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E3 ubiquitin ligase FBXO38 maintains antitumor function of NK cells through sustaining IL-15R signaling

ABSTRACT: E3 ubiquitin ligase FBXO38 maintains antitumor function of NK cells through sustaining IL-15R signaling

PROVIDER: PRJNA1068084 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR27697631_1.fastq.gz	Fastqsanger.gz
	SRR27697631_2.fastq.gz	Fastqsanger.gz
	SRR27697632_1.fastq.gz	Fastqsanger.gz
	SRR27697632_2.fastq.gz	Fastqsanger.gz
	SRR27697633_1.fastq.gz	Fastqsanger.gz

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E3 ubiquitin ligase FBXO38 maintains antitumor function of NK cells through sustaining IL-15R signaling

Project description:Natural killer (NK) cells are the main innate antitumor effector cells and can be constrained in the tumor microenvironment (TME). It has been reported that E3 ligase FBXO38 accelerates PD-1 degradation of tumor-infiltrating T cells to unleash their cytotoxic function. In this study, we found that FBXO38 transcripts were significantly lower in intra-tumoral NK cells than in peri-tumoral regions using specimens from cancer patients in The Cancer Genome Atlas (TCGA). Conditional knock-out (cKO) of FBXO38 in NK cells accelerated tumor growth and increased tumor metastasis. However, FBXO38 deficiency did not show an effect on the cytotoxic function of tumor-infiltrating NK (TINK) cells, but decreased proliferation and survival of TINK cells. Mechanically, FBXO38 deficiency led to TINK cell hyporesponsiveness to IL-15 by reducing the expression of IL-15Rβ and IL-15Rγc, which accounted for the reduced expansion of FBXO38-deficient TINK cells in TME. Furthermore, human NK-92 cells proliferated more rapidly when FBXO38 was overexpressed and exerted greater antitumor efficacy in xenograft mouse models. Conversely, the removal of FBXO38 led to a dramatic decrease in NK-92 cell proliferation. In conclusion, our results suggest that FBXO38 strongly sustains NK cell expansion in the antitumor immunity response.

2024-01-31 | GSE253993 | GEO

Regulation of metablism by mitochondrial MUL1 E3 ubiquitin ligase

Project description:Regulation of metablism by mitochondrial MUL1 E3 ubiquitin ligase

| PRJNA832764 | ENA

E3 ubiquitin ligase Rfwd2 inactivation effect on embryonic lung development

Project description:Transcriptome analysis by RNA-seq of lungs from control and Rfwd2 epithelial-specific conditional knockout mice at embryonic 13.5 day age. RFWD2, is an E3 ubiquitin ligase that modifies specific target proteins, priming their degradation via the ubiquitin proteasome system. Rfwd2 deficiency led to a striking halt in branching morphogenesis shortly after secondary branch formation. In the mutant lung, two ETS transcript factors essential for normal lung branching, ETV4 and ETV5, were upregulated at the protein, but not transcript level. Introduction of Etv loss-of-function alleles into the Rfwd2 mutant background attenuated the branching phenotype, suggesting that RFWD2 functions at least in part through degrading ETV proteins. As a number of E3 ligases are known to target factors important for lung development, our findings provides a preview of a protein-level regulatory network essential for lung branching morphogenesis.

2016-04-28 | GSE80707 | GEO

The E3 ubiquitin ligase Siah1 regulates adrenal gland organization and hyperaldosteronism

Project description:Primary and secondary hypertension are major risk factors for cardiovascular disease. Elevated secretion of aldosterone resulting from primary aldosteronism (PA) is a key driver of secondary hypertension. Here, we identify an unexpected role for the ubiquitin ligase Siah1 in adrenal gland development and PA. Siah1a-/- mice exhibit altered adrenal gland morphology, as reflected by dysregulated zonation of the glomerulosa, increased aldosterone levels and aldosterone target gene expression, and reduced plasma potassium levels. Genes involved in catecholamine biosynthesis and cAMP signaling are upregulated in the adrenal glands of Siah1a-/- mice, while genes related to retinoic acid signaling and cholesterol biosynthesis are downregulated. Loss of Siah1 leads to increased expression of PIAS1, an E3 SUMO-protein ligase implicated in the suppression of LXR. Notably, SIAH1 sequence variants which impaired SIAH1 ubiquitin ligase activity, resulting in elevated PIAS1 expression, were identified in patients with PA. The involvement of Siah1–PIAS1 in adrenal gland organization and function points to a possible new therapeutic target for hyperaldosteronism.

