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Our findings demonstrate that latrophilin-1 could be considered as a novel biomarker of human acute myeloid leukaemia
A single SNP in LPHN1 (rs3810256) was identified, with the minor allele increasing the risk of asthma.
Data suggest teneurin-1/TENM1 (show ODZ1 Antibodies) (and possibly TENM3 (show ODZ3 Antibodies)) undergoes proteolysis to TCAPs (teneurin C-terminal associated peptides) that form intercellular adhesive units with latrophilin; signaling via TENM1 (show ODZ1 Antibodies) TCAPs appears to regulate reproduction. [REVIEW]
In this article they evaluated the amount of p120 (show HNRNPU Antibodies)-p85 complex still presented on the cellular membrane and confirmed that on cell surface major amount of mature CIRL-1 presented as a p120 (show HNRNPU Antibodies)-p85 subunit complex.
The rhamnose binding lectin-like domain of latrophilin-1 (show LPHN2 Antibodies) has a unique alpha/beta fold with long structured loops important for monosaccharide recognition, as shown in the structure of a complex with L-rhamnose.
This gene encodes a member of the latrophilin subfamily of G-protein coupled receptors (GPCR). Latrophilins may function in both cell adhesion and signal transduction. In experiments with non-human species, endogenous proteolytic cleavage within a cysteine-rich GPS (G-protein-coupled-receptor proteolysis site) domain resulted in two subunits (a large extracellular N-terminal cell adhesion subunit and a subunit with substantial similarity to the secretin/calcitonin family of GPCRs) being non-covalently bound at the cell membrane. Latrophilin-1 has been shown to recruit the neurotoxin from black widow spider venom, alpha-latrotoxin, to the synapse plasma membrane. Alternative splicing results in multiple variants encoding distinct isoforms.
, calcium-independent alpha-latrotoxin receptor 1