Role of the C Terminus in Neuropeptide Y Y Receptor Desensitization and Internalization
Molecular Pharmacology, ISSN: 0026-895X, Vol: 67, Issue: 3, Page: 655-664
2005
- 36Citations
- 23Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations36
- Citation Indexes36
- 36
- CrossRef35
- Captures23
- Readers23
- 23
Article Description
We have studied truncation mutants of the rat neuropeptide Y (NPY) Y 1 receptor lacking four (Thr361stop, Y1T361*) or eight (Ser352stop, Y1S352*) potential serine/threonine C-terminal phosphorylation sites. NPY-stimulated hemagglutinin-tagged Y1, Y1T361*, and Y1S352* receptors all efficiently activated G proteins in Chinese hamster ovary (CHO) cell membranes, but desensitization after NPY pretreatment was only prevented in the HAY1S352* clone. In transfected colonic carcinoma epithelial layers, functional Y1 and Y1T361* peptide YY responses became more transient as the agonist concentration increased, whereas those mediated by the Y1S352* receptor remained sustained. NPY-stimulated HAY1 receptor phosphorylation was increased by transient overexpression of G protein-coupled receptor kinase 2, and only Ser352stop truncation abolished this response in CHO or human embryonic kidney (HEK) 293 cells. Rapid internalization of cell-surface HAY1 receptors in HEK293 cells was observed in response to agonist, resulting in partial colocalization with transferrin, a marker for clathrin-mediated endocytosis and recycling. It is surprising that both truncated receptors were constitutively internalized, predominantly in transferrin-positive compartments. NPY increased cell-surface localization of HAY1S352* receptors, whereas the distribution of both mutants was unaltered by BIBO3304. Recruitment of green fluorescent protein-tagged β-arrestin2 to punctate endosomes was observed only for HAY1 and HAY1T361* receptors and solely under NPY-stimulated conditions. Thus, the key C-terminal sequence between Ser352 and Lys360 is a major site for Y 1 receptor phosphorylation, is critical for its desensitization, and contributes to the association between the receptor and β-arrestin proteins. However, additional β-arrestin–independent mechanisms control Y 1 receptor trafficking under basal conditions.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0026895X24054828; http://dx.doi.org/10.1124/mol.104.006114; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=14944381164&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/15576634; https://linkinghub.elsevier.com/retrieve/pii/S0026895X24054828; https://dx.doi.org/10.1124/mol.104.006114; https://molpharm.aspetjournals.org/content/67/3/655
Elsevier BV
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