2018-05-01 | GSE102963 | GEO

Interactions between Yeast Proteins and Rsp5 Ubiquitin Ligase

Project description:To identify substrates of the ubiquitinating E3 enzyme Rsp5 we applied purified Rsp5 to duplicate protein arrays. The Rsp proteins were expressed as fusion proteins to GST. We used as a control Ubr1, a RING domain containing E3 ligase We analyzed Rsp5 from S.cerevisiae on duplicate arrays, with four control chips, two without Rsp5 and two with Ubr1.

2008-12-30 | E-GEOD-14218 | biostudies-arrayexpress

The E3 ubiquitin ligase HectD1 suppresses EMT and metastasis by targeting the +TIP protein ACF7 for degradation

Project description:Cancer cells exploit the epithelial-to-mesenchymal transition (EMT) program toward metastasis. Cytoskeletal regulators are dually required in mesenchymal cells by promoting EMT-induced migration and sustaining the EMT program itself. In search for novel regulators of metastasis, we conducted an shRNA screen targeting a class of microtubule regulators, the plus-end tracking proteins (+TIPs). We show that the +TIP ACF7 is required for both the maintenance of EMT and to promote migration. We identified HectD1 as a potent E3 ubiquitin ligase mediating ACF7 degradation. Depletion of HectD1 robustly increases ACF7 protein levels and this is sufficient to enhance migration and EMT in cells, as well as facilitate metastasis in vivo. Ours results report the HectD1/ACF7 axis as a novel regulator of metastasis of breast cancer cells.

2018-01-03 | GSE100092 | GEO

Merlin/NF2 Suppresses Tumorigenesis by Inhibiting the E3 Ubiquitin Ligase CRL4DCAF1 in the Nucleus

Project description:Current models imply that the FERM domain protein Merlin, encoded by the tumor suppressor NF2, inhibits mitogenic signaling at or near the plasma membrane. Here, we show that the closed, growth inhibitory form of Merlin accumulates in the nucleus, binds to the E3 ubiquitin ligase CRL4DCAF1, and suppresses its activity. Depletion of DCAF1 blocks the promitogenic effect of inactivation of Merlin. Conversely, enforced expression of a Merlin-insensitive mutant of DCAF1 counteracts the antimitogenic effect of Merlin. Re-expression of Merlin and silencing of DCAF1 induce a similar, tumor-suppressive program of gene expression. Tumor-derived mutations invariably disrupt Merlinâs ability to interact with or inhibit CRL4DCAF1. Finally, depletion of DCAF1 inhibits the hyperproliferation of Schwannoma cells from NF2 patients and suppresses the oncogenic potential of Merlin-deficient tumor cell lines. We propose that Merlin suppresses tumorigenesis by translocating to the nucleus to inhibit CRL4DCAF1. To examine if Merlin controls gene expression through inhibition of CRL4DCAF1, and define the general function of this ligase, we compared the gene expression program activated by expression of Merlin or by depletion of DCAF1 in Merlin-null FC-1801 mouse Schwannoma cells

2010-03-09 | E-GEOD-19305 | biostudies-arrayexpress

The E3 Ubiquitin Ligase AFF1 targets ARF19 to the proteasome

Project description:The E3 Ubiquitin Ligase AFF1 targets ARF19 to the proteasome

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EGFR is a target of the tumor suppressor E3-ligase FBXW7

Project description:FBXW7 is and E3 ubiquitin ligase and is highly mutated in colorectal cancer. We used human colon organoids with engineered FBXW7 hotspot mutations to investigate novel targets of E3 ligase activity with a combined transcriptomic and proteomic approach uncovering the EGFR-MAPK pathway as highly regulated by the E3 ligase activity.

2024-04-03 | GSE246896 | GEO

The E3 Ubiquitin Ligase AFF1 targets ARF19 to the proteasome

Project description:Auxin critically regulates nearly every aspect of plant growth and development. Auxin-driven transcriptional responses are mediated through the AUXIN RESPONSE FACTOR (ARF) family of transcription factors. Although ARF protein stability is regulated via the 26S proteasome, molecular mechanisms underlying ARF stability and turnover are unknown. Here, we report the identification and functional characterization of an F-Box E3 ubiquitin ligase, which we have named AUXIN RESPONSE FACTOR F-BOX1 (AFF1). AFF1 directly interacts with ARF19 and regulates its accumulation. Mutants defective in AFF1 display ARF19 protein hyperaccumulation, mild auxin resistance, and developmental defects. Together, our data suggest a new mechanism, namely control of ARF protein stability, in regulating auxin responsiveness.

2022-06-09 | GSE172353 | GEO

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