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LRRC37B is a member of the primate-specific LRRC37 family, typically found as a single-pass membrane protein with an extensive leucine-rich repeat extracellular domain. The LRR domain is crucial for binding proteins and is necessary/sufficient for binding its identified ligand FGF13A. LRRC37B acts as a co-receptor for extracellular secreted FGF13A, and this interaction inhibits the function of voltage-gated sodium channels (specifically Nav1.6) in neurons. This localization and function suggest a potential role in modulating neuronal excitability and possibly influencing neurodevelopmental processes. LRRC37B is also found on human chromosome 17q11, a region subject to frequent genomic rearrangements and duplications, which may confer susceptibility to certain genetic disorders, though the specific implications of LRRC37B in pathology remain largely uncharacterized. No drugs or established biomarkers are currently associated with LRRC37B, and its clinical significance is not yet defined.
Modulates sodium channel activity via interaction with FGF13A; Acts as a co-receptor for FGF13A; affects neuronal excitability by locally regulating FGF13A and Nav1.6 at the axon initial segment
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