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Intron retention of an adhesion GPCR generates 1TM isoforms required for 7TM-GPCR function.

Anne Bormann1, Marek B Körner2, Anne-Kristin Dahse1

  • 1Rudolf Schönheimer Institute of Biochemistry, Division of General Biochemistry, Medical Faculty, Leipzig University, 04103 Leipzig, Germany.

Cell Reports
|December 20, 2024
PubMed
Summary
This summary is machine-generated.

Researchers discovered novel single-transmembrane adhesion G protein-coupled receptors (aGPCRs) in Drosophila. These unconventional aGPCRs, generated by intron retention, enable Gαo-dependent signaling, enhancing neuronal mechanical sensory precision.

Keywords:
ADGRLCP: Cell biologyCP: Molecular biologyCirlaGPCRadhesion GPCRalternative splicingintron retentionisoformlatrophilinmechanobiologysensory neurons

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Area of Science:

  • Molecular Biology
  • Neuroscience
  • Cell Biology

Background:

  • Adhesion G protein-coupled receptors (aGPCRs) are crucial for mechanobiological processes across all organs.
  • Alternative splicing in aGPCRs suggests significant molecular structural diversity.
  • Conventional GPCRs possess a characteristic 7-transmembrane (7TM) signaling unit.

Purpose of the Study:

  • To investigate unconventional aGPCRs in Drosophila.
  • To understand the role of single-transmembrane (1TM) proteins in aGPCR signaling.
  • To elucidate the mechanism linking alternative splicing to aGPCR function and interactors.

Main Methods:

  • Analysis of Drosophila genome and proteome.
  • Identification of intron retention events leading to 1TM protein variants.
  • Biochemical assays to determine protein interactions and signaling pathways.
  • In vivo studies to assess neuronal function and sensory precision.

Main Results:

  • Discovery of 1TM-containing ADGRL/Cirl proteins in Drosophila, lacking the canonical 7TM domain.
  • These 1TM proteins are generated via intron retention.
  • The N-terminal fragment of 1TM proteins acts as an interactor for Gαo-dependent signaling.
  • This interaction facilitates signaling through conventional 7TM Cirl isoforms from the same gene.
  • Demonstrated enhancement of neuronal sensory precision in response to mechanical stimuli in vivo.

Conclusions:

  • Alternative splicing is a key mechanism for expressing aGPCRs with integrated molecular interactors.
  • Unconventional 1TM aGPCRs provide a novel mode of G protein signaling.
  • This discovery offers new avenues for therapeutic and experimental interventions targeting aGPCRs.