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Splice Factor Polypyrimidine tract-binding protein 1 (Ptbp1) Primes Endothelial Inflammation in Atherogenic Disturbed Flow Conditions

ABSTRACT: This SuperSeries is composed of the SubSeries listed below.

ORGANISM(S): Mus musculus

PROVIDER: GSE206851 | GEO | 2022/06/27

REPOSITORIES: GEO

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Splice Factor Polypyrimidine tract-binding protein 1 (Ptbp1) Primes Endothelial Inflammation in Atherogenic Disturbed Flow Conditions [Ptbp1]

Project description:Analysis of effects of Ptbp1 deletion on RNA splicing and expression in aortic endothelial cells

2022-06-27 | GSE206849 | GEO

Splice Factor Polypyrimidine tract-binding protein 1 (Ptbp1) Primes Endothelial Inflammation in Atherogenic Disturbed Flow Conditions [CRISPR]

Project description:Analysis of effects of Ptbp1 deletion on RNA splicing and expression in aortic endothelial cells

2022-06-27 | GSE206850 | GEO

Splice Factor Polypyrimidine tract-binding protein 1 (Ptbp1) Primes Endothelial Inflammation in Atherogenic Disturbed Flow Conditions [Ptbp1]

Project description:Splice Factor Polypyrimidine tract-binding protein 1 (Ptbp1) Primes Endothelial Inflammation in Atherogenic Disturbed Flow Conditions [Ptbp1]

| PRJNA852427 | ENA

Splice Factor Polypyrimidine tract-binding protein 1 (Ptbp1) Primes Endothelial Inflammation in Atherogenic Disturbed Flow Conditions

Project description:Splice Factor Polypyrimidine tract-binding protein 1 (Ptbp1) Primes Endothelial Inflammation in Atherogenic Disturbed Flow Conditions

| PRJNA852424 | ENA

Splice Factor Polypyrimidine tract-binding protein 1 (Ptbp1) Primes Endothelial Inflammation in Atherogenic Disturbed Flow Conditions [CRISPR]

Project description:Splice Factor Polypyrimidine tract-binding protein 1 (Ptbp1) Primes Endothelial Inflammation in Atherogenic Disturbed Flow Conditions [CRISPR]

| PRJNA852426 | ENA

Polypyrimidine tract binding proteins PTBP1 and PTBP2 interact with distinct proteins under splicing conditions.

Project description:RNA binding proteins play an important role in regulating alternative pre-mRNA splicing and in turn cellular gene expression. Polypyrimidine tract binding proteins, PTBP1 and PTBP2, are paralogous RNA binding proteins that play a critical role in the process of neuronal differentiation and maturation; changes in the concentration of PTBP proteins during neuronal development direct splicing changes in many transcripts that code for proteins critical for neuronal differentiation. How the two related proteins regulate different sets of neuronal exons is unclear. The distinct splicing activities of PTBP1 and PTBP2 can be recapitulated in an in vitro splicing system with the differentially regulated N1 exon of the c-src pre-mRNA. Here, we conducted experiments under these in vitro splicing conditions to identify PTBP1 and PTBP2 interacting partner proteins. Our results highlight that both PTBPs interact with proteins that participate in chromatin remodeling and transcription regulation. Our data reveal that PTBP1 interacts with many proteins involved in mRNA processing including splicing regulation while PTBP2 does not. Our results also highlight enzymes that can serve as potential "writers" and "erasers" in adding chemical modifications to the PTB proteins. Overall, our study highlights important differences in protein-protein interactions between the PTBP proteins under splicing conditions and supports a role for post-translational modifications in dictating their distinct splicing activities.

| S-EPMC8812845 | biostudies-literature

Post-Translational Modifications in Polypyrimidine Tract Binding Proteins PTBP1 and PTBP2.

Project description:RNA binding proteins play an important role in regulating alternative pre-mRNA splicing and in turn cellular gene expression. Many of these RNA binding proteins occur as gene families with members sharing a high degree of primary structure identity and domain organization yet have tissue-specific expression patterns and regulate different sets of target exons. How highly similar members in a gene family can exert different splicing outcomes is not well understood. We conducted mass spectrometry analysis of post-translational phosphorylation and acetylation modifications for two paralogs of the polypyrimidine tract binding protein family, PTBP1 and PTBP2, to discover modifications that occur in splicing reaction mixtures and to identify discrete modifications that may direct their different splicing activities. We find that PTBP1 and PTBP2 have many distinct phosphate modifications located in the unstructured N-terminal, linker 1, and linker 2 regions. We find that the two proteins have many overlapping acetate modifications in the RNA recognition motifs (RRMs) with a few distinct sites in PTBP1 RRM2 and RRM3. Our data also reveal that lysine residues in the nuclear localization sequence of PTBP2 are acetylated. Collectively, our results highlight important differences in post-translational modifications between the paralogs and suggest a role for them in the differential splicing activity of PTBP1 and PTBP2.

| S-EPMC6211845 | biostudies-literature

Polypyrimidine Tract Binding Proteins PTBP1 and PTBP2 Interact with Distinct Proteins Under Splicing Conditions

2022-01-20 | PXD029899 | Pride

Regulation of BCL-X splicing reveals a role for the polypyrimidine tract binding protein (PTBP1/hnRNP I) in alternative 5' splice site selection.

Project description:Alternative splicing (AS) modulates many physiological and pathological processes. For instance, AS of the BCL-X gene balances cell survival and apoptosis in development and cancer. Herein, we identified the polypyrimidine tract binding protein (PTBP1) as a direct regulator of BCL-X AS. Overexpression of PTBP1 promotes selection of the distal 5' splice site in BCL-X exon 2, generating the pro-apoptotic BCL-Xs splice variant. Conversely, depletion of PTBP1 enhanced splicing of the anti-apoptotic BCL-XL variant. In vivo cross-linking experiments and site-directed mutagenesis restricted the PTBP1 binding site to a polypyrimidine tract located between the two alternative 5' splice sites. Binding of PTBP1 to this site was required for its effect on splicing. Notably, a similar function of PTBP1 in the selection of alternative 5' splice sites was confirmed using the USP5 gene as additional model. Mechanistically, PTBP1 displaces SRSF1 binding from the proximal 5' splice site, thus repressing its selection. Our study provides a novel mechanism of alternative 5' splice site selection by PTBP1 and indicates that the presence of a PTBP1 binding site between two alternative 5' splice sites promotes selection of the distal one, while repressing the proximal site by competing for binding of a positive regulator.

| S-EPMC4231771 | biostudies-literature

Neuronal regulation of pre-mRNA splicing by polypyrimidine tract binding proteins, PTBP1 and PTBP2.

Project description:Alternative splicing patterns are regulated by RNA binding proteins that assemble onto each pre-mRNA to form a complex RNP structure. The polypyrimidine tract binding protein, PTB, has served as an informative model for understanding how RNA binding proteins affect spliceosome assembly and how changes in the expression of these proteins can control complex programs of splicing in tissues. In this review, we describe the mechanisms of splicing regulation by PTB and its function, along with its paralog PTBP2, in neuronal development.

| S-EPMC3422667 | biostudies-literature

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