Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Mutational scans of the chemokine receptors CXCR4 and CCR5 based on bimolecular fluorescence complementation reveal multiple mechanisms for receptor association

ABSTRACT: Mutational scans of the chemokine receptors CXCR4 and CCR5 based on bimolecular fluorescence complementation reveal multiple mechanisms for receptor association

PROVIDER: PRJNA516349 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR8469570_1.fastq.gz	Fastqsanger.gz
	SRR8469570_2.fastq.gz	Fastqsanger.gz
	SRR8469571_1.fastq.gz	Fastqsanger.gz
	SRR8469571_2.fastq.gz	Fastqsanger.gz
	SRR8469572_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 20

Similar Datasets

Mutational scans of the chemokine receptors CXCR4 and CCR5 based on bimolecular fluorescence complementation reveal multiple mechanisms for receptor association

Project description:Many G protein-coupled receptors (GPCRs) are found to homo- or hetero-oligomerize, but how and why GPCRs associate remains controversial. The class A chemokine receptors CCR5 and CXCR4 both homo- and heterodimerize with each other, and crystal structures of CXCR4 in inactive conformations have captured dimeric organization. By selecting libraries of CCR5 and CXCR4 variants based on bimolecular fluorescence complementation, we determine how nearly every single amino acid substitution effects homo-associations. We find three mechanisms for chemokine receptor association: (i) non-specific aggregation in the membrane phase enhanced by destabilizing structural mutations, (ii) specific protein-protein dimerization interfaces, and (iii) motifs in the cytoplasmic tails that are hypothesized to promote lipid raft localization, thereby bringing receptors close together at high density. We identify mutations that tease apart the effects of these respective mechanisms, and show that specific dimer organization, despite reducing agonist binding, is necessary for active signaling within the cell.

2020-05-01 | GSE125426 | GEO

Mutational scans of the chemokine receptors CXCR4 and CCR5 based on bimolecular fluorescence complementation reveal multiple mechanisms for receptor association

Project description:Mutational scans of the chemokine receptors CXCR4 and CCR5 based on bimolecular fluorescence complementation reveal multiple mechanisms for receptor association

| PRJNA516349 | ENA

People with HIV have higher percentages of circulating CCR5+ CD8+ T cells and lower percentages of CCR5+ regulatory T cells

Project description:CCR5 is the main HIV co-receptor. We aimed to (1) compare CCR5 expression on immune cells between people living with HIV (PLHIV) using combination antiretroviral therapy (cART) and HIV-uninfected controls, (2) relate CCR5 expression to viral reservoir size and (3) assess detereminants of CCR5 expression. Percentages of CCR5 positive cells (%) and CCR5 mean fluorescence intensity (MFI) assessed by flow cytometry in monocytes and lymphocyte subsets were correlated to host factors, HIV-1 cell-associated (CA)-RNA and CA-DNA, plasma inflammation markers and metabolites.

2022-08-12 | PXD031628 | Pride

Identification of Direct Upstream Kinases by Fluorescence Complementation Mass Spectrometry

Project description:Kinase-substrate networks are the main components of many signal transduction pathways. Although proteome-wide studies have been successful in elucidating many important biological events including the cataloging of thousands of sites of protein phosphorylation, there is a lack of a universal method to identify the direct upstream kinases responsible for many of these modifications. We have introduced Fluorescence ComplementatiKinase-substrate networks are the main components of many signal transduction pathways. Although proteome-wide studies have been successful in elucidating many important biological events including the cataloging of thousands of sites of protein phosphorylation, there is a lack of a universal method to identify the direct upstream kinases responsible for many of these modifications. We have introduced Fluorescence Complementation Mass Spectrometry (FCMS) as the first proteomic approach that identifies direct upstream kinases in living cells by stabilizing and capturing the kinase-substrate pairs. Using FCMS, we have identified both known and novel direct kinases of cAMP response element-binding protein (CREB). on Mass Spectrometry (FCMS) as the first proteomic approach that identifies direct upstream kinases in living cells by stabilizing and capturing the kinase-substrate pairs. Using FCMS, we have identified both known and novel direct kinases of cAMP response element-binding protein (CREB).

