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Homo sapiens

ABSTRACT: Splicing activation by Rbfox requires self-aggregation through its tyrosine-rich domain

PROVIDER: PRJNA352682 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR4999980.fastq.gz	Fastqsanger.gz
	SRR4999971.fastq.gz	Fastqsanger.gz
	SRR4999981.fastq.gz	Fastqsanger.gz
	SRR4999972.fastq.gz	Fastqsanger.gz
	SRR4999982.fastq.gz	Fastqsanger.gz

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Rett Syndrome linked to defects in forming the MeCP2/Rbfox/LASR complex in mouse models

Project description:Rett syndrome (RTT) is a severe neurological disorder which is mainly caused by mutations found in the X-linked gene encoding MeCP2. Despite extensive studies, the molecular functions of MeCP2 remain elusive. Here, we report that MeCP2 is a new subunit of a higher-order multiunit protein complex Rbfox/LASR and acts as a scaffold for this splicing complex. Deletion or mutation of MeCP2 leads to defects in forming MeCP2/Rbfox/LASR complex and aberrant alternative pre-mRNA splicing. Our data link RTT to an impaired function of MeCP2 in splicing control through its role in nucleating Rbfox/LASR macromolecule assembly.

2021-08-28 | GSE142716 | GEO

Concentration-dependent regulation by Rbfox enabled by motifs of intermediate affinity

Project description:The Rbfox family of splicing factors regulate alternative splicing during animal development and in disease, impacting thousands of exons in the maturing brain, heart, and muscle. Rbfox proteins have long been known to bind to the RNA sequence GCAUG with high affinity, but just half of Rbfox CLIP peaks contain a GCAUG motif. We incubated recombinant RBFOX2 with over 60,000 mouse and human transcriptomic sequences to reveal significant binding to several moderate-affinity, non-GCAYG sites at a physiologically relevant range of RBFOX concentrations. We find that many of these “secondary motifs” bind Rbfox robustly in cells and that several together can exert regulation comparable to a GCAUG in a trichromatic splicing reporter assay. Furthermore, secondary motifs regulate RNA splicing in neuronal development and in neuronal subtypes where cellular Rbfox concentrations are highest, enabling a second wave of splicing changes as Rbfox levels increase.

2020-06-16 | GSE152510 | GEO

Splicing activation by Rbfox requires self-aggregation through its tyrosine-rich domain

Project description:To determine how the higher order assembly of Rbfox proteins affect Rbfox-dependent splicing regulation, we expressed Rbfox wildtype and its mutant protein in Flp-In™ T-REx™ 293 Rbfox2-/- cells and extracted RNA from these cells to perform RASL-seq which profiles thousands of alternative splicing event.

2017-07-13 | GSE89597 | GEO

Homo sapiens

Project description:Slicing-Independent RISC Activation Requires the Argonaute PAZ Domain

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Rbfox contributes to a conservative program of self-antigen splicing in thymic epithelial cells

Project description:Rbfox contributes to a conservative program of self-antigen splicing in thymic epithelial cells

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Lysosomal integrity suppresses TIR-1/SARM1 aggregation to restrain toxic propagation of p38 innate immunity

Project description:Innate immunity in bacteria, plants and animals requires the specialized subset of TIR-domain proteins that are NAD+ hydrolases. Aggregation of these TIR proteins engages their enzymatic activity, but it is not known how this protein multimerization is regulated. Here, we discovered that TIR oligomerization is exquisitely controlled to prevent immune toxicity. We found that p38 propagates its own activation by promoting the feedforward expression and aggregation of the lone enzymatic TIR protein in the nematode C. elegans, TIR-1/SARM1. We performed a forward genetic screen to determine how the p38 positive feedforward loop is regulated. We discovered that the integrity of the specific lysosomal sub-compartment that expresses TIR-1/SARM1 is actively maintained to limit inappropriate aggregation of this protein and restrain toxic p38 immune activation. Thus, innate immune defenses in intestinal epithelial cells are regulated by specific control of TIR-1/SARM1 multimerization.

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Analysis of the effect of PSF on the gene expression profile in neuronal cells

Project description:The multi-domain RNA-binding protein (RBP), polypyrimidine tract-binding protein (PTB)-associated splicing factor (PSF) or splicing factor, proline and glutamine-rich (SFPQ), regulate alternative splicing and transcriptional activation/repression by binding to the target RNA molecules. However, the gene regulatory mechanism of PSF in human neuronal cells is still unclear. We investigated the effect of PSF knockdown on the gene expression profile by RNA-seq using human neuronal cells, SH-SY5Y.

2024-12-19 | GSE256401 | GEO

Rbfox contributes to a conservative program of self-antigen splicing in thymic epithelial cells [Rbfox_SKO_RNAseq]

Project description:Rbfox contributes to a conservative program of self-antigen splicing in thymic epithelial cells [Rbfox_SKO_RNAseq]

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Rbfox contributes to a conservative program of self-antigen splicing in thymic epithelial cells [mTEC_bulk_RNAseq]

Project description:Rbfox contributes to a conservative program of self-antigen splicing in thymic epithelial cells [mTEC_bulk_RNAseq]

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Rbfox contributes to a conservative program of self-antigen splicing in thymic epithelial cells [mTEC_ONT_RNAseq]

Project description:Rbfox contributes to a conservative program of self-antigen splicing in thymic epithelial cells [mTEC_ONT_RNAseq]

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