Unraveling the mechanism of how small molecule modulates 5' splice site recognition Article Swipe
Shasha Shi
,
Xueni Li
,
Zhiling Kuang
,
Bryan M. Dunyak
,
Frédéric H. Vaillancourt
,
Subbaiah Chalivendra
,
Rui Zhao
·
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1063/4.0000684
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1063/4.0000684
Pre-mRNA splicing, facilitated by the spliceosome, is crucial for eukaryotic gene regulation. U1snRNP, a component of the spliceosome, plays a crucial role in recognizing the 5' splice site (ss) during splicing initiation through the base pairing between a single-stranded region at the 5ʹ end of U1 snRNA and the 5ʹ ss. Spinal Muscular Atrophy (SMA) is a neuromuscular disease caused by loss of function mutations in SMN1. SMN2 partially compensates for the loss of SMN1 function. However, multiple silent mutations in SMN2 (compared to SMN1) lead to skipped exon 7 during pre-mRNA splicing, resulting in a truncated and unstable SMN protein. Small molecules like SMN-C5 and its analogs, including branaplam and risdiplam, have demonstrated the ability to enhance the binding between U1 snRNA and the 5'ss of SMN2, thereby promoting exon 7 inclusion. Risdiplam, an analog of SMN-C5, has been approved for SMA therapy. The mechanism of how these small molecules improves the recognition of weak 5' ss by U1 snRNP remains unclear and incomplete. The current NMR structure only represents the 5' ss (10 nt) and U1 snRNA (11 nt), lacking the context of U1 snRNP. Here we aim to solve the overall structure of branaplam-bound U1snRNP with SMN2 pre-mRNA using cryo-EM to address this gap. Successful completion of this research will enhance our understanding of splicing modulation by small molecules, particularly in strengthening weak 5' ss recognition, advancing therapeutic strategies for other splicing-related diseases. Pre-mRNA splicing, facilitated by the spliceosome, is crucial for eukaryotic gene regulation. U1snRNP, a component of the spliceosome, plays a crucial role in recognizing the 5' splice site (ss) during splicing initiation through the base pairing between a single-stranded region at the 5ʹ end of U1 snRNA and the 5ʹ ss. Spinal Muscular Atrophy (SMA) is a neuromuscular disease caused by loss of function mutations in SMN1. SMN2 partially compensates for the loss of SMN1 function. However, multiple silent mutations in SMN2 (compared to SMN1) lead to skipped exon 7 during pre-mRNA splicing, resulting in a truncated and unstable SMN protein. Small molecules like SMN-C5 and its analogs, including branaplam and risdiplam, have demonstrated the ability to enhance the binding between U1 snRNA and the 5'ss of SMN2, thereby promoting exon 7 inclusion. Risdiplam, an analog of SMN-C5, has been approved for SMA therapy. The mechanism of how these small molecules improves the recognition of weak 5' ss by U1 snRNP remains unclear and incomplete. The current NMR structure only represents the 5' ss (10 nt) and U1 snRNA (11 nt), lacking the context of U1 snRNP. Here we aim to solve the overall structure of branaplam-bound U1snRNP with SMN2 pre-mRNA using cryo-EM to address this gap. Successful completion of this research will enhance our understanding of splicing modulation by small molecules, particularly in strengthening weak 5' ss recognition, advancing therapeutic strategies for other splicing-related diseases.
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Metadata
- Type
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- en
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All OpenAlex metadata
Raw OpenAlex JSON
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https://doi.org/10.1063/4.0000684Digital Object Identifier
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Unraveling the mechanism of how small molecule modulates 5' splice site recognitionWork title
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articleOpenAlex work type
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enPrimary language
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2025Year of publication
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2025-03-01Full publication date if available
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Shasha Shi, Xueni Li, Zhiling Kuang, Bryan M. Dunyak, Frédéric H. Vaillancourt, Subbaiah Chalivendra, Rui ZhaoList of authors in order
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https://doi.org/10.1063/4.0000684Publisher landing page
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YesWhether a free full text is available
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goldOpen access status per OpenAlex
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https://doi.org/10.1063/4.0000684Direct OA link when available
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Mechanism (biology), splice, Small molecule, Computational biology, Computer science, Chemistry, Biology, Gene, Physics, Biochemistry, Quantum mechanicsTop concepts (fields/topics) attached by OpenAlex
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0Total citation count in OpenAlex
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10Other works algorithmically related by OpenAlex
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