ALG13, encoding a subunit of the uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) transferase enzyme, is crucial in the N-linked glycosylation pathway. This pathway attaches carbohydrate structures to asparagine residues in proteins within the endoplasmic reticulum, and N-glycosylated proteins are involved in processes like electrical gradients formation and neurotransmission [1].

In Alg13 knockout (KO) mouse models, KA-induced epileptic progressions were increased, including prolonged electrographic seizures, higher mortality rates, and more severe responses to epileptic seizures. The cortex and hippocampus of Alg13 KO mice showed hyperactive mTOR signaling pathways [2]. Also, about 20% of adult ALG13KO knockout mice display spontaneous seizures, with a marked decrease in gamma-aminobutyric acid A receptor (GABAAR)-mediated inhibitory synaptic transmission. ALG13 may influence the expression of GABAARα2 membrane and total protein by changing its transcription level [3].

In conclusion, ALG13 is essential for the N-linked glycosylation pathway. Studies using Alg13 KO mouse models have revealed its role in epilepsy, showing that ALG13 deficiency can increase seizure susceptibility and severity, potentially through the regulation of GABAAR function and mTOR signaling pathways [2,3].