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J Biol Chem, Vol. 273, Issue 19, 11472-11477, May 8, 1998
,
From the MRC Reproductive Biology Unit, Centre for Reproductive
Biology, 37 Chalmers Street, Edinburgh EH3 9EW, United Kingdom and
The mammalian gonadotropin-releasing hormone
receptor (GnRH-R) is the only G-protein-coupled receptor (GPCR) in
which the intracellular C-terminal tail is completely absent. In
contrast to other GPCRs, the GnRH-R does not show rapid desensitization of total inositol (IP) production, and the rates of internalization are
exceptionally slow. We investigated whether the incorporation of a
cytoplasmic tail into the C terminus of the GnRH-R affects desensitization events and receptor internalization rates. A
GnRH-R/TRH-R chimera was created where the intracellular tail of the
rat thyrotropin-releasing hormone receptor (TRH-R) was engineered into
the C terminus of the rat GnRH-R. Three different rat GnRH-R cDNA
stop codon mutations (one for each reading frame) were also made. The
GnRH-stimulated IP production of the wild-type rat GnRH-R expressed in
either COS-7 or HEK 293 cells did not desensitize even after prolonged stimulation with GnRH. In contrast, the catfish GnRH-R (which does
possess an intracellular tail) and the TRH-R rapidly (<10 min)
desensitized following agonist stimulation. The
GnRH-R/TRH-R chimera also desensitized following treatment
with GnRH, resembling the pattern shown by the TRH-R and the catfish
GnRH-R. Two of the stop codon mutants did not show desensitization of
IP production, and the third mutant with the longest tail was not
functional. Internalization experiments showed that the rat GnRH-R had
the slowest endocytosis and recycling rates compared with the TRH-R, the catfish GnRH-R, and the chimeric GnRH/TRH-R. This study
demonstrates that the addition of a functional intracellular
C-terminal tail to the GnRH-R produces rapid desensitization of
IP production and significantly increases internalization
rates.
Department of Experimental Zoology, Universiteit Utrecht,
Utrecht 3584 CH, The Netherlands
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G. B. Willars, J. E. Royall, S. R. Nahorski, F. El-Gehani, H. Everest, and C. A. McArdle Rapid Down-regulation of the Type I Inositol 1,4,5-Trisphosphate Receptor and Desensitization of Gonadotropin-releasing Hormone-mediated Ca2+ Responses in alpha T3-1 Gonadotropes J. Biol. Chem., January 26, 2001; 276(5): 3123 - 3129. [Abstract] [Full Text] [PDF]
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A. C. Hanyaloglu, M. Vrecl, K. M. Kroeger, L. E. C. Miles, H. Qian, W. G. Thomas, and K. A. Eidne Casein Kinase II Sites in the Intracellular C-terminal Domain of the Thyrotropin-releasing Hormone Receptor and Chimeric Gonadotropin-releasing Hormone Receptors Contribute to beta -Arrestin-dependent Internalization J. Biol. Chem., May 18, 2001; 276(21): 18066 - 18074. [Abstract] [Full Text] [PDF]
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K. M. Kroeger, A. C. Hanyaloglu, R. M. Seeber, L. E. C. Miles, and K. A. Eidne Constitutive and Agonist-dependent Homo-oligomerization of the Thyrotropin-releasing Hormone Receptor. DETECTION IN LIVING CELLS USING BIOLUMINESCENCE RESONANCE ENERGY TRANSFER J. Biol. Chem., April 13, 2001; 276(16): 12736 - 12743. [Abstract] [Full Text] [PDF]
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L. Wang, J. Bogerd, H. S. Choi, J. Y. Seong, J. M. Soh, S. Y. Chun, M. Blomenrohr, B. E. Troskie, R. P. Millar, W. H. Yu, et al. Three distinct types of GnRH receptor characterized in the bullfrog PNAS, January 2, 2001; 98(1): 361 - 366. [Abstract] [Full Text] [PDF]
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