ArticleThe Journal of biological chemistry2013
Recruitment of a cytoplasmic chaperone relay by the A2A adenosine receptor.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- Cathepsin D interacts with adenosine AThe Journal of biological chemistry · 2022Article
- Genetic tagging of the adenosine A2A receptor reveals its heterogeneous expression in brain regions.Frontiers in neuroanatomy · 2022Article
- Functional characterization of a loss-of-function mutant I324M of arginine vasopressin receptor 2 in X-linked nephrogenic diabetes insipidus.Scientific reports · 2021Article
- Amino Acid Transporter SLC6A14 (ATBFrontiers in cell and developmental biology · 2020Review
- Treprostinil reduces endothelial damage in murine sinusoidal obstruction syndrome.Journal of molecular medicine (Berlin, Germany) · 2019Article
- The Alpha Isoform of Heat Shock Protein 90 and the Co-chaperones p23 and Cdc37 Promote Opioid Anti-nociception in the Brain.Frontiers in molecular neuroscience · 2019Article
- Oxytocin-like signaling in ants influences metabolic gene expression and locomotor activity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Purinergic Receptors in Neurological Diseases With Motor Symptoms: Targets for Therapy.Frontiers in pharmacology · 2018Review
- Subtle modifications to oxytocin produce ligands that retain potency and improved selectivity across species.Science signaling · 2017Article
- Relax, Cool Down and Scaffold: How to Restore Surface Expression of Folding-Deficient Mutant GPCRs and SLC6 Transporters.International journal of molecular sciences · 2017Review
- Hyponatremia and V2 vasopressin receptor upregulation: a result of HSP90 inhibition.Cancer chemotherapy and pharmacology · 2017Article
- Chemical Proteomics for Target Discovery of Head-to-Tail Cyclized Mini-Proteins.Frontiers in chemistry · 2017Article
- Regulation of GPCR expression through an interaction with CCT7, a subunit of the CCT/TRiC complex.Molecular biology of the cell · 2016Article
- Functional Rescue of a MisfoldedThe Journal of biological chemistry · 2016Article
- Repurposing Treprostinil for Enhancing Hematopoietic Progenitor Cell Transplantation.Molecular pharmacology · 2016Article
- GABAB receptor cell-surface export is controlled by an endoplasmic reticulum gatekeeper.Molecular psychiatry · 2016Article
- A salt bridge linking the first intracellular loop with the C terminus facilitates the folding of the serotonin transporter.The Journal of biological chemistry · 2015Article
- Chaperoning of the A1-adenosine receptor by endogenous adenosine - an extension of the retaliatory metabolite concept.Molecular pharmacology · 2015Article
- A cytosolic relay of heat shock proteins HSP70-1A and HSP90β monitors the folding trajectory of the serotonin transporter.The Journal of biological chemistry · 2014Article
- [MUV Researcher of the Month, October 2014].Wiener klinische Wochenschrift · 2014Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The adenosine A2A receptor is a prototypical rhodopsin-like G protein-coupled receptor but has several unique structural features, in particular a long C terminus (of >120 residues) devoid of a palmitoylation site. It is known to interact with several accessory proteins other than those canonically involved in signaling. However, it is evident that many more proteins must interact with the A2A receptor, if the trafficking trajectory of the receptor is taken into account from its site of synthesis in the endoplasmic reticulum (ER) to its disposal by the lysosome. Affinity-tagged versions of the A2A receptor were expressed in HEK293 cells to identify interacting partners residing in the ER by a proteomics approach based on tandem affinity purification. The receptor-protein complexes were purified in quantities sufficient for analysis by mass spectrometry. We identified molecular chaperones (heat-shock proteins HSP90α and HSP70-1A) that interact with and retain partially folded A2A receptor prior to ER exit. Complex formation between the A2A receptor and HSP90α (but not HSP90β) and HSP70-1A was confirmed by co-affinity precipitation. HSP90 inhibitors also enhanced surface expression of the receptor in PC12 cells, which endogenously express the A2A receptor. Finally, proteins of the HSP relay machinery (e.g. HOP/HSC70-HSP90 organizing protein and P23/HSP90 co-chaperone) were recovered in complexes with the A2A receptor. These observations are consistent with the proposed chaperone/coat protein complex II exchange model. This posits that cytosolic HSP proteins are sequentially recruited to folding intermediates of the A2A receptor. Release of HSP90 is required prior to recruitment of coat protein complex II components. This prevents premature ER export of partially folded receptors.
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Registered trials
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