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Evidence for constitutive dimerization of niacin receptor subtypes.
Biochem Biophys Res Commun. 2010 Apr 30; 395(2):281-7.BB

Abstract

The recently deorphanized niacin receptor subtypes NIACR1 (GPR109A) and NIACR2 (GPR109B) play an essential role in the regulation of metabolic processes and immune reactions. Both receptors belong to the G-protein-coupled receptor (GPCR) family, whose members have traditionally been treated as monomeric entities, but now appear to exist and function as both homodimers and heterodimers. In this study, a close physical interaction is shown between the highly homologous niacin receptor subtypes, NIACR1 and NIACR2, using bioluminescence resonance energy transfer (BRET(2)) in living cells. The extent of homo- and hetero-dimerization of the niacin receptors did not vary after activation of the receptors with selective agonists, indicating that the dimerization state of NIACR1 and NIACR2 is not regulated by ligand binding. Moreover, detection of niacin receptor dimers in both plasma membrane- and endoplasmic reticulum-enriched fractions suggests that they are formed early in the biosynthetic pathway. Taken together, these results demonstrate that niacin receptor dimerization is a constitutive process occurring early during biosynthesis.

Authors+Show Affiliations

Latvian Biomedical Research and Study Centre, Riga, LV 1067, Latvia. ilona@biomed.lu.lvNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

20380810

Citation

Mandrika, Ilona, et al. "Evidence for Constitutive Dimerization of Niacin Receptor Subtypes." Biochemical and Biophysical Research Communications, vol. 395, no. 2, 2010, pp. 281-7.
Mandrika I, Petrovska R, Klovins J. Evidence for constitutive dimerization of niacin receptor subtypes. Biochem Biophys Res Commun. 2010;395(2):281-7.
Mandrika, I., Petrovska, R., & Klovins, J. (2010). Evidence for constitutive dimerization of niacin receptor subtypes. Biochemical and Biophysical Research Communications, 395(2), 281-7. https://doi.org/10.1016/j.bbrc.2010.04.011
Mandrika I, Petrovska R, Klovins J. Evidence for Constitutive Dimerization of Niacin Receptor Subtypes. Biochem Biophys Res Commun. 2010 Apr 30;395(2):281-7. PubMed PMID: 20380810.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Evidence for constitutive dimerization of niacin receptor subtypes. AU - Mandrika,Ilona, AU - Petrovska,Ramona, AU - Klovins,Janis, Y1 - 2010/04/07/ PY - 2010/03/30/received PY - 2010/04/02/accepted PY - 2010/4/13/entrez PY - 2010/4/13/pubmed PY - 2010/6/22/medline SP - 281 EP - 7 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 395 IS - 2 N2 - The recently deorphanized niacin receptor subtypes NIACR1 (GPR109A) and NIACR2 (GPR109B) play an essential role in the regulation of metabolic processes and immune reactions. Both receptors belong to the G-protein-coupled receptor (GPCR) family, whose members have traditionally been treated as monomeric entities, but now appear to exist and function as both homodimers and heterodimers. In this study, a close physical interaction is shown between the highly homologous niacin receptor subtypes, NIACR1 and NIACR2, using bioluminescence resonance energy transfer (BRET(2)) in living cells. The extent of homo- and hetero-dimerization of the niacin receptors did not vary after activation of the receptors with selective agonists, indicating that the dimerization state of NIACR1 and NIACR2 is not regulated by ligand binding. Moreover, detection of niacin receptor dimers in both plasma membrane- and endoplasmic reticulum-enriched fractions suggests that they are formed early in the biosynthetic pathway. Taken together, these results demonstrate that niacin receptor dimerization is a constitutive process occurring early during biosynthesis. SN - 1090-2104 UR - https://www.unboundmedicine.com/medline/citation/20380810/Evidence_for_constitutive_dimerization_of_niacin_receptor_subtypes_ DB - PRIME DP - Unbound Medicine ER -