Evidence map›Paper›PMID 10097141›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Specific association of the gene product of PKD2 with the TRPC1 channel.

L Tsiokas, T Arnould, C Zhu, E Kim, G Walz, V P Sukhatme

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 119 papers.

0numbers the graph read from it
0cells of the map it votes in
119citing papers in PubMed
6.4field-weighted citation impact, top 3% 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

119 citing papers in PubMed, 303 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. The mutual interaction of TRPC5 channel with polycystin proteins.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Polycystin Channel Complexes.Annual review of physiology · 2023
    Review
  12. Review
  13. Review
  14. UsingGenes · 2021
    Review
  15. Store-operated calcium entry: Pivotal roles in renal physiology and pathophysiology.Experimental biology and medicine (Maywood, N.J.) · 2021
    Review
  16. TRPP2 and STIM1 form a microdomain to regulate store-operated CaCell communication and signaling : CCS · 2020
    Article
  17. Review
  18. Review
  19. Article
  20. Review

59 more citing papers are in PubMed but not listed here.

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 1 country.

L TsiokasRenal Division, RW 563, Beth Israel Deaconess Medical Center, Harvard Medical School, 330 Brookline Avenue, Boston, MA 02215, USA.
T Arnould
C Zhu
E Kim
G Walz
V P Sukhatme
Massachusetts General Hospital · USBeth Israel Deaconess Medical Center · US

Funding

STRUCTURE/FUNCTION ANALYSIS OF K CADHERINF32DK009625 · NIDDK · BETH ISRAEL DEACONESS MEDICAL CENTER · PI TSIOKAS, LEONIDAS · 1997 to 1999
–
CLONING A SWEETNESS RECEPTORK20MH001147 · NIMH · MASSACHUSETTS GENERAL HOSPITAL · PI KIM, EMILY E · 1995 to 1999
–
NIDDK NIH HHS DK-09625NIDDK NIH HHS F32 DK009625NIMH NIH HHS MH-01147
6 · The paper itself

Abstract

The function(s) of the genes (PKD1 and PKD2) responsible for the majority of cases of autosomal dominant polycystic kidney disease is unknown. While PKD1 encodes a large integral membrane protein containing several structural motifs found in known proteins involved in cell-cell or cell-matrix interactions, PKD2 has homology to PKD1 and the major subunit of the voltage-activated Ca2+ channels. We now describe sequence homology between PKD2 and various members of the mammalian transient receptor potential channel (TRPC) proteins, thought to be activated by G protein-coupled receptor activation and/or depletion of internal Ca2+ stores. We show that PKD2 can directly associate with TRPC1 but not TRPC3 in transfected cells and in vitro. This association is mediated by two distinct domains in PKD2. One domain involves a minimal region of 73 amino acids in the C-terminal cytoplasmic tail of PKD2 shown previously to constitute an interacting domain with PKD1. However, distinct residues within this region mediate specific interactions with TRPC1 or PKD1. The C-terminal domain is sufficient but not necessary for the PKD2-TRPC1 association. A more N-terminal domain located within transmembrane segments S2 and S5, including a putative pore helical region between S5 and S6, is also responsible for the association. Given the ability of the TRPC to form functional homo- and heteromultimeric complexes, these data provide evidence that PKD2 may be functionally related to TRPC proteins and suggest a possible role of PKD2 in modulating Ca2+ entry in response to G protein-coupled receptor activation and/or store depletion.

Indexed as

Calcium ChannelsAmino Acid SequenceBinding SitesCell LineHumansIon ChannelsKidneyMembrane ProteinsMolecular Sequence DataPolycystic Kidney, Autosomal DominantProteinsRecombinant Fusion ProteinsRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidTransfectionCalcium ChannelsIon ChannelsMembrane ProteinsProteinsRecombinant Fusion ProteinsRecombinant Proteinstransient receptor potential cation channel, subfamily C, member 1TRPC Cation ChannelsTRPP Cation Channels

Identifiers

PMID10097141
PMCPMC22398
OpenAlexW2010237592

What OpenQuestion holds

Texttitle and abstract
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.