mProX™ Human GPR61 Stable Cell Line
- Product Category:
- Membrane Protein Stable Cell Lines
- Subcategory:
- GPCR Cell Lines
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Published Data
Fig.1 Knockdown of GPR61 in Neuro2A cells.
RNA was extracted from Neuro2A cells transfected with lentiviruses carrying sh-RNA, and real-time PCR analysis was performed on these samples. The results demonstrated a significant reduction in the relative expression of the target GPCRs due to the presence of their respective sh-RNA molecules, as confirmed by statistical analysis using Student's t-test (n = 5, *, P<0.05 and **, P<0.01).
Ref: Hossain, Md Shamim, Kurumi Mineno, and Toshihiko Katafuchi. "Neuronal orphan G-protein coupled receptor proteins mediate plasmalogens-induced activation of ERK and Akt signaling." PloS one 11.3 (2016): e0150846.
Pubmed: 26934370
DOI: 10.1371/journal.pone.0150846
Research Highlights
Lees JA, et al. "An inverse agonist of orphan receptor GPR61 acts by a G protein-competitive ." Nature communications, 2023.
GPR61, an orphan G-protein coupled receptor (GPCR) linked to biogenic amine receptors, is being investigated as a potential target for treating appetite-related phenotypes such as obesity and cachexia. However, due to a lack of structural information and knowledge of a biological ligand or tool compound, comprehensive studies on GPR61 have been limited. In this study, the authors present a structural analysis of GPR61 in both its active and inactive states, as well as the identification of a potent and selective small-molecule inverse agonist. These findings shed light on the structure and function of this orphan GPCR and provide valuable insights for further research.
Pubmed:
37741852
DOI:
10.1038/s41467-023-41646-3
Nie Y, et al. "Specific binding of GPR174 by endogenous lysophosphatidylserine leads to high ." Nature communications, 2023.
The study focused on exploring the role of endogenous ligands in the activation of orphan G protein-coupled receptors (GPCRs), a group of proteins that have received limited attention due to unknown ligands. Through the use of cryo-electron microscopy, researchers investigated the structures of three class A/rhodopsin-like orphan GPCRs, namely GPR61, GPR161 and GPR174, in complex with G(s) without the presence of exogenous ligands. It was found that GPR174 interacts with the endogenous lysophosphatidylserine (lysoPS) ligand, resulting in maximal activation. Mutations in GPR174 with reduced ligand binding affinity showed specific activation by lysoPS. Additionally, the structures of GPR161 and GPR61 revealed the involvement of the second extracellular loop (ECL2) in the receptor's orthosteric pocket, possibly contributing to constitutive activity. These findings provide valuable insights into the activation of orphan GPCRs by endogenous ligands and suggest that high constitutive activity may be attributed to naturally occurring ligands.
Pubmed:
37737235
DOI:
10.1038/s41467-023-41654-3
