Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein

@article{Bermak2001RegulationOT,
  title={Regulation of transport of the dopamine D1 receptor by a new membrane-associated ER protein},
  author={Jason C. Bermak and Ming Li and Clayton M. Bullock and Qun Zhou},
  journal={Nature Cell Biology},
  year={2001},
  volume={3},
  pages={492-498}
}
Many structural determinants for G protein-coupled receptor (GPCR) functions have been defined, but little is known concerning the regulation of their transport from the endoplasmic reticulum (ER) to the cell surface. Here we show that a carboxy-terminal hydrophobic motif, FxxxFxxxF, which is highly conserved among GPCRs, functions independently as an ER-export signal for the dopamine D1 receptor. A newly identified ER-membrane-associated protein, DRiP78, binds to this motif. Overexpression or… 

Regulation of Transport of the Angiotensin AT2 Receptor by a Novel Membrane-Associated Golgi Protein

The results indicate that ATBP50 regulates the transport of the AT2R to cell membrane by binding to a specific motif within its cytoplasmic carboxy-terminal and thereby enabling the antiproliferative effects of the receptor.

ER-bound steps in the biosynthesis of G protein-coupled receptors.

X-ray structures reveal a common polypeptide topology with little variation in the alignment and orientation of the seven transmembrane segments, the proximal carboxyl terminus (C-tail) and parts of the extracellular loops, which probably represents a major criterion for the receptor to pass endoplasmic reticulum (ER) quality control.

Anterograde trafficking of nascent α(2B)-adrenergic receptor: structural basis, roles of small GTPases.

α2B-Adrenergic Receptor Interaction with Tubulin Controls Its Transport from the Endoplasmic Reticulum to the Cell Surface*

The data provide the first evidence indicating that the α2B-AR C-terminal Arg cluster mediates its association with tubulin to coordinate its ER-to-cell surface traffic and suggest a novel mechanism of GPCR export through physical contact with microtubules.

Regulation of Anterograde Transport of α2-Adrenergic Receptors by the N Termini at Multiple Intracellular Compartments*

The Tyr-Ser motif, highly conserved in the membrane-proximal N termini of all α2-AR subtypes, is required for the exit of α2A-AR and α2B-AR from the Golgi apparatus, thus representing a novel Tyr-based motif modulating GPCR transport at the GolGI level.

Identification of a Novel Endocytic Recycling Signal in the D1 Dopamine Receptor*

This work identifies a novel sorting signal controlling the endocytic trafficking itinerary of a physiologically important dopamine receptor, provides the first example of such a sorting signal functioning in a proximal portion of the carboxyl-terminal cytoplasmic domain, and suggests the existence of a diverse array of sorting signals in the GPCR superfamily that mediate subtype-specific regulation of receptors viaendocytic membrane trafficking.
...

References

SHOWING 1-10 OF 40 REFERENCES

Modulation of dopamine D(2) receptor signaling by actin-binding protein (ABP-280).

A mechanism for a new molecular mechanism of modulating D(2) receptor signaling by cytoskeletal protein interaction is suggested, as determined by immunocytochemical analysis in ABP-deficient and replete cells.

Multiple GTP-binding proteins regulate vesicular transport from the ER to Golgi membranes

Results are consistent with the hypothesis that multiple GTP-binding proteins including a heterotrimeric G protein(s), ARF and rab1 differentially regulate steps in the transport of protein between early compartments of the secretory pathway.

Effects of truncations of the cytoplasmic tail of the luteinizing hormone/chorionic gonadotropin receptor on receptor-mediated hormone internalization.

It is suggested that a region(s) between residues 616 and 631 of the rLH/CG receptor are required for proper insertion and/or targeting of the receptor into the plasma membrane, and both hCG-stimulated cAMP production and hCG internalization are enhanced by the removal of the distal portion of the cytoplasmic tail.

RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor

It is shown that a receptor with seven transmembrane domains, the calcitonin-receptor-like receptor (CRLR), can function as either a CGRP receptor or an adrenomedullin receptor, depending on which members of a new family of single-trans Membrane-domain proteins, which are called receptor-activity-modifying proteins or RAMPs, are expressed.

Internal trafficking and surface mobility of a functionally intact beta2-adrenergic receptor-green fluorescent protein conjugate.

It is demonstrated that real-time optical measurements of beta2AR (as well as other GPCR) interactions and dynamics on living cells are feasible and fidelity of the biochemical properties of thebeta2AR/S65T/GFP can be engineered.

Sorting Determinants in the Transmembrane Domain of p24 Proteins*

The role of the transmembrane domain (TMD) of a p24 protein isolated from COPI-coated intra-Golgi transport vesicles is analyzed and TMD residues of p24 proteins may mediate the interaction with integral membrane proteins of the vesicle budding machinery to ensure p24 packaging into transportVesicles.

Export from the Endoplasmic Reticulum Represents the Limiting Step in the Maturation and Cell Surface Expression of the Human δ Opioid Receptor*

The overall low efficiency of receptor maturation, less than 50% of the precursor being processed to the fully glycosylated protein, suggests that only a fraction of the synthesized receptors attain properly folded conformation that allows exit from the ER.

Regulatory mechanisms that modulate signalling by G-protein-coupled receptors.

A greater understanding of the mechanisms that modulate signalling may lead to the development of new therapies and may help to explain the mechanism of drug tolerance.

The Recycling of ERGIC-53 in the Early Secretory Pathway

The results suggest that the ER-exit of ERGIC-53 is mediated by direct interaction of its cytosolic tail with the Sec23p·Sec24p complex of COPII and that protein sorting at the level of the ER occurs by a mechanism similar to receptor-mediated endocytosis or Golgi to ER retrograde transport.