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Last updated: 29 December 2024 Print

GABRB3 Mutations

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GABRB3 mutationsSevere Epileptic Encephalopathies

Introduction

  • GABRB3 gene is a recently identified gene located in 15q12 chromosome and encodes encodes the β3-subunit of the GABA-A receptor, a ligand-gated chloride channel.
  • The gene is believed to share a role in inhibitory GABAergic synapses, GABA iron-gated channel function, and possible cellular response to histamine.
  • The β3 subunit is expressed in cerebral grey matter, thalami, hippocampi, and cerebellum, among other structures.
  • GABA-A receptors mediate fast inhibitory neurotransmission in the central nervous system (CNS).
  • Faulty GABRB3 function is linked to several neurological disorders and clinical syndromes. However, the spectrum of such disorders is not yet well known
  • Mutations in GABRB3 are emerging as a significant cause of early infantile epileptic encephalopathy (EIEE), a severe developmental and epileptic encephalopathy.

GABA-A Receptor: Structure and Function

  • Composition: Pentameric assembly of subunits (α, β, γ, δ, etc.). Typical GABA-A receptors have:
    • 2 α-subunits
    • 2 β-subunits (e.g., GABRB3)
    • 1 γ-subunit

    Clinical Relevance of GABRB3

    • Formed by transmembrane domains M1–M4 of each subunit.
    • The M2 domain lines the ion channel pore.

    GABRB3 Mutations and Epilepsy

    • GABA binding leads to chloride influx (hyperpolarization → neuronal inhibition).
    • In immature neurons, GABA causes chloride efflux (depolarization → excitation) due to NKCC1 transporter activity​
    MutationAge at OnsetSeizure TypesEEG FindingsOther Features
    p.Asn110Asp 5 months Infantile spasms Hypsarrhythmia None
    p.Asn120Asp 10 months Infantile spasms Generalized 2 Hz bursts ADHD, impulsivity
    p.Thr287Ile 3 months Multiple seizure types Generalized fast activity Severe hypotonia, dysmorphia
    p.Tyr302Cys 10 months Focal dyscognitive Slow, left-temporal focus Behavioral arrest, severe ID

    Key Point: The p.Thr287Ile mutation, located in the M2 domain, impacts ion pore function and likely reduces chloride flux, causing hyperexcitability​

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