechanisms play essential roles in regulating different aspects of the innate immune response, ubiquitination is now recognized as another post-translational modification that works in parallel with phosphorylation to orchestrate the final proper innate immune response against invading pathogens. More precisely, this review will discuss the most recent advances that address the role of ubiquitination in pattern-recognition receptors and type I interferon receptor signaling.

MeSH Terms
Adaptor Proteins, Signal Transducing/physiology Animals DNA-Binding Proteins Deubiquitinating Enzyme CYLD Humans Intracellular Signaling Peptides and Proteins/physiology Membrane Proteins/physiology Nuclear Proteins/physiology Protein Processing, Post-Translational/physiology Receptor, Interferon alpha-beta/physiology Receptors, Pattern Recognition/physiology Signal Transduction/physiology Tumor Necrosis Factor Receptor-Associated Peptides and Proteins/physiology Tumor Necrosis Factor alpha-Induced Protein 3 Tumor Suppressor Proteins/physiology Ubiquitin-Protein Ligases/physiology Ubiquitination/physiology
Chemicals
Adaptor Proteins, Signal Transducing DNA-Binding Proteins Intracellular Signaling Peptides and Proteins Membrane Proteins Nuclear Proteins Receptors, Pattern Recognition TRAT1 protein, human Tumor Necrosis Factor Receptor-Associated Peptides and Proteins Tumor Suppressor Proteins Receptor, Interferon alpha-beta RNF216 protein, human Ubiquitin-Protein Ligases CYLD protein, human Deubiquitinating Enzyme CYLD TNFAIP3 protein, human Tumor Necrosis Factor alpha-Induced Protein 3
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bibeau-Poirier Annie
Faculté de Pharmacie, Université de Montréal, CP 6128, succursale Centre-Ville, Montréal, Québec, Canada.
Servant Marc J
Article Info
Journal
Cytokine
Abbr.
Cytokine
ISSN
1096-0023
Published
2008-09-00
Epub
2008-00-15
Pages
359-67
Language
English
Region
England
NLM ID
9005353
Subset
IM
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