Leucine-rich repeat-containing protein 4B (LRRC4B)

Leucine-rich repeat-containing protein 4B (LRRC4B), also known as NGL-3, is a member of the leucine-rich repeat (LRR) and immunoglobulin superfamilies, and functions primarily as a synaptic adhesion molecule and postsynaptic receptor within the brain. It plays a central role in **synaptic organization**, **formation**, and **maturation** of excitatory synapses by mediating both pre- and postsynaptic protein interactions, including binding to NMDA and AMPA glutamate receptors. LRRC4B contains an extracellular LRR domain, an immunoglobulin C2 (IgC2) domain, a transmembrane region, and a cytoplasmic PDZ-binding motif, indicating its function as a scaffold for synaptic protein complexes[2][3]. Expression is highly specific to neural tissue, with altered expression detected in neuroinflammatory and neurodevelopmental disorders as well as certain tumors, including glioblastoma. It may be considered a candidate biomarker for pathological synaptic remodeling in disorders such as encephalitis[3]. No specific therapeutic drugs or modulators are clinically approved targeting LRRC4B.

Other names

LRIG4NGL-3DKFZp761A179HSMNetrin-G3 ligandnetrin-G ligand-3netrin-G3 ligandleucine-rich repeats and immunoglobulin-like domains 4LRRC4B