Evidence map›Paper›PMID 23360390›Full record

ArticleThe Biochemical journal2013

Phosphorylation regulates TRPV1 association with β-arrestin-2.

Elaine D Por, Ruben Gomez, Armen N Akopian, Nathaniel A Jeske

Abstract read
In one paragraph

Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

18 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Integrating TRPV1 Receptor Function with Capsaicin Psychophysics.Advances in pharmacological sciences · 2016
    Review
  16. Article
  17. Review
  18. 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

4 authors at 1 institution in 1 country.

Elaine D PorDepartment of Pharmacology, The University of Texas Health Science Center, San Antonio, TX 78229, USA.
Ruben Gomez
Armen N Akopian
Nathaniel A Jeske
The University of Texas Health Science Center at San Antonio · US

Funding

AKAP MODULATES TRPV1 PHOSPHORYLATION AND SENSITIZATIONR01NS061884 · NINDS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI JESKE, NATHANIEL AARON · 2008 to 2011
$1.3M
TRPV1 regulation by B-arrestinsF31DE022517 · NIDCR · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI POR, ELAINE DARCEY · 2011 to 2012
$44k
NIDCR NIH HHS F31 DE022517NIDCR NIH HHS F31DE022517-01NINDS NIH HHS R01 NS061884
6 · The paper itself

Abstract

Post-translational modifications in TRPV1 (transient receptor potential vanilloid 1) play a critical role in channel activity. Phosphorylation of serine/threonine residues within the N- and C-termini of TRPV1 are implicated in receptor sensitization and activation. Conversely, TRPV1 desensitization occurs via a calcium-dependent mechanism and leads to receptor de-phosphorylation. Importantly, we recently demonstrated that TRPV1 association with β-arrestin-2 is critical to receptor desensitization via its ability to scaffold the phosphodiesterase PDE4D5 to the receptor, regulating TRPV1 phosphorylation. In the present study, we demonstrate that phosphorylation of TRPV1 and β-arrestin-2 regulates this association at the membrane. Under serum-free media conditions, we observed a significant decrease in TRPV1 and β-arrestin-2 association in transfected CHO (Chinese-hamster ovary) cells. Pharmacological activation of the kinases PKA (protein kinase A) and PKC (protein kinase C) led to a robust increase in TRPV1 and β-arrestin-2 association, whereas inhibition of PKA and PKC decreased association. Previously, we identified potential PKA residues (Ser(116), Thr(370)) in the N-terminus of TRPV1 modulated by β-arrestin-2. In the present study we reveal that the phosphorylation status of Thr(370) dictates the β-arrestin-2 and TRPV1 association. Furthermore, we demonstrate that CK2 (casein kinase 2)-mediated phosphorylation of β-arrestin-2 at Thr(382) is critical for its association with TRPV1. Taken together, the findings of the present study suggest that phosphorylation controls the association of TRPV1 with β-arrestin-2.

Indexed as

AnimalsArrestinsbeta-Arrestin 2beta-ArrestinsCasein Kinase IICell MembraneCHO CellsCricetinaeCricetulusCyclic AMP-Dependent Protein KinasesPhosphorylationProtein BindingProtein Kinase CProtein Structure, TertiaryRatsTRPV Cation ChannelsArrb2 protein, ratArrestinsbeta-Arrestin 2beta-ArrestinsCasein Kinase IICyclic AMP-Dependent Protein KinasesProtein Kinase CTrpv1 protein, ratTRPV Cation Channels

Identifiers

PMID23360390
PMCPMC13551559
OpenAlexW2000104695

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.