TLR4 and CD14 trafficking and its influence on LPS-induced pro-inflammatory signaling

Toll-like receptor (TLR) 4 belongs to the TLR family of receptors inducing pro-inflammatory responses to invading pathogens. TLR4 is activated by lipopolysaccharide (LPS, endotoxin) of Gram-negative bacteria and sequentially triggers two signaling cascades: the first one involving TIRAP and MyD88 ad...

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Published in	Cellular and molecular life sciences : CMLS Vol. 78; no. 4; pp. 1233 - 1261
Main Authors	Ciesielska, Anna, Matyjek, Marta, Kwiatkowska, Katarzyna
Format	Journal Article
Language	English
Published	Cham Springer International Publishing 01.02.2021 Springer Nature B.V
Subjects	Adaptor proteins Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Vesicular Transport - genetics Autoimmune diseases Bacteria Biochemistry Biodegradation Biomedical and Life Sciences Biomedicine CD14 antigen Cell Biology E coli Endocytosis Endosomes Endotoxins Escherichia coli Gram-negative bacteria Humans Immune system Inflammation Inflammation - chemically induced Inflammation - genetics Inflammation - pathology Internalization Life Sciences Lipopolysaccharide Receptors - genetics Lipopolysaccharides Lipopolysaccharides - toxicity Lysosomes Membrane Glycoproteins - genetics Membranes MyD88 protein Myeloid Differentiation Factor 88 - genetics Neurodegeneration neurodegenerative diseases Phagocytosis Phagocytosis - genetics plasma membrane Protein turnover Proteins Receptors Receptors, Interleukin-1 - genetics Review Signaling TLR4 protein Toll-Like Receptor 4 - genetics Toll-like receptors Endocytosis CD14 Endotoxin Endosome TLR4 LPS
Online Access	Get full text
ISSN	1420-682X 1420-9071 1420-9071
DOI	10.1007/s00018-020-03656-y

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Abstract	Toll-like receptor (TLR) 4 belongs to the TLR family of receptors inducing pro-inflammatory responses to invading pathogens. TLR4 is activated by lipopolysaccharide (LPS, endotoxin) of Gram-negative bacteria and sequentially triggers two signaling cascades: the first one involving TIRAP and MyD88 adaptor proteins is induced in the plasma membrane, whereas the second engaging adaptor proteins TRAM and TRIF begins in early endosomes after endocytosis of the receptor. The LPS-induced internalization of TLR4 and hence also the activation of the TRIF-dependent pathway is governed by a GPI-anchored protein, CD14. The endocytosis of TLR4 terminates the MyD88-dependent signaling, while the following endosome maturation and lysosomal degradation of TLR4 determine the duration and magnitude of the TRIF-dependent one. Alternatively, TLR4 may return to the plasma membrane, which process is still poorly understood. Therefore, the course of the LPS-induced pro-inflammatory responses depends strictly on the rates of TLR4 endocytosis and trafficking through the endo-lysosomal compartment. Notably, prolonged activation of TLR4 is linked with several hereditary human diseases, neurodegeneration and also with autoimmune diseases and cancer. Recent studies have provided ample data on the role of diverse proteins regulating the functions of early, late, and recycling endosomes in the TLR4-induced inflammation caused by LPS or phagocytosis of E. coli. In this review, we focus on the mechanisms of the internalization and intracellular trafficking of TLR4 and CD14, and also of LPS, in immune cells and discuss how dysregulation of the endo-lysosomal compartment contributes to the development of diverse human diseases.
