Latrophilin 1

Latrophilin 1 is a protein that in humans is encoded by the ADGRL1 gene. It is a member of the adhesion G protein-coupled receptor family, which is characterized by a long N-terminal extracellular domain. This protein is a receptor for alpha-latrotoxin, a potent neurotoxin secreted by the black widow spider.

Structure[edit | edit source]

Latrophilin 1 is a large protein, with a molecular weight of approximately 150 kDa. It is composed of a long N-terminal extracellular domain, a seven-transmembrane domain, and a short C-terminal intracellular domain. The extracellular domain contains several distinct regions, including a lectin-like domain, an olfactomedin-like domain, and a hormone-binding domain.

Function[edit | edit source]

Latrophilin 1 functions as a receptor for alpha-latrotoxin, a potent neurotoxin secreted by the black widow spider. Upon binding to alpha-latrotoxin, latrophilin 1 triggers a massive release of neurotransmitters from neurons, leading to severe symptoms such as pain, paralysis, and even death.

In addition to its role in neurotoxicity, latrophilin 1 is also involved in cell adhesion and signaling. It has been shown to interact with several other proteins, including teneurins, FLRTs, and neurexins, and is thought to play a role in the formation and maintenance of synapses in the nervous system.

Clinical significance[edit | edit source]

Mutations in the ADGRL1 gene, which encodes latrophilin 1, have been associated with several neurological disorders, including attention deficit hyperactivity disorder (ADHD), autism spectrum disorder (ASD), and schizophrenia. However, the exact role of latrophilin 1 in these disorders is still not fully understood.