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• W2148512452 abstract "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 of any subsequent NTF-CTF interactions remain to be identified. Using latrophilin, a well-studied member of the LNB family, we now demonstrate that cleavage is critical for delivery of this receptor to the cell surface. On the plasma membrane, NTF and CTF behave as separate membrane proteins involved, respectively, in cell-surface reception and signalling. The two fragments can also internalise independently. However, separated NTF and CTF can re-associate on solubilisation. Agonist binding to NTF on the cell surface also induces re-association of fragments and provokes signal transduction via CTF. These findings define a novel principle of structural and functional organisation of the cleaved, two-subunit GPCRs." @default.
• W2148512452 created "2016-06-24" @default.
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• W2148512452 date "2004-10-14" @default.
• W2148512452 modified "2023-10-13" @default.
• W2148512452 title "Latrophilin fragments behave as independent proteins that associate and signal on binding of LTXN4C" @default.
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• W2148512452 doi "https://doi.org/10.1038/sj.emboj.7600443" @default.
• W2148512452 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/526461" @default.
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