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Distinct regions of C‐terminus of the high affinity neurotensin receptor mediate the functional coupling with pertussis toxin sensitive and insensitive G‐proteins
Author(s) -
Najimi Mustapha,
Gailly Philippe,
Maloteaux Jean-Marie,
Hermans Emmanuel
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02285-8
Subject(s) - chinese hamster ovary cell , neurotensin , pertussis toxin , internalization , receptor , biology , g protein , neurotensin receptor , g protein coupled receptor , transfection , guanosine , microbiology and biotechnology , biochemistry , neuropeptide , gene
The functional coupling of C‐terminally truncated mutants of the high affinity rat neurotensin (NT) receptor (NTS1) was characterized in transfected Chinese hamster ovary cells. On cells expressing NTRΔ372 (truncated NTS1 lacking the entire 52 amino acid C‐terminus), NT failed to promote [ 35 S]guanosine 5′‐[γ‐ 35 S]triphosphate binding whereas a robust pertussis toxin (PTx) sensitive response was observed in cells expressing a partially truncated receptor (NTRΔ401 lacking the last 23 residues). Similar results were obtained when measuring the ability of NT to induce the production of arachidonic acid. Since neither deletions impaired the NT‐induced phosphoinositide hydrolysis, these results indicate that the membrane proximal region of the C‐terminus is specifically involved in the functional coupling of the receptor with PTx sensitive G‐proteins. This region was also found to be involved in the control of receptor internalization. However, PTx failed to impair internalization, indicating that these two properties are not directly related.