Evidence map›Paper›PMID 29230552›Full record

ArticlePflugers Archiv : European journal of physiology2018

Identification of clustered phosphorylation sites in PKD2L1: how PKD2L1 channel activation is regulated by cyclic adenosine monophosphate signaling pathway.

Eunice Yon June Park, Misun Kwak, Kotdaji Ha, Insuk So

Abstract read
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In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-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

7 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Review
  3. Polycystin Channel Complexes.Annual review of physiology · 2023
    Review
  4. CaThe Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2020
    Article
  5. Review
  6. Article
  7. The role of calmodulin in regulating calcium-permeable PKD2L1 channel activity.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2019
    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 2 institutions in 2 countries.

Eunice Yon June ParkDepartment of Physiology, Seoul National University, College of Medicine, Biomedical Science Building 117, 103 Daehakro, Jongro-gu, Seoul, 110-799, South Korea.
Misun KwakDepartment of Physiology, Seoul National University, College of Medicine, Biomedical Science Building 117, 103 Daehakro, Jongro-gu, Seoul, 110-799, South Korea.
Kotdaji HaDepartment of Physiology, University of California, San Francisco, CA, 94158-2517, USA.
Insuk SoDepartment of Physiology, Seoul National University, College of Medicine, Biomedical Science Building 117, 103 Daehakro, Jongro-gu, Seoul, 110-799, South Korea. insuk@snu.ac.kr.
Seoul National University · KRUniversity of California, San Francisco · US

Funding

Ministry of Science, ICT and Future Planning 2015R1A2A1A05001756
6 · The paper itself

Abstract

Polycystic kidney disease 2-like-1 (PKD2L1), or polycystin-L or TRPP2, formerly TRPP3, is a transient receptor potential (TRP) superfamily member. It is a calcium-permeable non-selective cation channel that regulates intracellular calcium concentration and thereby calcium signaling. PKD2L1 has been reported to take part in hedgehog signaling in renal primary cilia and sour tasting coupling with PKD1L3. In addition to the previous reports, PKD2L1 is recently found to play a crucial role in localization with β2-adrenergic receptor (β2AR) on the neuronal primary cilia. The disruption of PKD2L1 leads to the loss of β2AR on the primary cilia and reduction in intracellular concentration of cyclic adenosine monophosphate (cAMP). Since the role of cAMP and PKA is frequently mentioned in the studies of PKD diseases, we investigated on the mechanism of cAMP regulation in relation to the function of PKD2L1 channel. In this study, we observed the activity of PKD2L1 channel increased by the downstream cascades of β2AR and found the clustered phosphorylation sites, Ser-682, Ser-685, and Ser-686 that are significant in the channel regulation by phosphorylation.

Indexed as

Signal TransductionBinding SitesCalcium ChannelsCyclic AMPCyclic AMP-Dependent Protein KinasesHEK293 CellsHumansPhosphorylationReceptors, Cell SurfaceCalcium ChannelsCyclic AMPCyclic AMP-Dependent Protein KinasesPKD2L1 protein, humanReceptors, Cell SurfaceCalciumcAMPIon channelPhosphorylationPKD2L1TRPP3

Identifiers

PMID29230552
OpenAlexW2773595753

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.