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Neutralization of Acyl-CoA Binding Protein Confers Autophagy-Dependent Organ Protection

ABSTRACT: Neutralization of Acyl-CoA Binding Protein Confers Autophagy-Dependent Organ Protection

PROVIDER: PRJNA800343 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR17735530_1.fastq.gz	Fastqsanger.gz
	SRR17735530_2.fastq.gz	Fastqsanger.gz
	SRR17735531_1.fastq.gz	Fastqsanger.gz
	SRR17735531_2.fastq.gz	Fastqsanger.gz
	SRR17735532_1.fastq.gz	Fastqsanger.gz

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Neutralization of Acyl-CoA Binding Protein Confers Autophagy-Dependent Organ Protection

Project description:Total liver RNA extracts from adult male mice (8 weeks old, C57BL/6) injected with monoclonal anti-ACBP/DBI (1 dose per week) and subjected to Methionine and Choline Deficient Diet (regime duration: 4weeks) were analyzed to describe the effect of neutralization of ACBP/DBI to NASH-induced transcriptomic alterations.

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Acyl-coA Binding Protein neutralization improves cancer immunosurveillance

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Acyl-coA Binding Protein neutralization improves cancer immunosurveillance

Project description:The plasma concentrations of acyl coenzyme A binding protein (ACBP, also known as diazepam-binding inhibitor, DBI, or ‘endozepine’) increase with age and obesity, two parameters that are also the most important risk factors for cancer. In mice bearing MCA205 fibrosarcoma, antibody mediated ACBP/DBI neutralization enhanced the anticancer T-cell response in the context of chemoimmunotherapy. T-cells infiltrating MCA205 tumors were sorted and submitting to single-cell TCR sequencing and single-cell RNA sequencing (scRNAseq) to identify the mechanisms driving this improvement.

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Arabidopsis thaliana SWATH-MS - Overexpression of a Monocot Acyl-CoA-Binding Protein Confers Broad-Spectrum Pathogen Protection in a Dicot

Project description:Plants are continuously infected by various pathogens throughout their lifecycle. Previous studies have reported that the expression of Class III acyl-CoA-binding proteins (ACBPs) such as the Arabidopsis ACBP3 and rice ACBP5 were induced by pathogen infection. Transgenic Arabidopsis AtACBP3-overexpressors (AtACBP3-OEs) displayed enhanced protection against the bacterial biotroph, Pseudomonas syringae, although they became susceptible to the fungal necrotroph Botrytis cinerea. A Class III ACBP from a monocot, rice (Oryza sativa) OsACBP5 was overexpressed in the dicot Arabidopsis. The resultant transgenic Arabidopsis lines conferred resistance not only to the bacterial biotroph P. syringae but to fungal necrotrophs (Rhizoctonia solani, B. cinerea, Alternaria brassicicola) and a hemibiotroph, (Colletotrichum siamense). Changes in protein expression in R. solani-infected Arabidopsis OsACBP5-overexpressors (OsACBP5-OEs) were demonstrated using proteomic analysis. Biotic stress-related proteins including cell wall-related proteins such as FASCILIN-LIKE ARABINOGALACTAN-PROTEIN10, LEUCINE-RICH REPEAT EXTENSIN-LIKE PROTEINS, XYLOGLUCAN ENDOTRANSGLUCOSYLASE/HYDROLASE PROTEIN4 and PECTINESTERASE INHIBITOR18; proteins associated with glucosinolate degradation including GDSL-LIKE LIPASE23, EPITHIOSPECIFIER MODIFIER1, MYROSINASE1, MYROSINASE2 and NITRILASE1; as well as a protein involved in jasmonate biosynthesis, ALLENE OXIDE CYCLASE2, were induced in OsACBP5-OEs upon R. solani infection. These results indicated that upregulation of these proteins in OsACBP5-OEs conferred protection against various plant pathogens.

2019-05-10 | PXD013031 | Pride

A class of reactive acyl-CoA species reveals the nonenzymatic origins of protein acylation

Project description:The mechanisms underlying the formation of acyl protein modifications remain poorly understood. By investigating the reactivity of endogenous acyl-CoA metabolites, we found a class of acyl-CoAs that undergoes intramolecular catalysis to form reactive intermediates which non-enzymatically modify proteins. Based on this mechanism, we predicted, validated, and characterized the protein modification: 3-hydroxy-3-methylglutaryl(HMG)-lysine. In a model of altered HMG-CoA metabolism, we found evidence of two additional protein modifications: 3-methylglutaconyl(MGc)-lysine and 3-methylglutaryl(MG)-lysine. Using quantitative proteomics, we compared the ‘acylomes’ of two reactive acyl-CoA species, namely HMG-CoA and glutaryl-CoA, which are generated in different pathways. We found proteins that are uniquely modified by each reactive metabolite, as well as common proteins and pathways. We identified the tricarboxylic acid cycle as a pathway commonly regulated by acylation, and validated malate dehydrogenase as a key target. These data identify a fundamental relationship between reactive acyl-CoA species and proteins, and define a new regulatory paradigm in metabolism.

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Project description:Acyl-CoAs are essential for life. These metabolites serve as fundamental cellular building blocks in the biosynthesis of lipids, intermediates in energy production via the TCA cycle, and essential precursors for reversible protein acetylation. Each of these roles are dependent on acyl-CoA/protein interactions, physical contacts that can regulate protein function via a variety of mechanisms. We utilized systems-level analyses to characterize novel protein networks that interact with metabolic acyl-CoAs, and evaluate the potential of these interactions to facilitate enzyme activity or non-enzymatic acylation. Our studies provide a roadmap for integrating chemoproteomic data with systems biology analysis, and establish a novel resource for understanding the diverse signaling roles of acyl-CoAs in biology and disease.

2019-11-21 | PXD013157 | Pride

Acyl CoA binding protein as a potential driver of pathological aging.

Project description:Acyl CoA binding protein as a potential driver of pathological aging.

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Carboxyltransferase Subunit of the Acyl-CoA Carboxylase in Mycobacterium tuberculosis.

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2006-10-07 | GSE5977 | GEO

Response of Arabidopsis thaliana seedlings to acyl-CoAs

Project description:Floodings already have a nearly 60% share in the worldwide damage to crops provoked by natural disasters. Climate change will cause plants to be even more frequently exposed to oxygen limiting conditions (hypoxia) in the near future due to heavy precipitation and concomitant waterlogging or flooding events in large areas of the world. Although the homeostatic regulation of adaptive responses to low oxygen stress in plants is well described, it remained unknown by which initial trigger the molecular response to low-oxygen stress is activated. Here, we show that a hypoxia-induced decline of the ATP level of the cell reduces LONG-CHAIN ACYL-COA SYNTHETASE (LACS) activity, which leads to a shift in the composition of the acyl-CoA pool. High oleoyl-CoA levels release the transcription factor RELATED TO APETALA 2.12 (RAP2.12) from its interaction partner ACYL-COA BINDING PROTEIN (ACBP) at the plasma membrane to induce low oxygen-specific gene expression. We show that different acyl-CoAs provoke unique molecular responses revealing a novel role as cellular signalling component also in plants. In terms of hypoxia signalling, dynamic acyl-CoA levels integrate the cellular energy status into the oxygen signalling cascade with ACBP and RAP2.12 being the central hub. The conserved nature of the ACBP:RAP2.12 module in crops and the novel mechanistic understanding of how low-oxygen stress responses are initiated by oleoyl-CoA in plants provide useful leads for enhancing future food security.

2018-04-30 | GSE97186 | GEO

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