AbstractList	Toll-like receptor (TLR) 4 belongs to the TLR family of receptors inducing pro-inflammatory responses to invading pathogens. TLR4 is activated by lipopolysaccharide (LPS, endotoxin) of Gram-negative bacteria and sequentially triggers two signaling cascades: the first one involving TIRAP and MyD88 adaptor proteins is induced in the plasma membrane, whereas the second engaging adaptor proteins TRAM and TRIF begins in early endosomes after endocytosis of the receptor. The LPS-induced internalization of TLR4 and hence also the activation of the TRIF-dependent pathway is governed by a GPI-anchored protein, CD14. The endocytosis of TLR4 terminates the MyD88-dependent signaling, while the following endosome maturation and lysosomal degradation of TLR4 determine the duration and magnitude of the TRIF-dependent one. Alternatively, TLR4 may return to the plasma membrane, which process is still poorly understood. Therefore, the course of the LPS-induced pro-inflammatory responses depends strictly on the rates of TLR4 endocytosis and trafficking through the endo-lysosomal compartment. Notably, prolonged activation of TLR4 is linked with several hereditary human diseases, neurodegeneration and also with autoimmune diseases and cancer. Recent studies have provided ample data on the role of diverse proteins regulating the functions of early, late, and recycling endosomes in the TLR4-induced inflammation caused by LPS or phagocytosis of E. coli. In this review, we focus on the mechanisms of the internalization and intracellular trafficking of TLR4 and CD14, and also of LPS, in immune cells and discuss how dysregulation of the endo-lysosomal compartment contributes to the development of diverse human diseases. Toll-like receptor (TLR) 4 belongs to the TLR family of receptors inducing pro-inflammatory responses to invading pathogens. TLR4 is activated by lipopolysaccharide (LPS, endotoxin) of Gram-negative bacteria and sequentially triggers two signaling cascades: the first one involving TIRAP and MyD88 adaptor proteins is induced in the plasma membrane, whereas the second engaging adaptor proteins TRAM and TRIF begins in early endosomes after endocytosis of the receptor. The LPS-induced internalization of TLR4 and hence also the activation of the TRIF-dependent pathway is governed by a GPI-anchored protein, CD14. The endocytosis of TLR4 terminates the MyD88-dependent signaling, while the following endosome maturation and lysosomal degradation of TLR4 determine the duration and magnitude of the TRIF-dependent one. Alternatively, TLR4 may return to the plasma membrane, which process is still poorly understood. Therefore, the course of the LPS-induced pro-inflammatory responses depends strictly on the rates of TLR4 endocytosis and trafficking through the endo-lysosomal compartment. Notably, prolonged activation of TLR4 is linked with several hereditary human diseases, neurodegeneration and also with autoimmune diseases and cancer. Recent studies have provided ample data on the role of diverse proteins regulating the functions of early, late, and recycling endosomes in the TLR4-induced inflammation caused by LPS or phagocytosis of E. coli. In this review, we focus on the mechanisms of the internalization and intracellular trafficking of TLR4 and CD14, and also of LPS, in immune cells and discuss how dysregulation of the endo-lysosomal compartment contributes to the development of diverse human diseases. Toll-like receptor (TLR) 4 belongs to the TLR family of receptors inducing pro-inflammatory responses to invading pathogens. TLR4 is activated by lipopolysaccharide (LPS, endotoxin) of Gram-negative bacteria and sequentially triggers two signaling cascades: the first one involving TIRAP and MyD88 adaptor proteins is induced in the plasma membrane, whereas the second engaging adaptor proteins TRAM and TRIF begins in early endosomes after endocytosis of the receptor. The LPS-induced internalization of TLR4 and hence also the activation of the TRIF-dependent pathway is governed by a GPI-anchored protein, CD14. The endocytosis of TLR4 terminates the MyD88-dependent signaling, while the following endosome maturation and lysosomal degradation of TLR4 determine the duration and magnitude of the TRIF-dependent one. Alternatively, TLR4 may return to the plasma membrane, which process is still poorly understood. Therefore, the course of the LPS-induced pro-inflammatory responses depends strictly on the rates of TLR4 endocytosis and trafficking through the endo-lysosomal compartment. Notably, prolonged activation of TLR4 is linked with several hereditary human diseases, neurodegeneration and also with autoimmune diseases and cancer. Recent studies have provided ample data on the role of diverse proteins regulating the functions of early, late, and recycling endosomes