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Protein prenylation drives discrete signaling programs for the differentiation and maintenance of effector Treg cells [Microarray Dataset 3]

ABSTRACT: An interplay between immune signals, isoprenoids-mediated protein prenylation, and intracellular signaling for the differentiation and maintenance of eTreg cells. We used microarrays to compare the global transcription profiles of in vitro activated CD4+YFP+CD44loCD62Lhi cTreg cells sorted from Foxp3YFP-Cre mice and activated by 10 ug/ml anti-CD3/28 antibodies plus 200 U/ml IL-2 for different time points in the presence of prenylation inhibitors

ORGANISM(S): Mus musculus

PROVIDER: GSE158862 | GEO | 2021/01/20

REPOSITORIES: GEO

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Protein prenylation drives discrete signaling programs for the differentiation and maintenance of effector Treg cells [Microarray Dataset 1]

Project description:An interplay between immune signals, isoprenoids-mediated protein prenylation, and intracellular signaling for the differentiation and maintenance of eTreg cells. We used microarrays to compare the global transcription profiles of CD4+YFP+Treg cells from WT, Foxp3CreFntbfl/fl mixed bone marrow chimeras

2021-01-20 | GSE158860 | GEO

Protein prenylation drives discrete signaling programs for the differentiation and maintenance of effector Treg cells [Microarray Dataset 2]

2021-01-20 | GSE158861 | GEO

Protein prenylation drives discrete signaling programs for the differentiation and maintenance of effector Treg cells [Pggt1b_ATACseq]

Project description:An interplay between immune signals, isoprenoids-mediated protein prenylation, and intracellular signaling for the differentiation and maintenance of eTreg cells.

2021-01-20 | GSE158921 | GEO

Protein prenylation drives discrete signaling programs for the differentiation and maintenance of effector Treg cells [Fntb_ATACseq]

Project description:An interplay between immune signals, isoprenoids-mediated protein prenylation, and intracellular signaling for the differentiation and maintenance of eTreg cells.

2021-01-20 | GSE158920 | GEO

Transcriptome analysis of OGT-sufficient and OGT-deficient regulatory T (Treg) cells

Project description:To gain comprehensive insight into the OGT-dependent transcriptional program in Treg cells, we performed RNA-sequencing of isolated YFP+ Treg cells from Foxp3YFP-Cre/wtOgtwt/fl and healthy Foxp3YFP-Cre/wtOgtfl/fl females to avoid secondary changes in gene expression caused by inflammation. We were able to identify 269 differentially expressed genes including 154 downregulated and 115 upregulated with p values less than 0.01, OGT-deficient Treg cells had impaired suppressive function and attenuated IL2/STAT5 signaling pathway.

2018-12-21 | GSE116758 | GEO

Protein prenylation drives discrete signaling programs for the differentiation and maintenance of effector Treg cells

Project description:Protein prenylation drives discrete signaling programs for the differentiation and maintenance of effector Treg cells

| PRJNA666782 | ENA

Thinking outside the CaaX-box: an unusual reversible prenylation on ALDH9A1

Project description:Protein lipidation is a post-translational modification that confers hydrophobicity on protein substrates to control their cellular localization, mediate protein trafficking, and regulate protein function. In particular, protein prenylation is a C-terminal modification on proteins bearing canonical motifs catalyzed by prenyltransferases. Prenylated proteins have been of interest due to their numerous associations with various diseases. Chemical proteomic approaches have been pursued over the last decade to define prenylated proteomes (prenylome) and probe their responses to perturbations in various cellular systems. Here, we describe the discovery of prenylation of a non-canonical prenylated protein, ALDH9A1, which lacks any apparent prenylation motif. This enzyme was initially identified through chemical proteomic profiling of prenylomes in various cell lines. Metabolic labeling with an isoprenoid probe using overexpressed ALDH9A1 revealed that this enzyme can be prenylated inside cells but does not respond to inhibition by prenyltransferase inhibitors. Site-directed mutagenesis of the key residues involved in ALDH9A1 activity indicates that the catalytic C288 bears the isoprenoid modification likely through an NAD+-dependent mechanism. Furthermore, the isoprenoid modification is also susceptible to hydrolysis, indicating a reversible modification. We hypothesize that this modification originates from endogenous farnesal or geranygeranial, the established degradation products of prenylated proteins and results in a thioester form that accumulates. This novel reversible prenoyl modification on ALDH9A1 expands the current paradigm of protein prenylation by illustrating a potentially new type of protein–lipid modification that may also serve as a novel mechanism for controlling enzyme function

2023-11-06 | PXD036365 | Pride

Protein prenylation drives discrete signaling programs for the differentiation and maintenance of effector Treg cells [Pggt1b_ATACseq]

Project description:Protein prenylation drives discrete signaling programs for the differentiation and maintenance of effector Treg cells [Pggt1b_ATACseq]

| PRJNA667026 | ENA

Protein prenylation drives discrete signaling programs for the differentiation and maintenance of effector Treg cells [Fntb_ATACseq]

Project description:Protein prenylation drives discrete signaling programs for the differentiation and maintenance of effector Treg cells [Fntb_ATACseq]

| PRJNA667029 | ENA

A Quantitative Chemical Proteomics Approach Using a Novel Two-Probe System Enables System-Wide Analysis of Protein Prenylation

Project description:Proteins prenylation, the post-translational attachment of a farnesyl or geranylgeranyl isoprenoid to one or more C-terminal cysteine residues, is an important modulator of localization and function of proteins such as the Ras isoforms, and a widely studied therapeutic target in number of cancer and other diseases. Despite its clinical importance, tools to interrogate prenylation and to quantify changes in response to treatment or disease on a global scale are lacking. Herein we report the development of two novel isoprenoid analogues, YnF and YnGG, which when used in combination with quantitative proteomics technologies enables the global profiling of prenylated proteins in living cells. The workflow enabled validation of a 51 prenylated CXXX-motif proteins, including seven novel farnesylated substrates, and 29 Rab proteins. Furthermore, we present tools which enable the detection of prenylated peptides at native abundance. We developed a quantitative strategy to decipher changes in prenylation in response to several inhibitors, including the clinically relevant farnesyl transferase inhibitor Tipifarnib, enabling in-cell dose responses of individual inhibitors, as well as shedding light on the alternative prenylation dynamics caused by inhibition of one prenyl transferase. Finally, we show how our methodology can be employed to further our understanding of prenylation in disease models such as Choroideremia by quantifying the effect of prenylation on 30 Rab substrates in response to Rep-1 knock-out.

2019-03-29 | PXD009155 | Pride

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