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<p>BRI23, composed of the 23 last amino acids of the integral transmembrane protein 2B (ITM2B) C-terminus, is associated with several neurodegenerative diseases, including retinal dystrophy (RD) and familial dementia. Its role in the retina remains poorly understood. This study provides a comprehensive analysis of BRI23 interactome in the human retina. Using a peptide-bead coupling system, we identified 2302 proteins, primarily involved in mitochondrial processes, synaptic transmission and photoreceptor function. Our findings show that the BRI23-RD variant, associated with the ITM2B-related RD (IRRD), exhibits significantly altered protein interactions compared to the wild-type form. Notably, we observed an increased abundance of mitochondrial proteins and synaptic molecules, indicating a potential disruption of cellular pathways driven by the IRRD variant.</p>

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The ITM2B-associated retinal dystrophy mutation modifies BRI23 peptide interactions in the human retina

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年6月23日

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  • Tasnim Ben Yacoub,
  • Andréa Amprou,
  • Camille Letellier,
  • Christelle Michiels,
  • Julien Navarro,
  • Said El Shamieh,
  • Tual Monfort,
  • Salvatore Azzollini,
  • Juliette Wohlschlegel,
  • Guillaume Chevreux,
  • Véronique Legros,
  • Morgane Lemao,
  • Guy Lenaers,
  • Kate Grieve,
  • Manuela Argentini,
  • Christina Zeitz,
  • Isabelle Audo

摘要

BRI23, composed of the 23 last amino acids of the integral transmembrane protein 2B (ITM2B) C-terminus, is associated with several neurodegenerative diseases, including retinal dystrophy (RD) and familial dementia. Its role in the retina remains poorly understood. This study provides a comprehensive analysis of BRI23 interactome in the human retina. Using a peptide-bead coupling system, we identified 2302 proteins, primarily involved in mitochondrial processes, synaptic transmission and photoreceptor function. Our findings show that the BRI23-RD variant, associated with the ITM2B-related RD (IRRD), exhibits significantly altered protein interactions compared to the wild-type form. Notably, we observed an increased abundance of mitochondrial proteins and synaptic molecules, indicating a potential disruption of cellular pathways driven by the IRRD variant.