Reelin marks cocaine-activated striatal neurons, promotes neuronal excitability, and regulates cocaine reward

Sci Adv. 2025 Mar 28;11(13):eads4441. doi: 10.1126/sciadv.ads4441. Epub 2025 Mar 26.

Abstract

Drugs of abuse activate defined neuronal populations in reward structures such as the nucleus accumbens (NAc), which promote the enduring synaptic, circuit, and behavioral consequences of drug exposure. While the molecular and cellular effects arising from experience with drugs like cocaine are increasingly well understood, mechanisms that dictate NAc neuronal recruitment remain unknown. Here, we leveraged unbiased single-nucleus transcriptional profiling and targeted in situ detection to identify Reln (encoding the secreted glycoprotein, Reelin) as a marker of cocaine-activated neuronal populations within the rat NAc. A CRISPR interference approach enabling selective Reln knockdown in the adult NAc altered expression of calcium signaling genes, promoted a transcriptional trajectory consistent with loss of cocaine sensitivity, and decreased MSN excitability. Behaviorally, Reln knockdown prevented cocaine locomotor sensitization, abolished cocaine place preference memory, and decreased cocaine self-administration behavior. These results identify Reelin as a critical mechanistic link between neuronal activation and cocaine-induced behavioral adaptations.

MeSH terms

  • Animals
  • Cell Adhesion Molecules, Neuronal* / genetics
  • Cell Adhesion Molecules, Neuronal* / metabolism
  • Cocaine* / pharmacology
  • Corpus Striatum* / drug effects
  • Corpus Striatum* / metabolism
  • Extracellular Matrix Proteins* / genetics
  • Extracellular Matrix Proteins* / metabolism
  • Male
  • Nerve Tissue Proteins* / genetics
  • Nerve Tissue Proteins* / metabolism
  • Neurons* / drug effects
  • Neurons* / metabolism
  • Nucleus Accumbens / drug effects
  • Nucleus Accumbens / metabolism
  • Rats
  • Rats, Sprague-Dawley
  • Reelin Protein
  • Reward*
  • Serine Endopeptidases* / genetics
  • Serine Endopeptidases* / metabolism

Substances

  • Reelin Protein
  • Cocaine
  • Reln protein, rat
  • Nerve Tissue Proteins
  • Cell Adhesion Molecules, Neuronal
  • Extracellular Matrix Proteins
  • Serine Endopeptidases