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Evidence of G-protein-coupled receptor and substrate transporter heteromerization at a single molecule level

Item Type:Article
Title:Evidence of G-protein-coupled receptor and substrate transporter heteromerization at a single molecule level
Creators Name:Fischer, J. and Kleinau, G. and Rutz, C. and Zwanziger, D. and Khajavi, N. and Müller, A. and Rehders, M. and Brix, K. and Worth, C.L. and Führer, D. and Krude, H. and Wiesner, B. and Schülein, R. and Biebermann, H.
Abstract:G-protein-coupled receptors (GPCRs) can constitute complexes with non-GPCR integral membrane proteins, while such interaction has not been demonstrated at a single molecule level so far. We here investigated the potential interaction between the thyrotropin receptor (TSHR) and the monocarboxylate transporter 8 (MCT8), a member of the major facilitator superfamily (MFS), using fluorescence cross-correlation spectroscopy (FCCS). Both the proteins are expressed endogenously on the basolateral plasma membrane of the thyrocytes and are involved in stimulation of thyroid hormone production and release. Indeed, we demonstrate strong interaction between both the proteins which causes a suppressed activation of G(q/11) by TSH-stimulated TSHR. Thus, we provide not only evidence for a novel interaction between the TSHR and MCT8, but could also prove this interaction on a single molecule level. Moreover, this interaction forces biased signaling at the TSHR. These results are of general interest for both the GPCR and the MFS research fields.
Keywords:GPCR, MCT8, MFS Transporters, Oligomerization, TSHR, Animals
Source:Cellular and Molecular Life Sciences
ISSN:1420-682X
Publisher:Springer (Switzerland)
Volume:75
Number:12
Page Range:2227-2239
Date:June 2018
Official Publication:https://doi.org/10.1007/s00018-017-2728-1
PubMed:View item in PubMed

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