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Transcriptional contribution of nuclear lamina protein emerin and BAF in Drosophila ovaries

ABSTRACT: Transcriptional contribution of nuclear lamina protein emerin and BAF in Drosophila ovaries

PROVIDER: PRJNA705972 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR13827131.fastq.gz	Fastqsanger.gz
	SRR13827132.fastq.gz	Fastqsanger.gz
	SRR13827133_1.fastq.gz	Fastqsanger.gz
	SRR13827133_2.fastq.gz	Fastqsanger.gz
	SRR13827134_1.fastq.gz	Fastqsanger.gz

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Transcriptional contribution of nuclear lamina protein emerin and BAF in Drosophila ovaries

Project description:Nuclear lamina (NL) contributes to tissue homeostasis. In Drosophila, compromised NL blocks differentiation and causes loss of germline stem cells (GSCs) due to activation of the Chk2 checkpoint kinase. Checkpoint activation occurs upon loss of the NL protein Drosophila emerin or its partner Barrier-to-autointegration factor (BAF). As NL has long been thought to interact with specific genomic loci and regulate transcription, we examined transcriptional changes in emerin-/- and baf KD ovaries. We found thousands of genes are mis-regulated upon loss of emerin or BAF in GSCs. Remarkably, more than 90% of mis-regulated genes are shared between emerin-/- and baf KD. Finally, we show that transcriptional changes are downstream of Chk2 activation, as transcription are restored in chk2, emerin double mutant ovaries.

2021-12-01 | GSE168062 | GEO

Stochastic genome-nuclear lamina interactions: Modulating roles of Lamin A and BAF

Project description:The nuclear lamina (NL) is a filamentous layer lining the inner-nuclear-membrane (INM) that aids in the organization of the genome in large domains of low transcriptional activity. Recently, it was shown that the single-cell genome-NL interactions are much more dynamic than previously anticipated, which challenges the concept of the NL as a safe guard for transcriptional repressed genes. Here we discuss the role of the NL in light of these new findings and introduce Lamin A and BAF as potential modulators of LAD positioning BAF-chromatin and Lamin B2-chromatin interactions were assayed in human HT1080 by DamID on Nimblegen microarrays, with two biological replicates each, that were hybridized in a dye-swap design.

2014-02-15 | E-GEOD-55066 | biostudies-arrayexpress

Mechanical-biochemical signaling accelerates scleral remodeling in myopia via the LaminA/C-Emerin-MKL1 axis

Project description:Scleral remodeling is the pathological basis of axial elongation during the progression of myopia. However, the mechanism underlying the onset and progression of scleral remodeling remains unclear. Here, based on reanalysis of single-cell RNA sequencing data, we showed that aberrant biomechanics in the sclera serve as signals that promote extracellular matrix (ECM) remodeling during the development of myopia via LaminA/C-Emerin-MKL1 axis, and followed by a decrease in collagen synthesis in scleral fibroblasts. Mice with lens-induced myopia (LIM) and guinea pigs with form-deprivation myopia (FDM) exhibited nuclear deformation and dysregulation of nuclear envelope (NE) proteins in sclera. We established a mechanical model to investigate the role of matrix stiffness in regulating collagen synthesis in human primary scleral fibroblasts. In contrast to stiff substrates, soft matrix attenuated the sequestration of LaminA/C and Emerin in the NE and impaired MKL1 nuclear accumulation and COL1A1 transcription. Interventions for MKL1 induced or inhibited the progression of myopia in vivo. We illustrate the therapeutic potential of a novel mechanointerference strategy that blocks scleral remodeling and myopia progression.

2026-06-03 | GSE316874 | GEO

Identification of PP2A-B55 targets in Drosophila uncovers regulation of Emerin during nuclear envelope reassembly

Project description:Entry into mitosis is triggered by mitotic kinases that phosphorylate multiple proteins to induce profound cellular changes including nuclear envelope breakdown, chromosome condensation and spindle assembly. Conversely, mitotic exit requires protein dephosphorylation as cells return to their interphase organization. Protein Phosphatase 2A in complex with its B55/Tws regulatory subunit (PP2A-B55) is known to play a crucial role in this transition. However, the precise events and substrates that it regulates are incompletely understood. We used proteomic approaches in Drosophila to identify proteins that interact with PP2A-B55 and are dephosphorylated in a PP2A-B55 dependent manner. Among several candidates, we identified Otefin (also known as Emerin) as a target of PP2A-B55 in the process of nuclear envelope reformation after mitosis. Emerin is a protein of the inner nuclear membrane that interacts with the DNA-binding protein Barrier-to-Autointegration Factor (BAF) via a LEM domain. Our results indicate that phosphorylation of Emerin at Ser50 and Ser54 near its LEM domain negatively regulates its association with BAF, Lamin and additional Emerin. Using live imaging, we show that dephosphorylation of Emerin at the identified sites determines the timing of nuclear envelope reformation. Genetic rescue experiments indicate that this regulation is required in vivo during embryonic development. Phosphoregulation of the Emerin-BAF complex formation by PP2A-B55 appears as a key event of mitotic exit that is likely to be conserved across species.

2023-08-10 | PXD041091 | Pride

Identification of PP2A-B55 targets in Drosophila uncovers regulation of Emerin during nuclear envelope reassembly

2023-08-10 | PXD041030 | Pride

Identification of PP2A-B55 targets in Drosophila uncovers regulation of Emerin during nuclear envelope reassembly

2023-08-10 | PXD041032 | Pride

The molecular basis of emerin-emerin and emerin-BAF interactions.

Project description: Not available

| S-EPMC4163644 | biostudies-literature

Mechanical-biochemical signaling accelerates scleral remodeling in myopia via the LaminA/C-Emerin-MKL1 axis

Project description:Mechanical-biochemical signaling accelerates scleral remodeling in myopia via the LaminA/C-Emerin-MKL1 axis

| PRJNA1405473 | ENA

Stochastic genome-nuclear lamina interactions: Modulating roles of Lamin A and BAF

2014-02-15 | GSE55066 | GEO

EDMD-causing emerin mutant myogenic progenitors exhibit impaired differentiation using similar mechanisms

Project description:RNA sequencing was performed on proliferating and differentiating emerin-null myogenic progenitors expressing emerin and EDMD-causing emerin mutants to identify molecular pathways implicated in Emery-Dreifuss Muscular Dystrophy.

2020-07-01 | GSE152226 | GEO

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