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• W2069805230 endingPage "41590" @default.
• W2069805230 startingPage "41578" @default.
• W2069805230 abstract "Agonist-induced internalization of G protein-coupled receptors plays an important role in signal regulation. The underlying mechanisms of the internalization of the human neuropeptide Y2 receptor (hY2R), as well as its desensitization, endocytosis, and resensitization are mainly unknown. In the present study we have investigated the role of carboxyl-terminal (C-terminal) Ser/Thr residues and acidic amino acids in regulating receptor internalization, arrestin interaction, and recycling by fluorescence microscopy, cell surface enzyme-linked immunosorbent assay, and bioluminescence resonance energy transfer in several cell lines. Strikingly, C-terminal truncation mutants revealed two different internalization motifs. Whereas a distal motif 373DSXTEXT379 was found to be the primary regulatory internalization sequence acting in concert with arrestin-3, the proximal motif 347DXXXSEXSXT356 promoted ligand-induced internalization in an arrestin-3-independent manner. Moreover, we identified a regulatory sequence located between these internalization motifs (357FKAKKNLEVRKN368), which serves as an inhibitory element. We found that hY2R recycling is also governed by structural determinants within the proximal internalization motif. In conclusion, these results indicate that the hY2R C terminus is involved in multiple molecular events that regulate internalization, interaction with arrestin-3, and receptor resensitization. Our findings provide novel insights into complex mechanisms of controlled internalization of hY2R, which is likely applicable to other GPCRs. Agonist-induced internalization of G protein-coupled receptors plays an important role in signal regulation. The underlying mechanisms of the internalization of the human neuropeptide Y2 receptor (hY2R), as well as its desensitization, endocytosis, and resensitization are mainly unknown. In the present study we have investigated the role of carboxyl-terminal (C-terminal) Ser/Thr residues and acidic amino acids in regulating receptor internalization, arrestin interaction, and recycling by fluorescence microscopy, cell surface enzyme-linked immunosorbent assay, and bioluminescence resonance energy transfer in several cell lines. Strikingly, C-terminal truncation mutants revealed two different internalization motifs. Whereas a distal motif 373DSXTEXT379 was found to be the primary regulatory internalization sequence acting in concert with arrestin-3, the proximal motif 347DXXXSEXSXT356 promoted ligand-induced internalization in an arrestin-3-independent manner. Moreover, we identified a regulatory sequence located between these internalization motifs (357FKAKKNLEVRKN368), which serves as an inhibitory element. We found that hY2R recycling is also governed by structural determinants within the proximal internalization motif. In conclusion, these results indicate that the hY2R C terminus is involved in multiple molecular events that regulate internalization, interaction with arrestin-3, and receptor resensitization. Our findings provide novel insights into complex mechanisms of controlled internalization of hY2R, which is likely applicable to other GPCRs." @default.
• W2069805230 created "2016-06-24" @default.
• W2069805230 creator A5001319749 @default.
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• W2069805230 creator A5068125461 @default.
• W2069805230 creator A5073399193 @default.
• W2069805230 date "2010-12-01" @default.
• W2069805230 modified "2023-10-13" @default.
• W2069805230 title "Ligand-induced Internalization and Recycling of the Human Neuropeptide Y2 Receptor Is Regulated by Its Carboxyl-terminal Tail" @default.
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• W2069805230 doi "https://doi.org/10.1074/jbc.m110.162156" @default.
• W2069805230 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3009885" @default.
• W2069805230 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20959467" @default.
• W2069805230 hasPublicationYear "2010" @default.
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