2017-11-08 | PXD004739 | Pride

Mapping Interaction Sites on Human Chemokine Receptors by Deep Mutational Scanning

Project description:Chemokine receptors CXCR4 and CCR5 regulate white blood cell trafficking, and are engaged by the HIV-1 envelope glycoprotein gp120 during infection. We combine directed evolution of CXCR4 and CCR5 libraries comprising nearly all ~7,000 single amino acid substitutions with deep sequencing to define sequence-fitness landscapes for surface expression and ligand interactions. Functional interaction sites are mapped based on conservation; for example, extracellular residues are conserved for binding HIV-1-blocking antibodies, as expected. Chemokine CXCL12 interacts with residues extending asymmetrically into the CXCR4 ligand-binding cavity, and distal mutations within allosteric and G protein coupling sites are identified that enhance chemokine binding. CCR5 residues conserved for gp120 interactions partially overlap with the chemokine-binding site, and gp120 binding is increased by acidic substitutions in the CCR5 N-terminus and extracellular loops. Furthermore, general features are apparent from sequence patterns, including membrane regions that are intolerant to polar mutations, and deleterious cysteine substitutions within extracellular loops.

2018-04-23 | GSE100368 | GEO

study of medical treatment reactivity by the chemokine receptor (CXCR4)as 1st line treatment in patients with metastatic colorectal cancer

Project description:Interventions: CXCR4-CEC>=20 mFOLFOX6,Bevacizumab L-OHP:85mg/m2 5-FU(bolus):400mg/m2 l-LV:200mg/m2 5-FU(infusion):2,400mg/m2 Bevacizumab:5mg/m2 CXCR4-CEC>=20 mFOLFOX6,Panitumumab L-OHP:85mg/m2 5-FU(bolus):400mg/m2 l-LV:200mg/m2 5-FU(infusion):2,400mg/m2 Panitumumab :6mg/m2 CXCR4-CEC<20 mFOLFOX6,Bevacizumab L-OHP:85mg/m2 5-FU(bolus):400mg/m2 l-LV:200mg/m2 5-FU(infusion):2,400mg/m2 Bevacizumab:5mg/m2 CXCR4-CEC<20 mFOLFOX6,Panitumumab L-OHP:85mg/m2 5-FU(bolus):400mg/m2 l-LV:200mg/m2 5-FU(infusion):2,400mg/m2 Panitumumab :6mg/m2 Primary outcome(s): Progression-free survival Study Design: Parallel Randomized

| 2623948 | ecrin-mdr-crc

Differential Gene expression in CCR5+ versus CCR5- OT-I T cells

Project description:OT-I T cells were exposed to CpG ODN-activated CCR5ko Lymph nodes for 6 h, stained for surface CCR5 and FACS-sorted into CCR5+ and CCR5- fractions In the study presented here freshly isolated OT1 T cells were exposed for 6h at 37oC to teased-out CpG ODN-activated CCR5ko LNs in 96-well plates and stained for surface CCR5 before sorting into CCR5+ (Hua2) and CCR5- (Hua1) fractions. High quality total RNA isolated from each cell fraction using TRIZOL and Qiagen RNEasy kit per manufacture's recommendation was subjected to microarray analysis using the Affymetrix Mouse Gene ST 1.0 array chip to discover differentially expressed genes.

2016-01-14 | E-GEOD-76820 | biostudies-arrayexpress

Differential Gene expression in CCR5+ versus CCR5- OT-I T cells

Project description:OT-I T cells were exposed to CpG ODN-activated CCR5ko Lymph nodes for 6 h, stained for surface CCR5 and FACS-sorted into CCR5+ and CCR5- fractions

2016-01-14 | GSE76820 | GEO

CCR5 HIV controllers

Project description:CCR5 HIV controllers

| PRJEB48153 | ENA

IL-15 Enhances HIV-1 infection by Promoting Differentiation and Survival of CCR5+CD4+ T cells

Project description:HIV-1 usually utilize CCR5 as the co-receptor and rarely switches to CXCR4-tropic until late stage of infection. CCR5+CD4+ T cells are the major virus-producing cells in patients as well as SIV-infected non-human primates. The differentiation of CCR5+CD4+ T cells is associated with the availability of IL-15, which increases during acute HIV-1 infection. Here, we report that CCR5 is expressed by CD4+ T cells exhibiting effector or effector memory phenotype with high expression levels of the IL-2/IL-15 receptor common beta and gamma chains. IL-15 but not IL-7 improves the survival of CCR5+CD4+ T cells, drives their expansion, and facilitates HIV-1 infection in vitro and in humanized mice. Our study suggests that IL-15 plays confounding roles in HIV-1 infection, and future studies on the IL-15-based boosting of anti-HIV-1 immunity should carefully exam the potential effects on the expansion of HIV-1 reservoirs in CCR5+CD4+ T cells.

2022-04-03 | GSE199729 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data