ArticlePloS one2011
C-terminal di-leucine motif of dopamine D₁ receptor plays an important role in its plasma membrane trafficking.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Sorting nexins: role in the regulation of blood pressure.The FEBS journal · 2023Review
- Lipid Rafts and Dopamine Receptor Signaling.International journal of molecular sciences · 2020Review
- Lipid rafts are required for effective renal DFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- The emerging role of sorting nexins in cardiovascular diseases.Clinical science (London, England : 1979) · 2019Review
- Regulation of αScientific reports · 2016Article
- GGA3 Interacts with a G Protein-Coupled Receptor and Modulates Its Cell Surface Export.Molecular and cellular biology · 2016Article
- Mutations in XPR1 cause primary familial brain calcification associated with altered phosphate export.Nature genetics · 2015Article
- Regulation of α2B-Adrenerigc Receptor Export Trafficking by Specific Motifs.Progress in molecular biology and translational science · 2015Review
- β-Arrestin1 and distinct CXCR4 structures are required for stromal derived factor-1 to downregulate CXCR4 cell-surface levels in neuroblastoma.Molecular pharmacology · 2014Article
- Novel role of sorting nexin 5 in renal D(1) dopamine receptor trafficking and function: implications for hypertension.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013Article
- Sorting nexin 1 loss results in D5 dopamine receptor dysfunction in human renal proximal tubule cells and hypertension in mice.The Journal of biological chemistry · 2013Article
- The angiotensin II type 1 receptor C-terminal Lys residues interact with tubulin and modulate receptor export trafficking.PloS one · 2013Article
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The dopamine D₁ receptor (D₁R), a G protein-coupled receptor, plays a critical role in regulating blood pressure through its actions on renal hemodynamics and epithelial ion transport, which are highly linked to its intracellular trafficking. In this study, we generated a series of C-terminal mutants of D₁R that were tagged with or without enhanced yellow fluorescent protein, and analyzed the consequences of these mutants on the plasma membrane trafficking of D₁R and cyclic AMP response to D₁R stimulation. D₁R with mutations within the endocytic recycling signal (amino acid residues 360-382) continued to be functional, albeit decreased relative to wild-type D₁R. Mutation of the palmitoylation site (347C>S) of D₁R did not impair its trafficking to the plasma membrane, but abolished its ability to increase cyclic AMP accumulation. In contrast, replacement of di-leucines (344-345L>A) by alanines resulted in the retention of D₁R in the early endosome, decreased its glycosylation, and prevented its targeting to the plasma membrane. Our studies suggest that di-L motif at the C-terminus of D₁R is critical for the glycosylation and cell surface targeting of D₁R.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.