Native and cloned 5-HT(3A)(S) receptors are anchored to F-actin in clonal cells and neurons

Using selective antibodies to visualize the short isoform of the 5-HT(3A) receptor, we report here that both native and cloned 5-HT(3A)(S) receptors formed clusters associated with F-actin in all cell types studied. NG 108-15 cells expressing native 5-HT(3A)(S) receptors, COS-7 cells transiently exp...

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Bibliographic Details
Published in:Molecular and cellular neuroscience 2002-05, Vol.20 (1), p.110-124
Main Authors: Emerit, Michel B, Doucet, Edith, Darmon, Michèle, Hamon, Michel
Format: Article
Language:English
Subjects:
Actins - metabolism
Animals
Binding Sites - drug effects
Binding Sites - physiology
Bridged Bicyclo Compounds, Heterocyclic - pharmacology
Cell Membrane - metabolism
Central Nervous System - cytology
Central Nervous System - metabolism
CHO Cells
Clone Cells - cytology
Clone Cells - metabolism
Cloning, Molecular
COS Cells
Cricetinae
Culture Media, Serum-Free - pharmacology
Cytoskeleton - metabolism
Fetus
Gene Expression Regulation - physiology
Hippocampus - cytology
Hippocampus - metabolism
Macromolecular Substances
Molecular Conformation
Neurons - cytology
Neurons - metabolism
Polymers - metabolism
Rats
Receptors, Serotonin - drug effects
Receptors, Serotonin - genetics
Receptors, Serotonin - metabolism
Receptors, Serotonin, 5-HT3
Synaptic Transmission - genetics
Thiazoles - pharmacology
Thiazolidines
Transfection
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Summary:Using selective antibodies to visualize the short isoform of the 5-HT(3A) receptor, we report here that both native and cloned 5-HT(3A)(S) receptors formed clusters associated with F-actin in all cell types studied. NG 108-15 cells expressing native 5-HT(3A)(S) receptors, COS-7 cells transiently expressing 5-HT(3A)(S) subunits, and CHO cells stably transfected with a plasmid encoding the 5-HT(3A)(S) sequence all exhibited similar surface receptor topology with 5-HT(3A)(S) receptor cluster accumulation in F-actin-rich lamellipodia and microspikes. Colocalization and coclustering of 5-HT(3A)(S) subunits and F-actin were also observed in transfected hippocampal neurons. Treatment of the neurons with latrunculin-A, a compound altering F-actin polymerization, demonstrated that 5-HT(3A)(S) receptor cluster size and topology were dependent on F-actin integrity. These results suggest that the anchoring of 5-HT(3A)(S) receptor clusters to the cytoskeletal network probably plays a key role in the physiological regulation of the receptor topology and dynamics, as is the case for other members of the 4-TMD ion channel receptor family.
ISSN:1044-7431