Evidence map›Paper›PMID 20959467›Full record

ArticleThe Journal of biological chemistry2010

Ligand-induced internalization and recycling of the human neuropeptide Y2 receptor is regulated by its carboxyl-terminal tail.

Cornelia Walther, Stefanie Nagel, Luis E Gimenez, Karin Mörl, Vsevolod V Gurevich, Annette G Beck-Sickinger

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.9field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. DynamicNano letters · 2022
    Article
  6. Review
  7. Article
  8. Review
  9. Unusually persistent GαCell communication and signaling : CCS · 2020
    Article
  10. The structural basis of the arrestin binding to GPCRs.Molecular and cellular endocrinology · 2019
    Review
  11. Identifying the localization and exploring a functional role for Gprc5c in the kidney.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  12. C-terminal motif of human neuropeptide YCellular signalling · 2017
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Targeting individual GPCRs with redesigned nonvisual arrestins.Handbook of experimental pharmacology · 2014
    Article
  19. Structural determinants of arrestin functions.Progress in molecular biology and translational science · 2013
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Cornelia WaltherFaculty of Biosciences, Institute of Biochemistry, Leipzig University, Brüderstrasse 34, 04103 Leipzig, Germany.
Stefanie Nagel
Luis E Gimenez
Karin Mörl
Vsevolod V Gurevich
Annette G Beck-Sickinger
Leipzig University · DEVanderbilt University · US

Funding

Conformational regulation of arrestin-mediated signalingR01GM081756 · NIGMS · VANDERBILT UNIVERSITY · PI GUREVICH, VSEVOLOD V. · 2008 to 2011
$1.5M
NIGMS NIH HHS GM081756NIGMS NIH HHS R01 GM081756
6 · The paper itself

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 Y(2) receptor (hY(2)R), 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 (373)DSXTEXT(379) was found to be the primary regulatory internalization sequence acting in concert with arrestin-3, the proximal motif (347)DXXXSEXSXT(356) promoted ligand-induced internalization in an arrestin-3-independent manner. Moreover, we identified a regulatory sequence located between these internalization motifs ((357)FKAKKNLEVRKN(368)), which serves as an inhibitory element. We found that hY(2)R recycling is also governed by structural determinants within the proximal internalization motif. In conclusion, these results indicate that the hY(2)R 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 hY(2)R, which is likely applicable to other GPCRs.

Indexed as

Gene Expression RegulationAmino Acid MotifsAnimalsArrestinsChlorocebus aethiopsCOS CellsEndocytosisFluorescence Resonance Energy TransferHumansLigandsMicroscopy, FluorescenceMutationNeuropeptidesProtein Structure, TertiaryReceptors, Neuropeptide Yarrestin3ArrestinsLigandsNeuropeptidesneuropeptide Y2 receptorReceptors, Neuropeptide Y

Identifiers

PMID20959467
PMCPMC3009885
OpenAlexW2069805230

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.