High-content screening identifies a small molecule that restores AP-4-dependent protein trafficking in neuronal models of AP-4-associated hereditary spastic paraplegia

Nat Commun. 2024 Jan 17;15(1):584. doi: 10.1038/s41467-023-44264-1.

Abstract

Unbiased phenotypic screens in patient-relevant disease models offer the potential to detect therapeutic targets for rare diseases. In this study, we developed a high-throughput screening assay to identify molecules that correct aberrant protein trafficking in adapter protein complex 4 (AP-4) deficiency, a rare but prototypical form of childhood-onset hereditary spastic paraplegia characterized by mislocalization of the autophagy protein ATG9A. Using high-content microscopy and an automated image analysis pipeline, we screened a diversity library of 28,864 small molecules and identified a lead compound, BCH-HSP-C01, that restored ATG9A pathology in multiple disease models, including patient-derived fibroblasts and induced pluripotent stem cell-derived neurons. We used multiparametric orthogonal strategies and integrated transcriptomic and proteomic approaches to delineate potential mechanisms of action of BCH-HSP-C01. Our results define molecular regulators of intracellular ATG9A trafficking and characterize a lead compound for the treatment of AP-4 deficiency, providing important proof-of-concept data for future studies.

MeSH terms

  • Humans
  • Mutation
  • Neurons / metabolism
  • Protein Transport
  • Proteins / metabolism
  • Proteomics
  • Spastic Paraplegia, Hereditary* / drug therapy
  • Spastic Paraplegia, Hereditary* / genetics
  • Spastic Paraplegia, Hereditary* / metabolism

Substances

  • Proteins