in the TLR4-induced inflammation caused by LPS or phagocytosis of E. coli. In this review, we focus on the mechanisms of the internalization and intracellular trafficking of TLR4 and CD14, and also of LPS, in immune cells and discuss how dysregulation of the endo-lysosomal compartment contributes to the development of diverse human diseases.Toll-like receptor (TLR) 4 belongs to the TLR family of receptors inducing pro-inflammatory responses to invading pathogens. TLR4 is activated by lipopolysaccharide (LPS, endotoxin) of Gram-negative bacteria and sequentially triggers two signaling cascades: the first one involving TIRAP and MyD88 adaptor proteins is induced in the plasma membrane, whereas the second engaging adaptor proteins TRAM and TRIF begins in early endosomes after endocytosis of the receptor. The LPS-induced internalization of TLR4 and hence also the activation of the TRIF-dependent pathway is governed by a GPI-anchored protein, CD14. The endocytosis of TLR4 terminates the MyD88-dependent signaling, while the following endosome maturation and lysosomal degradation of TLR4 determine the duration and magnitude of the TRIF-dependent one. Alternatively, TLR4 may return to the plasma membrane, which process is still poorly understood. Therefore, the course of the LPS-induced pro-inflammatory responses depends strictly on the rates of TLR4 endocytosis and trafficking through the endo-lysosomal compartment. Notably, prolonged activation of TLR4 is linked with several hereditary human diseases, neurodegeneration and also with autoimmune diseases and cancer. Recent studies have provided ample data on the role of diverse proteins regulating the functions of early, late, and recycling endosomes in the TLR4-induced inflammation caused by LPS or phagocytosis of E. coli. In this review, we focus on the mechanisms of the internalization and intracellular trafficking of TLR4 and CD14, and also of LPS, in immune cells and discuss how dysregulation of the endo-lysosomal compartment contributes to the development of diverse human diseases.
Author	Matyjek, Marta Ciesielska, Anna Kwiatkowska, Katarzyna
Author_xml	– sequence: 1 givenname: Anna orcidid: 0000-0001-9902-494X surname: Ciesielska fullname: Ciesielska, Anna email: a.ciesielska@nencki.edu.pl organization: Laboratory of Molecular Membrane Biology, Nencki Institute of Experimental Biology of Polish Academy of Sciences – sequence: 2 givenname: Marta surname: Matyjek fullname: Matyjek, Marta organization: Laboratory of Molecular Membrane Biology, Nencki Institute of Experimental Biology of Polish Academy of Sciences – sequence: 3 givenname: Katarzyna orcidid: 0000-0002-0550-8394 surname: Kwiatkowska fullname: Kwiatkowska, Katarzyna organization: Laboratory of Molecular Membrane Biology, Nencki Institute of Experimental Biology of Polish Academy of Sciences
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/33057840$$D View this record in MEDLINE/PubMed
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Issue	4
Keywords	Endocytosis CD14 Endotoxin Endosome TLR4 LPS
Language	English
License	Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. cc-by
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PublicationTitle	Cellular and molecular life sciences : CMLS
PublicationTitleAbbrev	Cell. Mol. Life Sci
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PublicationYear	2021
Publisher	Springer International Publishing Springer Nature B.V
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Snippet	Toll-like receptor (TLR) 4 belongs to the TLR family of receptors inducing pro-inflammatory responses to invading pathogens. TLR4 is activated by...
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SubjectTerms	Adaptor proteins Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Vesicular Transport - genetics Autoimmune diseases Bacteria Biochemistry Biodegradation Biomedical and Life Sciences Biomedicine CD14 antigen Cell Biology E coli Endocytosis Endosomes Endotoxins Escherichia coli Gram-negative bacteria Humans Immune system Inflammation Inflammation - chemically induced Inflammation - genetics Inflammation - pathology Internalization Life Sciences Lipopolysaccharide Receptors - genetics Lipopolysaccharides Lipopolysaccharides - toxicity Lysosomes Membrane Glycoproteins - genetics Membranes MyD88 protein Myeloid Differentiation Factor 88 - genetics Neurodegeneration neurodegenerative diseases Phagocytosis Phagocytosis - genetics plasma membrane Protein turnover Proteins Receptors Receptors, Interleukin-1 - genetics Review Signaling TLR4 protein Toll-Like Receptor 4 - genetics Toll-like receptors
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Title	TLR4 and CD14 trafficking and its influence on LPS-induced pro-inflammatory signaling
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