Latrophilin fragments behave as independent proteins that associate and signal on binding of LTX(N4C).

@article{Volynski2004LatrophilinFB,
  title={Latrophilin fragments behave as independent proteins that associate and signal on binding of LTX(N4C).},
  author={Kirill E. Volynski and John-Paul Silva and Vera G. Lelianova and M Atiqur Rahman and Colin Hopkins and Yuri A. Ushkaryov},
  journal={The EMBO journal},
  year={2004},
  volume={23 22},
  pages={4423-33}
}
Heptahelical, or G-protein-coupled, receptors control many cellular functions and normally consist of one polypeptide chain. In contrast, heptahelical receptors that belong to the long N-terminus, group B (LNB) family are cleaved constitutively into two fragments. The N-terminal fragments (NTFs) resemble cell-adhesion proteins and the C-terminal fragments (CTFs) are typical G-protein-coupled receptors (GPCRs) with seven transmembrane regions. However, the functional roles of this cleavage and… CONTINUE READING