ArticleThe Journal of biological chemistry2014
Identification and functional characterization of the phosphorylation sites of the neuropeptide FF2 receptor.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Ubiquitination plays a key role in an insecticide resistance fitness cost.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Functional crosstalk between neuropeptide FF system and N-type voltage-gated calcium channels in ziconotide-mediated antinociception in mice.Psychopharmacology · 2026Article
- Group A Streptococcus interacts with glycosaminoglycans via M proteins to modulate bacterial adherence in vitro.The FEBS journal · 2025Article
- An Overview on Renal and Central Regulation of Blood Pressure by Neuropeptide FF and Its Receptors.International journal of molecular sciences · 2024Review
- GPCR-MAPK signaling pathways underpin fitness trade-offs in whitefly.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Hydrophobic cue-induced appressorium formation depends on MoSep1-mediated MoRgs7 phosphorylation and internalization in Magnaporthe oryzae.PLoS genetics · 2023Article
- Article
- G Protein-Coupled Receptor Signaling Through β-Arrestin-Dependent Mechanisms.Journal of cardiovascular pharmacology · 2017Review
- Identification and functional characterisation of 5-HT4 receptor in sea cucumber Apostichopus japonicus (Selenka).Scientific reports · 2017Article
- Novel Structural Approaches to Study GPCR Regulation.International journal of molecular sciences · 2016Review
- Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The neuropeptide FF2 (NPFF2) receptor belongs to the rhodopsin family of G protein-coupled receptors and mediates the effects of several related RFamide neuropeptides. One of the main pharmacological interests of this system resides in its ability to regulate endogenous opioid systems, making it a potential target to reduce the negative effects of chronic opioid use. Phosphorylation of intracellular residues is the most extensively studied post-translational modification regulating G protein-coupled receptor activity. However, until now, no information concerning NPFF2 receptor phosphorylation is available. In this study, we combined mass spectrometric analysis and site-directed mutagenesis to analyze for the first time the phosphorylation pattern of the NPFF2 receptor and the role of the various phosphorylation sites in receptor signaling, desensitization, and trafficking in a SH-SY5Y model cell line. We identified the major, likely GRK-dependent, phosphorylation cluster responsible for acute desensitization, (412)TNST(415) at the end of the C terminus of the receptor, and additional sites involved in desensitization ((372)TS(373)) and internalization (Ser(395)). We thus demonstrate the key role played by phosphorylation in the regulation of NPFF2 receptor activity and trafficking. Our data also provide additional evidence supporting the concept that desensitization and internalization are partially independent processes relying on distinct phosphorylation patterns.
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