Variants in FGF13, associated with developmental and epileptic encephalopathies, alter neuronal excitability by affecting inhibitory neurons and by a sodium channel-independent mechanism.

lncDACH1 is a novel regulator of sodium channel, which suppresses the membrane trafficking of Nav1.5 by disturbing the function of dystrophin.

A single amino acid change in a neuronal ion channel called KCNQ2 blocks ion flow, prevents protein localization on axons, and results in severe epilepsy and slowed neurological development.

NMR and clustering results show that N-terminal acetylation of α-syn enhances its binding to the neutral phospholipid lysophosphatidylcholine, thereby promoting its function of clustering synaptic vesicles.

Genome-wide CRISPRi screens and proteome profiling of lysosomes link lipid dysregulation to ESCRT disruption and proteostasis defect.