As for other GPCRs, the oligomerization of glycoprotein hormone receptors (GPHRs) appears as critical event for receptor function. By means of modern techniques based on the BRET or FRET principle, GPHR oligomerization has been reported to explain several physiological and pathological conditions. In particular, the presence of oligomers was demonstrated not only in in vitro heterologous systems but also in in vivo tissues, and GPHR homodimerization appears associated with strong negative cooperativity, thus suggesting that one hormone molecule may be sufficient for receptor dimer stimulation. In addition, oligomerization has been reported to occur early during the posttranslational maturation process and to be involved in the dominant negative effect exerted by loss-of-function TSH receptor (TSHR) mutants, that are prevalently retained inside the cell, on the surface expression of wild-type receptors. This molecular mechanism thus explains the dominant inheritance of certain forms of TSH resistance. Here, we provide the description of the methods used in the original BRET, FRET, and HTRF-RET experiments.
Modern methods to investigate the oligomerization of glycoprotein hormone receptors (TSHR, LHR, FSHR) / M. Bonomi, L. Persani (METHODS IN ENZYMOLOGY). - In: G protein coupled receptors : trafficking and oligomerization / [a cura di] P.M. Conn. - [s.l] : Elsevier, 2013. - ISBN 9780123918628. - pp. 367-383 [10.1016/B978-0-12-391862-8.00020-X]
Modern methods to investigate the oligomerization of glycoprotein hormone receptors (TSHR, LHR, FSHR)
M. Bonomi;L. Persani
2013
Abstract
As for other GPCRs, the oligomerization of glycoprotein hormone receptors (GPHRs) appears as critical event for receptor function. By means of modern techniques based on the BRET or FRET principle, GPHR oligomerization has been reported to explain several physiological and pathological conditions. In particular, the presence of oligomers was demonstrated not only in in vitro heterologous systems but also in in vivo tissues, and GPHR homodimerization appears associated with strong negative cooperativity, thus suggesting that one hormone molecule may be sufficient for receptor dimer stimulation. In addition, oligomerization has been reported to occur early during the posttranslational maturation process and to be involved in the dominant negative effect exerted by loss-of-function TSH receptor (TSHR) mutants, that are prevalently retained inside the cell, on the surface expression of wild-type receptors. This molecular mechanism thus explains the dominant inheritance of certain forms of TSH resistance. Here, we provide the description of the methods used in the original BRET, FRET, and HTRF-RET experiments.File | Dimensione | Formato | |
---|---|---|---|
Bonomi & Persani, MIE 2013.pdf
accesso riservato
Tipologia:
Publisher's version/PDF
Dimensione
1.15 MB
Formato
Adobe PDF
|
1.15 MB | Adobe PDF | Visualizza/Apri Richiedi una copia |
Pubblicazioni consigliate
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.