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Bat3 regulates T cell terminal differentiation in an mTORC2-dependent manner

ABSTRACT: Bat3 regulates T cell terminal differentiation in an mTORC2-dependent manner

PROVIDER: PRJNA707416 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR13884491_1.fastq.gz	Fastqsanger.gz
	SRR13884491_2.fastq.gz	Fastqsanger.gz
	SRR13884492_1.fastq.gz	Fastqsanger.gz
	SRR13884492_2.fastq.gz	Fastqsanger.gz
	SRR13884493_1.fastq.gz	Fastqsanger.gz

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Bat3 regulates T cell terminal differentiation in an mTORC2-dependent manner

Project description:Human leukocyte antigen B (HLA-B)-associated transcript 3 (Bat3), also called Bcl-2-associated athanogene 6 (BAG6), is a multifunctional adapter protein that was previously shown to bind to the cytoplasmic tail of the checkpoint inhibitor Tim-3 and inhibit its downstream signaling pathway. Using mouse genetic models, we now demonstrate that deficiency of Bat3 selectively in T cells elicits a profound exhaustion phenotype and dampens autoreactive T cell-mediated neuroinflammation. Mechanistically, Bat3 acts as a critical mTORC2 inhibitor to suppress Akt function. As a result, Bat3 deficiency leads to increased Akt activity, and FOXO1 phosphorylation, indirectly promoting Prdm1. Transcriptional analysis of myelin antigen-specific CNS-infiltrating Bat3 deficient CD4 T cells revealed upregulation of dysfunction-associated genes concomitant with downregulation of genes associated with T cell effector function. Genes upregulated in Bat3cko T cells were significantly enriched for Prdm1(BLIMP1) and exhaustion gene signatures suggesting the absence of Bat3 can trigger T cell dysfunction even under highly inflammatory autoimmune conditions. Taken together, in this paper we identify a novel mechanism by which Bat3 not only directly suppresses Tim-3 signaling, but also plays a critical role in controlling the mTORC2-Akt-Blimp-1 pathway thereby suppressing the induction of the co-inhibitory module and preventing terminal differentiation and dysfunction of T cells.

2021-04-30 | GSE168435 | GEO

Chaperone dependent coordination of nutrient sensing and energy metabolism by mTORC2

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Epigenome analysis of control and mTORC2-suppressed glioblastoma cells

Project description:Genome wide DNA methylation profiling of control and mTORC2-suppressed glioblastoma cells (U87-EGFRvIII cells). The Illumina Infinium HumanMethylation EPIC BeadChip Array was used to obtain DNA methylation profiles with 865,918 probes in glioblastoma cell line samples. Samples included 2 control U87-MG cells without mTORC2 suppresion, and mTORC2-knockdown U87-MG cells with lentivirus-mediated suppression of mTORC2.

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screen miRNAs specifically regulated by mTORC1 or mTORC2

Project description:To screen miRNAs specifically regulated by mTORC1 or mTORC2, a global miRNA expression profile in MCF-7 cells treated with rapamycin or PP242 (mTORC1/2 kinase inhibitor) was developed using microarray. control, rapamycin or PP242 treated human MCF-7 cells were harvested 48h post-treatment and subjected to total RNA extraction.

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Next Generation Sequencing Facilitates Quantitative Analysis of Wild Type and Bat3-/- BMDC Transcriptomes III

Project description:Purpose: Next-generation sequencing (NGS) has revolutionized systems-based analysis of cellular pathways. The goals of this study are to compare NGS-derived WT or Bat3 KO BMDC transcriptome profiling (RNA-seq) to microarray and quantitative reverse transcription polymerase chain reaction (qRT–PCR) methods and to evaluate protocols for optimal high-throughput data analysis

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Project description:Mutations in cancer reprogram amino acid metabolism to drive tumor growth, but the molecular mechanisms are not well understood. Using an unbiased proteomic screen, we identified mTORC2 as a critical regulator of amino acid metabolism in cancer via phosphorylation of the cystine-glutamate antiporter xCT. mTORC2 phosphorylates serine 26 at the cytosolic N-terminus of xCT, inhibiting its activity. Genetic inhibition of mTORC2, or pharmacologic mTOR kinase inhibition, promotes glutamate secretion, cystine uptake and incorporation into glutathione linking growth factor receptor signaling with amino acid uptake and utilization. These results identify an unanticipated mechanism of amino acid metabolic reprogramming in cancer, enabling tumor cells to adapt to changing environmental conditions.

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HLA-B-associated transcript 3 (Bat3) stabilizes and activates p53 in a HAUSP-dependent manner.

Project description:The p53 pathway is a highly complex signaling network including several key regulators. HAUSP is a critical component of the p53 pathway acting as a deubiquitinase for both p53 and its key repressor Mdm2. Here, we identified a novel HAUSP-interacting protein, HLA-B-associated transcript 3 (Bat3) and found it to be capable of inducing p53 stabilization and activation via a HAUSP-dependent mechanism, resulting in cell growth inhibition. Surprisingly, the deubiquitylating enzymatic activity of HAUSP was not required for this phenomenon. Co-immunoprecipitation showed that p53 coexisted in a complex with Bat3 and HAUSP in vivo, and HAUSP may serve as a binding mediator to enhance the interaction between p53 and Bat3. Further studies revealed that formation of this three-protein complex interfered with the binding of p53 to its proteasome receptor S5a and promoted the accumulation of p53 in nucleus. Notably, Mdm2 protein abundance is also regulated by Bat3 in the presence of HAUSP. Overexpression of Bat3 and HAUSP increases Mdm2 protein levels without influencing the p53-Mdm2 interaction and Mdm2-mediated p53 ubiquitination, indicating that Bat3-HAUSP-mediated protein stabilization is not specific to p53 and different mechanisms may be involved in Bat3-mediated regulation of p53-Mdm2 pathway. Together, our study unravels a novel mechanism by which p53 is stabilized and activated by HAUSP-mediated interaction with Bat3 and implies that Bat3 might function as a tumor suppressor through the stabilization of p53.

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mTORC2-mediated cell-cell interaction promote BMP4-induced WNT activation and mesoderm differentiation

Project description:The mechanistic target of rapamycin complex 2 (mTORC2) is essential for embryonic development but the underlying molecular mechanisms remain unclear. Here we show that disruption of mTORC2 in human embryonic stem cells (hESCs) considerably alters the balance of Rho/Rac signaling and reduces cell adhesion. Although these changes have no clear effect on their self-renewal and the expression of pluripotent markers, they significantly impede BMP-induced activation of canonical WNT genes, leading to impaired mesendoderm differentiation. Direct activation of the downstream WNT pathway by inhibiting GSK3 dramatically improves mesendoderm differentiation in mTORC2-deficient hESCs. Our studies uncover a new mechanism by which mTORC2 regulates cell fate determination and link the intercellular contacts with the activation of WNT genes.

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Project description:We herein demonstrate that mammalian target of rapamycin complex 2 (mTORC2), a critical core component of the growth factor signaling system, globally alters histone acetylation through metabolic reprogramming in the highly malignant brain tumor glioblastoma (GBM). Integrated analyses unravel that mTORC2 regulates iron trafficking via histone H3K9 acetylation of the ferritin promoter, facilitating GBM growth and survival. These findings nominate mTORC2 as a critical epigenetic regulator of iron metabolism in cancer.

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