Serotonin receptor oligomerization regulates cAMP-based signaling.
5-HT1AR
5-HT7R
Epac
FRET
Förster resonance energy transfer
G protein-coupled receptor
GPCR
Hetero-oligomerization
Lux-FRET
Quantitative confocal microscopy
Stoichiometry
cAMP signaling
Journal
Journal of cell science
ISSN: 1477-9137
Titre abrégé: J Cell Sci
Pays: England
ID NLM: 0052457
Informations de publication
Date de publication:
23 08 2019
23 08 2019
Historique:
received:
25
01
2019
accepted:
22
07
2019
pubmed:
3
8
2019
medline:
9
7
2020
entrez:
3
8
2019
Statut:
epublish
Résumé
Protein-protein interaction is often investigated using quantitative molecular microscopy with Förster resonant energy transfer (FRET). Here, we combined 'linear unmixing FRET' (lux-FRET) with the simultaneous application of a FRET-based biosensor for cAMP to investigate the oligomerization between the 5-HT
Identifiants
pubmed: 31371490
pii: jcs.230334
doi: 10.1242/jcs.230334
pii:
doi:
Substances chimiques
Htr1a protein, mouse
0
Receptors, Serotonin
0
serotonin 7 receptor
0
Receptor, Serotonin, 5-HT1A
112692-38-3
Cyclic AMP
E0399OZS9N
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
© 2019. Published by The Company of Biologists Ltd.
Déclaration de conflit d'intérêts
Competing interestsThe authors declare no competing or financial interests.