期刊
JOURNAL OF CELL SCIENCE
卷 123, 期 8, 页码 1320-1328出版社
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.057919
关键词
Adiponectin; Adiponectin receptor; Receptor dimerization; Bimolecular fluorescence complementation
类别
资金
- Deutsche Forschungsgemeinschaft [KFO152, Be 1264/10-1]
- Europaische Fonds fur regionale Entwicklung [EFRE-13401]
- Studienstiftung des deutschen Volkes
AdipoR1 and AdipoR2 are newly discovered members of the huge family of seven-transmembrane receptors, but both receptors are structurally and functionally different from G-protein-coupled receptors. Little is known about the oligomerization of the AdipoRs. Here, we show the presence of endogenous AdipoR1 dimers in various cell lines and human muscle tissue. To directly follow and localize the dimerization, we applied bimolecular fluorescence complementation (BiFC) in combination with flow cytometry. We visualized and quantified AdipoR1 homodimers in HEK293 cells. Moreover, we identified a GxxxG dimerization motif in the fifth transmembrane domain of the AdipoR1. By mutating both glycine residues to phenylalanine or glutamic acid, we were able to modulate the dimerization of AdipoR1, implicating a role for the GxxxG motif in AdipoR1 dimerization. Furthermore, we tested whether the AdipoR1 ligand adiponectin had any influence on receptor dimerization. Interestingly, we found that adiponectin decreases the receptor dimerization in a concentration-dependent manner. This effect is mainly mediated by segments of the collagen-like domain of full-length adiponectin. Accordingly, this is the first direct read-out signal of adiponectin at the AdipoR1 receptor, which revealed the involvement of specific amino acids of both the receptor and the ligand to modulate the quaternary structure of the AdipoR1.
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