Topic: protein folding

The human γ-aminobutyric acid (GABA) transporter 1 (hGAT-1) is responsible for clearing GABA from synapse into neurons and astrocytes.Its mutations are known to impair protein folding and trigger epilepsy.Such folding defects are amenable to rescue by chemical and pharmacological chaperones.Our aim is to elucidate molecular features of two novel disease variants, in HEK293 cells (in vitro) and Drosophila melanogaster (in vivo).Deglycosylation experiments (endoglycosidase H(Endo H)) revealed distinct expression patterns for wild type hGAT-1 and the mutants: ER-resident proteins are core-glycosy

Heat shock protein 60 (Hsp60) functions as a molecular chaperone, playing a vital role in maintaining protein homeostasis by regulating protein folding and preventing protein aggregation. Levels of heat shock proteins increase in response to oxidative stress and mitochondrial damage, both of which are symptoms commonly associated with various forms of epilepsy. Hsp60 levels are increased in the plasma of patients with temporal lobe epilepsy (TLE). It is crucial to understand what conformations and functions Hsp60 obtains within its folding cycle to determine Hsp60’s role in seizure response. F