MHC class II association with lipid rafts on the antigen presenting cell surface

Anderson, Howard A.; Roche, Paul A.

doi:10.1016/j.bbamcr.2014.09.019

Cited by 49 publications

(40 citation statements)

References 72 publications

(89 reference statements)

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“…Recent studies using super-resolution microscopy or single particle tracking indicate that lipid rafts are highly dynamic, transient nanometer-scaled membrane domains (8,9), present in numerous cellular organelles (10,11). Together, these studies support the potential role of lipid rafts in signal transduction by selective recruitment of transmembrane or peripheral membrane proteins with affinity for liquid ordered membranes (6,(12)(13)(14)(15)(16)(17).…”

Section: Introductionmentioning

confidence: 83%

RaftProt V2: understanding membrane microdomain function through lipid raft proteomes

Mohamed

Shah

Chen

et al. 2018

Preprint

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Cellular membranes feature dynamic submicrometer-scale lateral membrane domainsvariously referred to as lipid rafts, membrane rafts or glycosphingolipid-enriched microdomains (GEM). In order to understand the molecular functions of lipid rafts, numerous studies have utilized various biochemical methods to isolate and examine the protein composition of membrane rafts. However, interpretation of individual raft proteomics studies are confounded by the limitations of isolation methods and the dynamic nature of rafts. Knowledge-based approaches can facilitate biological data interpretation by integrating experimental evidence from existing studies. To this end, we previously developed RaftProt (http://lipid-raft-database.di.uq.edu.au/), a searchable database of mammalian lipid raft-associated proteins. Despite being a valuable and highly used resource, improvements in search capabilities and visualisation were still needed. Here, we present RaftProt V2 (http://raftprot.org), an improved update of RaftProt, enabling interrogation and integration of datasets at the cell/tissue type and UniRef/Gene level. Besides the addition of new datasets and re-mapping of all entries to both UniProt and UniRef IDs, we have annotated the level of experimental evidence for each protein entry. The search engine now allows for multiple protein or experiment searches where correlations, interactions or overlaps can be investigated. The web-interface has been completely redesigned and offers new interactive tools for data and subset selection, correlation analysis and network visualization. Overall, RaftProt aims to advance our understanding of lipid raft function by revealing the proteomes and pathways that are associated with membrane microdomains in diverse tissue and conditions.

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Section: Introductionmentioning

confidence: 83%

RaftProt V2: understanding membrane microdomain function through lipid raft proteomes

Mohamed

Shah

Chen

et al. 2018

Preprint

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“…These interactions lead to the formation of cellular membrane microdomains, so called lipid rafts, which are rich domains in cholesterol, GSLs, sphingomyelin, glycosylphosphatidylinositol, and membrane‐anchored molecules . GSL‐enriched lipid rafts contribute innate and adaptive immune systems . The innate and adaptive immune systems are involved in resistance to invading pathogens, but the two systems are functionally distinct.…”

mentioning

confidence: 99%

The regulatory roles of glycosphingolipid‐enriched lipid rafts in immune systems

et al. 2018

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Lipid rafts formed by glycosphingolipids (GSLs) on cellular membranes play important roles in innate and adaptive immunity. Lactosylceramide (LacCer) forms lipid rafts on plasma and granular membranes of human neutrophils. These LacCer‐enriched lipid rafts bind directly to pathogenic components, such as pathogenic fungi‐derived β‐glucan and Mycobacteria‐derived lipoarabinomannan via carbohydrate‐carbohydrate interactions, and mediate innate immune responses to these pathogens. In contrast, a‐series and o‐series gangliosides form distinct rafts on CD4+ and CD8+ T cell subsets, respectively, contributing to the respective functions of these cells and stimulating adaptive immune responses through T cell receptors. These findings suggest that gangliosides play indispensable roles in T cell selection and activation. This Review introduces the involvement of GSL‐enriched lipid rafts in innate and adaptive immunity.

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“…Given the importance of microdomains, also called nanodomains, in providing a platform for organizing the signaling of many receptors and proteins including the B cell receptor, T cell receptor 92–94 and major histocompatibility class receptors 95, 96 it follows that lipid raft composition must be carefully regulated. The cholesterol needed for lipid raft formation and maintenance can be derived from exogenous sources such as lipoproteins, especially LDL, or from cellular synthesis via the mevalonate pathway in the ER followed by transport to the plasma membrane.…”

Section: Microdomain Cholesterol Regulation: the Role Of Effluxmentioning

confidence: 99%

Microdomains, Inflammation, and Atherosclerosis

Sorci‐Thomas

Thomas

2016

Circulation Research

139

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Elevated levels of cholesteryl ester (CE) enriched apoB containing plasma lipoproteins lead to increased foam cell formation, the first step in the development of atherosclerosis. Unregulated uptake of LDL cholesterol by circulating monocytes and other peripheral blood cells takes place through scavenger receptors and over time causes disruption in cellular cholesterol homeostasis. As lipoproteins are taken up, their CE core is hydrolyzed by liposomal lipases to generate free cholesterol (FC). FC can either be re-esterified and stored as CE droplets or shuttled to the plasma membrane for ATP binding cassette transporter A1 (ABCA1) mediated efflux. Since cholesterol is an essential component of all cellular membranes some FC may be incorporated into microdomains or lipid rafts. These platforms are essential for receptor signaling and transduction, requiring rapid assembly and disassembly. ABCA1 plays a major role in regulating microdomain cholesterol and is most efficient when lipid-poor HDL apolipoprotein A-I (apoA-I) packages raft cholesterol into soluble particles that are eventually catabolized by the liver. If FC is not effluxed from the cell, it becomes esterified and CE droplets accumulate. It follows that as the cell accumulates CE, microdomain cholesterol content becomes poorly regulated. This dysregulation leads to prolonged activation of immune cell signaling pathways, resulting in receptor over-sensitization. The availability of HDL apoA-I or other amphipathic α-helix rich apoproteins relieves the burden of excess microdomain cholesterol in immune cells allowing a reduction in immune cell proliferation and infiltration, thereby, stimulating regression of foam cells in the artery. Therefore, cellular balance between FC and CE is essential for proper immune cell function and prevents chronic immune cell overstimulation and proliferation.

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MHC class II association with lipid rafts on the antigen presenting cell surface

Cited by 49 publications

References 72 publications

RaftProt V2: understanding membrane microdomain function through lipid raft proteomes

RaftProt V2: understanding membrane microdomain function through lipid raft proteomes

The regulatory roles of glycosphingolipid‐enriched lipid rafts in immune systems

Microdomains, Inflammation, and Atherosclerosis

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