Latrophilins are a family of secretin-like GPCRs that can be subdividedinto 3 subtypes: Latrophilin-1 (LPH1), -2 (LPH2), and -3 (LPH3). LPH1 is a brain-specific calcium independent receptor of alpha-latrotoxin (LTX), a neurotoxin present in black widow spider venom which triggers massive exocytosis from presynaptic nerve terminals [, ]. It is the affinity of this form of the receptor for LTX that gives the family its name.Two endogenous ligands for latrophilins have been described, teneurin-2 []and FLRT3 []. LPH1 has been shown to bind Lasso (a splice variant of teneurin-2). LPH1 and Lasso interact across intercellular and synaptic junctions, suggesting an involvement in synaptic functions []. Latrophilins are potential synaptic cell-adhesion molecules that interact trans-synaptically with teneurins and FLRTs [].
Latrophilins are a family of secretin-like GPCRs that can be subdividedinto 3 subtypes: LPH1, LPH2 and LPH3. LPH1 is a brain-specific calciumindependent receptor of alpha-latrotoxin (LTX), a neurotoxin. It is the affinity of this form of the receptor for LTX that gives the family its name. LPH2 and LPH3, whilst sharing extensive sequence similarity to LPH1, do not bind LTX. LPH2 is distributed throughout most tissues, whereas LPH3 is also brain-specific []. The endogenous ligand(s) for these receptors are at present unknown. Binding of LTX to LPH1 stimulates exocytosis and the subsequent release of large amounts of neurotransmitters from neuronal and endocrine cells. The latrophilins possess up to 7 sites of alternative splicing; the resulting number of possible splice variants leads to a highly variable family of proteins.Structurally, these proteins have a seven-transmembrane region and a large extracellular N-terminal region which consists of several domains: a rhamnose binding lectin (RBL) domain, an olfactomedin-like (OLF) domain followed by a Serine/Threonine rich domain that is O-linked glycosylated, a hormone binding (HR) domain; and a GPCR Autoproteolysis INducing (GAIN) domain [].This entry represents latrophilin-3 (LPH3). It plays a role in cell-cell adhesion, neuron guidance and in the development of glutamatergic synapses in the cortex through interaction with FLRT3 []. A common variant of the latrophilin 3 gene confers susceptibility to Attention-Deficit/Hyperactivity Disorder (ADHD) [].
Latrophilins are a family of secretin-like GPCRs that can be subdividedinto 3 subtypes: Latrophilin-1 (LPH1), -2 (LPH2), and -3 (LPH3). LPH1 is a brain-specific calcium independent receptor of alpha-latrotoxin (LTX), a neurotoxin present in black widow spider venom which triggers massive exocytosis from presynaptic nerve terminals [, ]. It is the affinity of this form of the receptor for LTX that gives the family its name.Two endogenous ligands for latrophilins have been described, teneurin-2 []and FLRT3 []. LPH1 has been shown to bind Lasso (a splice variant of teneurin-2). LPH1 and Lasso interact across intercellular and synaptic junctions, suggesting an involvement in synaptic functions []. Latrophilins are potential synaptic cell-adhesion molecules that interact trans-synaptically with teneurins and FLRTs []. LPH2 and LPH3, whilst sharing extensive sequence similarity to LPH1, do not bind LTX. LPH1 and LPH3 are expressed in neurons, while LPH2 is ubiquitous []. LPH2 is a component of the epithelial-mesenchymal transition in the heart []and may be involved in breast cancer []. This entry refers to both latrophilin-2.
