ReviewWiley interdisciplinary reviews. RNA
Alternative Splicing of Exon 23a in Neurofibromatosis Type 1 Pre-mRNA: Its Contribution to the Protein Structure and Function of Neurofibromin.
Review in Wiley interdisciplinary reviews. RNA. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Alternative splicing in cancer drug resistance: Mechanisms and therapeutic prospects (Review).Oncology reports · 2026Review
- Alternative Splicing of Exon 23a in Neurofibromatosis Type 1 Pre-mRNA: Its Contribution to the Protein Structure and Function of Neurofibromin.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The neurofibromatosis type 1 (NF1) gene has 61 exons. The major alternative exon in NF1 pre-mRNA is exon 23a. Skipping and inclusion of this exon produce isoform I and isoform II neurofibromin, respectively. When the alternative exon was discovered in 1993, several experiments conducted in yeast and human cell lines quickly led to the conclusion that inclusion of this exon reduced the RasGAP function of the neurofibromin protein by 5-10-fold. Since then, research efforts on this seemingly important alternative splicing event have been sporadic, leaving many important questions unanswered, until after 2020 when several important papers related to the structure and function of exon 23a have been published. Two major advancements have been made. First, the cryo-EM structures of the full-length neurofibromin, of both isoforms, have been solved. More excitingly, the structure of isoform II neurofibromin that includes exon 23a provides important insight into why this isoform has reduced RasGAP activity. Second, the role of the altered splicing pattern of exon 23a in the development of high-grade glioma (HGG) has been investigated. In this review, we start with the introduction of alternative splicing of exon 23a, its discovery, differential expression patterns, and regulatory mechanisms that control this alternative splicing event. Next, we discuss the structural differences between the two isoforms which give insight into the differing RasGAP activities. We then review the in vivo biological function of the regulated inclusion of exon 23a, focusing on cognitive behaviors and brain tumor development. Finally, we briefly discuss the future directions of studies on NF1 exon 23a. This article is categorized under: RNA Processing > Splicing Regulation/Alternative Splicing.
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Registered trials
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