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Angel2 phosphatase activity is required for non-canonical mitochondrial RNA processing in metazoa

ABSTRACT: Angel2 phosphatase activity is required for non-canonical mitochondrial RNA processing in metazoa

PROVIDER: PRJNA784409 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR17062619_1.fastq.gz	Fastqsanger.gz
	SRR17062619_2.fastq.gz	Fastqsanger.gz
	SRR17062620_1.fastq.gz	Fastqsanger.gz
	SRR17062620_2.fastq.gz	Fastqsanger.gz
	SRR17062621_1.fastq.gz	Fastqsanger.gz

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Angel2 phosphatase activity is required for non-canonical mitochondrial RNA processing in metazoa

Project description:Canonical RNA processing in mammalian mitochondria necessitates that tRNAs are recognised by nucleases to release flanking transcripts. However, not all mitochondrial transcripts are punctuated by tRNAs, and the mechanism and factors involved in their processing has remained unsolved. Here, we demonstrate that phosphatase activity of the carbon catabolite repressor 4 domain containing family member ANGEL2 is required for the hydrolysis of 3′ phosphates, resulting from non-canonical processing. Interaction studies in Drosophila further identify that members of the FAST kinase domain containing protein family are involved in the formation of these 3′ phosphates. Our results therefore resolve the mechanism of RNA processing in metazoan mitochondria, by defining the outstanding non-canonical processing mechanism.

2022-09-04 | GSE189750 | GEO

Angel2 phosphatase activity is required for non-canonical mitochondrial RNA processing

Project description:Canonical RNA processing in mammalian mitochondria is defined by tRNAs acting as recognition sites for nucleases to release flanking transcripts. The relevant factors, their structures, and mechanism are well described, but not all mitochondrial transcripts are punctuated by tRNAs, and their mode of processing has remained unsolved. Using Drosophila and mouse models, we demonstrate that non-canonical processing results in the formation of 3′ phosphates, and that phosphatase activity by the carbon catabolite repressor 4 domain-containing family member ANGEL2 is required for their hydrolysis. Furthermore, our data suggest that members of the FAST kinase domain-containing protein family are responsible for these 3′ phosphates. Our results therefore resolve the mechanism of non-canonical RNA processing in metazoan mitochondria, by defining the role of ANGEL2.

2022-09-01 | PXD033394 | Pride

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ANGEL2 phosphatase activity is required for non-canonical mitochondrial RNA processing.

Project description:Canonical RNA processing in mammalian mitochondria is defined by tRNAs acting as recognition sites for nucleases to release flanking transcripts. The relevant factors, their structures, and mechanism are well described, but not all mitochondrial transcripts are punctuated by tRNAs, and their mode of processing has remained unsolved. Using Drosophila and mouse models, we demonstrate that non-canonical processing results in the formation of 3' phosphates, and that phosphatase activity by the carbon catabolite repressor 4 domain-containing family member ANGEL2 is required for their hydrolysis. Furthermore, our data suggest that members of the FAST kinase domain-containing protein family are responsible for these 3' phosphates. Our results therefore propose a mechanism for non-canonical RNA processing in metazoan mitochondria, by identifying the role of ANGEL2.

| S-EPMC9525292 | biostudies-literature

marine Metazoa environmental sample

Project description:marine Metazoa environmental sample overview

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Hmga2 is required for canonical WNT signaling during lung development

Project description:The high-mobility-group (HMG) proteins are the most abundant non-histone chromatin-associated proteins. Here we deciphered the role of the high mobility group AT-hook protein 2 (HMGA2) during lung development by analyzing the lung of Hmga2 deficient mice (Hmga2-/-).We found that Hmga2 is expressed in the mouse embryonic lung at the distal airways. Analysis of Hmga2-/- mice showed that Hmga2 is required for proper cell proliferation and distal epithelium differentiation during embryonic lung development. Hmga2 knockout (KO) led to enhanced canonical WNT signaling due to an increased expression of secreted WNT glycoproteins Wnt2b, Wnt7b and Wnt11 as well as a reduction of the WNT signaling antagonizing proteins GATA6 (GATA binding protein 6) and FZD2 (frizzled homolog 2). Comparison of Hmga2-/- with Hmga2+/+ mice by Affymetrix microarray-based expression analysis of embryonic lung revealed an increased expression of genes whose products participate in cell cycle and canonical Wnt signaling. Affymetrix microarray transcriptome analysis of Hmga2-/- and Hmga2+/+ embryonic lung (E18.5) was performed and analyzed

2014-03-07 | E-GEOD-55340 | biostudies-arrayexpress

The Protein Phosphatase 4 Complex Promotes Transcription and Processing of Primary microRNAs in Arabidopsis

Project description:The Protein Phosphatase 4 Complex Promotes Transcription and Processing of Primary microRNAs in Arabidopsis

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The Protein Phosphatase 4 Complex Promotes Transcription and Processing of Primary microRNAs in Arabidopsis [ncRNA-Seq]

Project description:Protein phosphatase 4 (PP4) is a highly conserved serine/threonine protein phosphatase in yeast, plants, and animals. The composition and functions of the plant PP4 are poorly understood. Here, we uncovered previously unsuspected complexity of Arabidopsis PP4 and identified the composition of one form of PP4 containing the regulatory subunit PP4R3A. We showed that PP4R3A, together with one of two redundant catalytic subunit genes PPX1 and PPX2, promotes the biogenesis of microRNAs. PP4R3A is a chromatin-associated protein, interacts with RNA polymerase II (Pol II), and recruits Pol II to the promoters of MIR genes to promote their transcription. PP4R3A probably also promotes the cotranscriptional processing of miRNA precursors as it recruits the microprocessor component HYPONASTIC LEAVES1 (HYL1) to MIR genes and nuclear dicing bodies. Moreover, we showed that hundreds of introns exhibit splicing defects in pp4r3a mutants. Together, this study revealed a role of Arabidopsis PP4 in transcription and nuclear RNA metabolism.

2019-02-08 | GSE121453 | GEO

The Protein Phosphatase 4 Complex Promotes Transcription and Processing of Primary microRNAs in Arabidopsis [RNA-Seq]

2019-02-08 | GSE121450 | GEO

PTEN phosphatase inhibits metastasis

Project description:PTEN encodes a tumor suppressor with lipid and protein phosphatase activities whose dysfunction has been implicated in melanomagenesis; less is known about how its phosphatases regulate melanoma metastasis. We show that PTEN expression negatively correlates with metastatic progression in human melanoma samples and a PTEN-deficient mouse melanoma model. Wildtype PTEN expression inhibited melanoma cell invasiveness and metastasis in a dose-dependent manner, behaviors that specifically required PTEN protein phosphatase activity. PTEN phosphatase activity regulated metastasis through Entpd5. Entpd5 knockdown reduced metastasis and IGF1R levels while promoting ER stress. In contrast, Entpd5 overexpression promoted metastasis and enhanced IGF1R levels, while reducing ER stress. Moreover, Entpd5 expression was regulated by the ER stress sensor ATF6. Altogether, our data show that PTEN phosphatase activity inhibits metastasis by negatively regulating the Entpd5/IGF1R pathway through ATF6, thereby identifying novel candidate therapeutic targets for the treatmtreatingwith PTEN mutant melanoma.

2023-03-09 | GSE210359 | GEO

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