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Detection of Alternative Splicing During Epithelial-Mesenchymal Transition
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Alternative splicing regulates stochastic NLRP3 activity.

Florian Hoss1, James L Mueller2, Francisca Rojas Ringeling3

  • 1Institute of Innate Immunity, University Hospital, University of Bonn, 53127, Bonn, Germany.

Nature Communications
|July 21, 2019
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Summary
This summary is machine-generated.

Alternative splicing (AS) of leucine-rich repeat (LRR) domains in human NLRP3 inflammasome sensors impacts innate immunity. This AS generates isoforms that affect protein interactions and immune function.

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Area of Science:

  • Molecular Biology
  • Immunology
  • Genetics

Background:

  • Leucine-rich repeat (LRR) domains are crucial, conserved protein structures involved in development and immunity.
  • Alternative splicing (AS) is a key mechanism for generating protein diversity from a limited number of genes.

Purpose of the Study:

  • To investigate the role of exonic modularity in LRR domains concerning alternative splicing.
  • To examine the impact of AS on Nod-like receptors, particularly the NLRP3 inflammasome sensor.

Main Methods:

  • Analysis of exonic structure in human LRR-containing gene families.
  • Identification and characterization of alternative splicing variants of NLRP3 in human and mouse.
  • Functional assessment of NLRP3 isoforms, including interaction studies with NEK7.

Main Results:

  • Strict exonic modularity was observed in LRR domains, enabling alternative splicing.
  • Human NLRP3 exhibits AS, producing a major isoform lacking exon 5 (NLRP3 Δ exon 5).
  • NLRP3 Δ exon 5 lacks the NEK7 interaction site, leading to a loss of inflammasome activity.

Conclusions:

  • Alternative splicing of LRR domains represents a novel regulatory mechanism in vertebrate innate immunity.
  • Differential utilization of LRR modules via AS, as seen in human NLRP3, critically affects immune signaling pathways.