Evidence map›Paper›PMID 19244406›Full record

ReviewAmerican journal of physiology. Renal physiology2009

Function and regulation of TRPP2 at the plasma membrane.

Leonidas Tsiokas

Open access · greenAbstract readReview
In one paragraph

Review in American journal of physiology. Renal physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.8field-weighted citation impact, top 4% 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

33 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Non-voltage-gated CaAmerican journal of physiology. Renal physiology · 2024
    Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Primary Cilia as Signaling Hubs in Health and Disease.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019
    Review
  10. Article
  11. TRPs in Pain Sensation.Frontiers in physiology · 2017
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Polycystins and cellular Ca2+ signaling.Cellular and molecular life sciences : CMLS · 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

1 author at 1 institution in 1 country.

Leonidas TsiokasDepartment of Cell Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA. leonidas-tsiokas@ouhsc.edu
University of Oklahoma Health Sciences Center · US

Funding

UNDERSTANDING THE ROLE OF RETINOL DEHYDROGENASES RDH11 AND RDH12 IN VISIONP20RR017703 · NCRR · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI MANDAL, NAWAJES · 2002 to 2011
$23.6M
Regulation of Ca++ signaling by the PDK 2 gene productR01DK059599 · NIDDK · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI TSIOKAS, LEONIDAS · 2002 to 2020
$4.2M
Regulation of calcium signaling by the PKD2 gene productR56DK059599 · NIDDK · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI TSIOKAS, LEONIDAS · 2010 to 2010
$178k
NCRR NIH HHS P20 RR017703NCRR NIH HHS P20-RR01-7703-06NIDDK NIH HHS DK-59599-07NIDDK NIH HHS R01 DK059599NIDDK NIH HHS R56 DK059599
6 · The paper itself

Abstract

The vast majority (approximately 99%) of all known cases of autosomal dominant polycystic kidney disease (ADPKD) are caused by naturally occurring mutations in two separate, but genetically interacting, loci, pkd1 and pkd2. pkd1 encodes a large multispanning membrane protein (PKD1) of unknown function, while pkd2 encodes a protein (TRPP2, polycystin-2, or PKD2) of the transient receptor potential (TRP) superfamily of ion channels. Biochemical, functional, and genetic studies support a model in which PKD1 physically interacts with TRPP2 to form an ion channel complex that conveys extracellular stimuli to ionic currents. However, the molecular identity of these extracellular stimuli remains elusive. Functional studies in cell culture show that TRPP2 can be activated in response to mechanical cues (fluid shear stress) and/or receptor tyrosine kinase (RTK) and G protein-coupled receptor (GPCR) activation at the cell surface. Recent genetic studies in Chlamydomonas reinhardtii show that CrPKD2 functions in a pathway linking cell-cell adhesion and Ca(2+) signaling. The mode of activation depends on protein-protein interactions with other channel subunits and auxiliary proteins. Therefore, understanding the mechanisms underlying the molecular makeup of TRPP2-containing complexes is critical in delineating the mechanisms of TRPP2 activation and, most importantly, the mechanisms by which naturally occurring mutations in pkd1 or pkd2 lead not only to ADPKD, but also to other defects reported in model organisms lacking functional TRPP2. This review focuses on the molecular assembly, function, and regulation of TRPP2 as a cell surface cation channel and discusses its potential role in Ca(2+) signaling and ADPKD pathophysiology.

Indexed as

AnimalsCalcium SignalingCell MembraneHumansMutationPolycystic Kidney, Autosomal DominantTRPP Cation ChannelsTRPP Cation Channels

Identifiers

PMID19244406
PMCPMC2711710
OpenAlexW2146165694

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.