Latrophilin-1 (Nematode) (LAT-1)

The Nematode latrophilin-like G-protein-coupled receptor, specifically Latrophilin-1 (LAT-1), is an adhesion-class G protein-coupled receptor (aGPCR) essential for the physiological function of nematodes (UniProt: P90768). It is widely expressed in the pharyngeal and body wall muscles, as well as the nervous system, where it regulates vital processes such as pharyngeal pumping, locomotion, and egg-laying (Willson et al., 2004). LAT-1 is recognized as the primary molecular target for the anthelmintic drug emodepside, a semi-synthetic cyclooctadepsipeptide used to treat parasitic worm infections (Harder et al., 2005). When emodepside binds to LAT-1, it acts as an agonist, initiating a signal transduction pathway involving Gq proteins and phospholipase C (Guest et al., 2007). This signaling cascade leads to the activation of SLO-1 calcium-activated potassium channels, resulting in the hyperpolarization of muscle cells and neurons. The consequence of this activation is flaccid paralysis of the nematode, which prevents feeding and movement, ultimately leading to the parasite's death. Beyond its role in drug interaction, LAT-1 is involved in developmental processes, including tissue polarity and cell alignment during embryogenesis. Due to its distinct pharmacological profile and essentiality in parasites, LAT-1 remains a focal point for developing novel treatments against resistant helminth strains.

Other names

Latrophilin-like receptor 1B0457.1Adhesion G protein-coupled receptor L1Nematode latrophilin-like G-protein-coupled receptor

Agonist; binding of emodepside to LAT-1 activates a Gq-protein signaling cascade (Gq/11 and Phospholipase C) that leads to the release of inhibitory neuropeptides or the direct activation of SLO-1 potassium channels, resulting in hyperpolarization and flaccid paralysis of the nematode (Willson et al., 2004; Guest et al., 2007).