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Conserved role for spliceosomal component PRPF40A in microexon splicing.

Bikash Choudhary1, Adam Norris2

  • 1Department of Biochemistry, University of California, Riverside, California 92521, USA.

RNA (New York, N.Y.)
|October 10, 2024
PubMed
Summary

PRPF40A is essential for splicing microexons in mouse cells, working with SRRM4. This splicing factor also regulates its own gene expression, revealing cross-regulation within the spliceosome.

Keywords:
microexonsplicing

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Area of Science:

  • Molecular Biology
  • Genetics
  • Neuroscience

Background:

  • Microexons are crucial for neuronal gene expression but present splicing challenges.
  • Previous work identified PRP-40 as vital for microexon splicing in C. elegans.

Purpose of the Study:

  • To investigate the role of the homologous PRPF40A in microexon splicing in mammalian cells.
  • To elucidate the relationship between PRPF40A, SRRM4, and microexon size.
  • To explore potential cross-regulatory mechanisms involving PRPF40A.

Main Methods:

  • Utilized mouse neuroblastoma cells to study microexon splicing.
  • Performed knockdown experiments to assess the function of PRPF40A.
  • Analyzed the interplay between PRPF40A and SRRM4 in regulating microexons of varying sizes.
  • Investigated the impact of PRPF40A knockdown on the splicing of its binding partner, Luc7l.

Main Results:

  • PRPF40A is globally required for microexon splicing in mouse neuroblastoma cells.
  • PRPF40A and SRRM4 coregulate microexons, with distinct size-dependent relationships.
  • SRRM4-dependence shows a threshold at ~30 nt, while PRPF40A-dependence decreases gradually with increasing exon size.
  • PRPF40A knockdown enhances productive splicing of Luc7l by promoting the skipping of a poison exon.

Conclusions:

  • PRPF40A is a key regulator of microexon splicing in mammals, analogous to its C. elegans counterpart.
  • The findings reveal a novel size-dependent regulatory mechanism for microexons involving PRPF40A and SRRM4.
  • Demonstrated homeostatic cross-regulation between spliceosomal components, extending this concept to evolutionarily distinct proteins.