Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1803, Issue 7, Pages 813-825Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2010.04.002
Keywords
G protein-coupled receptor; Muscarinic acetylcholine receptor; Receptor oligomerization
Categories
Funding
- Ministerio de Ciencia e Innovacion [SAF2005-0848-C04-02, SAF2002-0345-C0302, SAF2008-01462, CSD2008-00005]
- European Social Foundation [FI2004]
- Catalonian Government [BE-2006]
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Besides some pharmacological, biochemical and biophysical evidences support the contention that muscarinic acetylcholine receptors can form homo- and heterodimers, the existence of specific M-3 and M-5 muscarinic receptors oligomers in living cells is a new concept Interestingly, this phenomenon might have relevance in lymphocytic cholinergic function since both T- and B-cells naturally express high levels of these two receptor subtypes. Here, by means of co-immunoprecipitation and bioluminescence resonance energy transfer methods we demonstrated that M-3 and M-5 muscarinic receptors could form constitutive homo- and heterodimers in transiently transfected HEK-293T cells. Interestingly, this receptor-receptor interaction was unaltered by carbachol treatment but it was affected by the expression of a peptide corresponding to a portion of the third intracellular loop of the M-5 muscarinic receptor. In addition, the same peptide was able to abrogate the carbachol-induced mitogen-activated protein kinase phosphorylation and the carbachol-enhanced PHA-induced IL-2 production in derived lymphocytic T cells. Overall, these results suggest that the third intracellular loop of the M-5 muscarinic receptor might play a regulatory role in receptor function and heteromerization, thus providing the molecular framework for a potential cholinergic-based therapeutic intervention of the immune system. (C) 2010 Elsevier B.V. All rights reserved.
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