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Adhesion GPCR ADGRE2 maintains proteostasis to promote progression in acute myeloid leukemia

ABSTRACT: Adhesion GPCR ADGRE2 maintains proteostasis to promote progression in acute myeloid leukemia

PROVIDER: PRJNA1087687 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR28341933_1.fastq.gz	Fastqsanger.gz
	SRR28341933_2.fastq.gz	Fastqsanger.gz
	SRR28341934_1.fastq.gz	Fastqsanger.gz
	SRR28341934_2.fastq.gz	Fastqsanger.gz
	SRR28341935_1.fastq.gz	Fastqsanger.gz

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Adhesion GPCR ADGRE2 maintains proteostasis to promote progression in acute myeloid leukemia

Project description:Acute myeloid leukemia (AML) is an aggressive and heterogenous hematological malignancy. In elderly patients, AML incidence is high and has a poor prognosis due to a lack of effective therapies. G-protein coupled receptors (GPCRs) play integral roles in physiological processes and human diseases. Particularly, one-third of adhesion GPCRs, the second largest group of GPCRs, are highly expressed in hematopoietic stem and progenitor cells or lineage cells. Therefore, we investigated the role of adhesion GPCRs in AML and whether they could be harnessed as anti-leukemia targets. Systematic screening of the impact of adhesion GPCRs on AML functionality by combined bioinformatic and functional analyses revealed high expression of ADGRE2 in AML, particularly in leukemic stem cells (LSCs), which was associated with poor patient outcomes. Silencing ADGRE2 not only exerted anti-leukemia effects in AML cell lines and AML patient-derived cells in vitro but also delayed AML progression in xenograft models in vivo. Mechanistically, ADGRE2 activated PLC-β/PKC/MEK/ERK signaling to enhance expression of AP-1 and transcriptionally drive expression of DUSP1, a protein phosphatase. DUSP1 de-phosphorylated Ser16 in the J-domain of the co-chaperone DNAJB1, which facilitated DNAJB1-HSP70 interaction and maintenance of proteostasis in AML. Finally, combined inhibition of MEK, AP-1, and DUSP1 exhibited robust therapeutic efficacy in AML xenograft mouse models. Collectively, this study deciphers the roles and mechanisms of ADGRE2 in AML and provides a promising therapeutic strategy for treating AML.

2024-03-19 | GSE261574 | GEO

The Adhesion GPCR ADGRL2 engages Galpha13 to Enable Epidermal Differentiation

Project description:The Adhesion GPCR ADGRL2 engages Galpha13 to Enable Epidermal Differentiation

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The Adhesion GPCR ADGRL2 engages Galpha13 to Enable Epidermal Differentiation

Project description:The Adhesion GPCR ADGRL2 engages Galpha13 to Enable Epidermal Differentiation

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A Neuronal GPCR Modifies Neuropeptide Signaling to Suppress Proteostasis in distal tissues

Project description:The proteostasis network (PN) safeguards the integrity of proteins by the promotion of various cellular activities. However, with aging the competence of the PN declines and aggregated proteins accrue within cells. This process can underlie the development of neurodegenerative disorders, such as Alzheimer’s and Huntington’s diseases. Although the activities of the PN occur within the cell, this network is regulated across the organism by inter-tissue communication, which is partially governed by neurons. We discovered previously, that reducing the expression of gtr-1, which encodes a neuronal GPCR, protects worms from the toxicity of the Alzheimer’s-causing, Aβ peptide. Here we investigated the mechanism that is acted upon the knockdown of gtr-1 and found that gtr-1 RNAi treatment modulates the expression of neuropeptide-coding genes, differentially modifies the aggregation of proteotoxic proteins, and enhances protein degradation. These findings highlight the roles of neuropeptides as coordinators of proteostasis across the organism.

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Project description:A Neuronal GPCR Modifies Neuropeptide Signaling to Suppress Proteostasis in distal tissues

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