2002
DOI: 10.1074/jbc.m209340200
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Homo- and Hetero-oligomerization of Thyrotropin-releasing Hormone (TRH) Receptor Subtypes

Abstract: G-protein-coupled receptors (GPCRs) are regulated by a complex network of mechanisms such as oligomerization and internalization. Using the GPCR subtypes for thyrotropin-releasing hormone (TRHR1 and TRHR2), the aim of this study was to determine if subtype-specific differences exist in the trafficking process. If so, we wished to determine the impact of homo-and hetero-oligomerization on TRHR subtype trafficking as a potential mechanism for the differential cellular responses induced by TRH. Expression of eith… Show more

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Cited by 68 publications
(46 citation statements)
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“…The formation of TRHR1/2 heterodimers increased the interaction of TRHR2 with arrestin2. Most importantly, even heterodimerization between TRHR2 and truncated TRHR1 (C335Stop), which by itself does not interact with non-visual arrestins, enhanced TRHR2-arrestin2 interaction (Hanyaloglu et al, 2002). The simplest mechanistic interpretation of these findings is that in a heterodimer with TRHR1 (but not in the TRHR2 homo-dimer) the conformation of the TRHR2 cytoplasmic elements changes in such a way as to permit arrestin2 binding tight enough to promote arrestin2-dependent internalization.…”
Section: Where Do Receptor Dimers Fit In?mentioning
confidence: 96%
See 1 more Smart Citation
“…The formation of TRHR1/2 heterodimers increased the interaction of TRHR2 with arrestin2. Most importantly, even heterodimerization between TRHR2 and truncated TRHR1 (C335Stop), which by itself does not interact with non-visual arrestins, enhanced TRHR2-arrestin2 interaction (Hanyaloglu et al, 2002). The simplest mechanistic interpretation of these findings is that in a heterodimer with TRHR1 (but not in the TRHR2 homo-dimer) the conformation of the TRHR2 cytoplasmic elements changes in such a way as to permit arrestin2 binding tight enough to promote arrestin2-dependent internalization.…”
Section: Where Do Receptor Dimers Fit In?mentioning
confidence: 96%
“…However, a few recent studies suggest that at least non-visual arrestins can bind receptors within a dimer. One study took advantage of the difference between arrestin preference of the 2 types of thyrotropin-releasing hormone receptor (TRHR): TRHR1 interacts with both arrestin2 and arrestin3, whereas TRHR2 interacts only with arrestin3, as evidenced by the enhanced internalization of TRHR1 by overexpression of either non-visual arrestin; TRHR2 endocytosis was enhanced only by arrestin3 (Hanyaloglu et al, 2002). Accordingly, the trafficking of TRHR2 was impaired in mouse embryonic fibroblasts lacking either arrestin3 or both arrestins 2 and 3, whereas the trafficking of TRHR1 was only impaired in fibroblasts lacking both non-visual arrestins.…”
Section: Where Do Receptor Dimers Fit In?mentioning
confidence: 99%
“…First, using the BRET technique, we provide evidence that binding of ␣-MSH to the MC3R induced the recruitment of ␤-arrestins in living cells. BRET assays have been successfully used to monitor arrestinreceptor interactions of multiple GPCRs (25,26,36,37) and thus have become an established tool to analyze the interaction of a given receptor with arrestins in living cells. Second, cotransfection of siRNAs specifically decreasing expression of ␤-arrestins reduced MC3R endocytosis in HEK-293 cells.…”
Section: Discussionmentioning
confidence: 99%
“…To address this question, we monitored recruitment of ␤-arrestin-1-YFP to MCR-Rluc fusion proteins in HEK-293 cells using the BRET technique as described in previous reports (25,26,36,37). As shown in Fig.…”
Section: Agrp Promotes Endocytosis Of Mcr Expressed In Hek-293mentioning
confidence: 99%
“…Inhibitors of receptor homodimerization and dimerization-defective mutants are not available for most GPCRs, including the TRH receptor. Although dimerization of the TRH receptor has been demonstrated by several approaches and TRH has been found to increase the fraction of receptors behaving as dimers (14,15), the physiological ratio of the monomer:dimer:higher oligomer in cells is unknown. Solubilized TRH receptors run at the size of monomers and dimers on SDS/PAGE, and receptors with different epitope tags coimmunoprecipitate when coexpressed (14).…”
Section: T He Thyrotropin (Ish)-releasing Hormone (Trh) Receptormentioning
confidence: 99%