Assembly and Cell Surface Expression of Homomeric and Heteromeric 5-HT3 Receptors: The Role of Oligomerization and Chaperone Proteins

@article{Boyd2002AssemblyAC,
  title={Assembly and Cell Surface Expression of Homomeric and Heteromeric 5-HT3 Receptors: The Role of Oligomerization and Chaperone Proteins},
  author={Gary W. Boyd and Pamela J. Low and James I Dunlop and Laura A. Robertson and Audrey Vardy and Jeremy J. Lambert and John A. Peters and Christopher N. Connolly},
  journal={Molecular and Cellular Neuroscience},
  year={2002},
  volume={21},
  pages={38-50}
}
The ability of differing subunit combinations of 5-HT3 receptors to form functional cell surface receptors was analyzed by a variety of approaches. The results revealed that 5-HT3 receptor assembly occurred within the endoplasmic reticulum (ER) and involved the interaction with chaperone proteins. The 5-HT3A subunit could assemble into functional homomeric receptors that were expressed on the cell surface. In contrast, the 5-HT3B subunit did not exhibit 5-hydroxytryptamine binding or function… 
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84 Citations

Cell Surface Expression of 5-Hydroxytryptamine Type 3 Receptors Is Controlled by an Endoplasmic Reticulum Retention Signal*
TLDR
This study addresses the mechanism controlling the release of 5-HT3B from the endoplasmic reticulum (ER) and identifies the presence of an ER retention signal located within the first cytoplasmic loop between transmembrane domains I and II of5-HT2B.
RIC-3 Exclusively Enhances the Surface Expression of Human Homomeric 5-Hydroxytryptamine Type 3A (5-HT3A) Receptors Despite Direct Interactions with 5-HT3A, -C, -D, and -E Subunits*
TLDR
It is shown that RIC-3 can interact with 5- HT3A, -C, -D, and -E subunits and predominantly enhances the surface expression of homomeric 5-HT3A receptors in HEK293 cells.
Differential Subcellular Localization of RIC-3 Isoforms and Their Role in Determining 5-HT3 Receptor Composition*
TLDR
Both isoforms of RIC-3 play a role in determining 5-HT3 receptor composition, with isoform d capable of enhancing homomeric, and inhibiting heteromersic, 5- HT3 receptor expression.
The Role of Oligomerization in G Protein-Coupled Receptor Maturation
TLDR
Progress is still being made to determine the cellular implications of the relatively novel concept of GPCR oligomers, as well as the formation and functional significance of oligomerization in these other receptor families.
Assembly and trafficking of nicotinic and 5HT3 receptors.
TLDR
The RIC3 protein has been identified as an a7-interacting protein which promotes the efficient assembly and folding of the subunit and may be mediated by both the N- and C-terminal domains of 5HT3A.
The 5-HT3AB receptor shows an A3B2 stoichiometry at the plasma membrane.
Cell Surface Expression of 5-Hydroxytryptamine Type 3 Receptors Is Promoted by RIC-3*
TLDR
The role of RIC-3 in the recruitment of 5-hydroxytryptamine type 3A (5-HT3A) receptors to the cell surface is investigated and it is found that its presence enhances both receptor transport and function in a concentration-dependent manner.
The 5-HT 3 AB Receptor Shows an A 3 B 2 Stoichiometry at the Plasma Membrane
TLDR
The straightforward and unambiguous combination of plasma membrane-sheet isolation, fluorescence intensity ratios, and FRET is a generally promising procedure for determining stoichiometry of proteins on the plasma membrane.
Glutamate Receptor Trafficking: Endoplasmic Reticulum Quality Control Involves Ligand Binding and Receptor Function
TLDR
Results confirm the role of R523, T690, and E738 directly in ligand binding to GluR6 and further support the previous report that nonfunctional GluRs are retained intracellularly by a functional checkpoint in ER quality control.
Atomic force microscopy reveals the stoichiometry and subunit arrangement of 5-HT3 receptors.
TLDR
It is found that, for the 5-HT 3A/B receptor, the distribution of angles between antibodies against the A-subunit had a single peak at approximately 144 degrees, whereas the distribution for antibody against the B-subunits had two peaks at approximately 72 degrees and 144 degrees.
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