English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Preprint

A new class of receptors: Lipids regulate mammalian Gsalpha-stimulated adenylyl cyclase activities via their membrane anchors

MPS-Authors
/persons/resource/persons272125

Fuchs,  A       
Protein Folding, Unfolding and Degradation Group, Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society;
Department Protein Evolution, Max Planck Institute for Biology Tübingen, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Landau, M., Elsabbagh, S., Gross, H., Fuchs, A., Schultz, A., & Schultz, J. (submitted). A new class of receptors: Lipids regulate mammalian Gsalpha-stimulated adenylyl cyclase activities via their membrane anchors.


Cite as: https://hdl.handle.net/21.11116/0000-000F-E07F-6
Abstract
The biosynthesis of cAMP by mammalian membrane-bound adenylyl cyclases (mACs) is predominantly regulated by G-protein-coupled-receptors (GPCRs). Up to now the two hexahelical transmembrane domains of mACs were considered to fix the enzyme to membranes. Here we show that the transmembrane domains serve in addition as signal receptors and transmitters of lipid signals that control Gsalpha-stimulated mAC activities. We identify aliphatic fatty acids and anandamide as receptor ligands of mAC isoforms 1 to 7 and 9. The ligands enhance (mAC isoforms 2, 3, 7, and 9) or attenuate (isoforms 1, 4, 5, and 6) Gsalpha-stimulated mAC activities in vitro and in vivo. Substitution of the stimulatory membrane receptor of mAC3 by the inhibitory receptor of mAC5 results in a ligand inhibited mAC5-mAC3 chimera. Thus, we discovered a new class of membrane receptors in which two signaling modalities are at a crossing, direct tonic lipid and indirect phasic GPCR-Gsalpha signaling regulating the biosynthesis of cAMP.