Position-dependent alternative splicing activity revealed by global profiling of alternative splicing events regulated by PTB
Open accessAbstract
To gain global insights into the role of the well-known repressive splicing regulator PTB, we analyzed the consequences of PTB knockdown in HeLa cells using high-density oligonucleotide splice-sensitive microarrays. The major class of identified PTB-regulated splicing event was PTB-repressed cassette exons, but there was also a substantial number of PTB-activated splicing events. PTB-repressed and PTB-activated exons showed a distinct arrangement of motifs with pyrimidine-rich motif enrichment within and upstream of repressed exons but downstream of activated exons. The N-terminal half of PTB was sufficient to activate splicing when recruited downstream of a PTB-activated exon. Moreover, insertion of an upstream pyrimidine tract was sufficient to convert a PTB-activated exon to a PTB-repressed exon. Our results show that PTB, an archetypal splicing repressor, has variable splicing activity that predictably depends upon its binding location with respect to target exons.
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PTB was the most highly connected protein to both α-synuclein and tau in the ECII network.
“PTB, a regulator of alternative splicing (Llorian et al., 2010), was the most highly connected protein to both α-synuclein and tau in the ECII network.”
From Selective Neuronal Vulnerability in Alzheimer’s Disease: A Network-Based Analysis (2020) · cites this paper as Llorian et al., 2010
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“Consistent with reports showing that Ptbp1 primarily functions to repress exon splicing (Boutz et al., 2007; Han et al., 2014; Llorian et al., 2010), knockdown of Ptbp1”
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Self-citation
- Authors
- Llorian, M., Schwartz, S., Clark, T. A., Hollander, D., Tan, L.-Y., Spellman, R., Gordon, A., Schweitzer, A. C., de la Grange, P., Ast, G., & Smith, C. W. J.
- Affiliations
- University of Cambridge (GB)
- Tel Aviv University (IL)
- Affymetrix (United States) (US)
- Institute of Cancer Research (GB)
- Corresponding author
- Smith, Christopher W J
- Venue
- Nature Structural & Molecular Biology
- Published
- 2010-08-15
- Volume
- 17
- Issue
- 9
- Pages
- 1114-1123
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC2933513
- OpenAlex
- W2042086006
- Cited by
- 263
- References
- 69
- Citations by year
- 2026: 9 · 2025: 13 · 2024: 15 · 2023: 22 · 2022: 9 · 2021: 15 · 2020: 12 · 2019: 8 · 2018: 17 · 2017: 15 · 2016: 17 · 2015: 19 · 2014: 21 · 2013: 22 · 2012: 28
- FWCI
- 9.11
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Wellcome Trust (077877)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- polypyrimidine tract-binding protein, PTB, alternative splicing, splicing regulation, cassette exons, HeLa cells
- MeSH terms
- Base Sequence, Exons, HeLa Cells, Humans, Introns, Molecular Sequence Data, Alternative Splicing, Oligonucleotide Array Sequence Analysis, Silencer Elements, Transcriptional, Polypyrimidine Tract-Binding Protein
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