Evidence map›Paper›PMID 20538909›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2010

Interaction between PKD1L3 and PKD2L1 through their transmembrane domains is required for localization of PKD2L1 at taste pores in taste cells of circumvallate and foliate papillae.

Yoshiro Ishimaru, Yuka Katano, Kurumi Yamamoto, Masato Akiba, Takumi Misaka, Richard W Roberts, Tomiko Asakura, Hiroaki Matsunami, Keiko Abe

Open access · greenAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.3field-weighted citation impact, top 9% 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

25 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
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  12. Chemosensory receptor specificity and regulation.Annual review of neuroscience · 2015
    Review
  13. Article
  14. Structural biology of TRP channels.Handbook of experimental pharmacology · 2014
    Review
  15. Article
  16. Article
  17. Article
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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

9 authors at 3 institutions in 2 countries.

Yoshiro IshimaruDepartment of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan. ayishi@mail.ecc.u-tokyo.ac.jp
Yuka Katano
Kurumi Yamamoto
Masato Akiba
Takumi Misaka
Richard W Roberts
Tomiko Asakura
Hiroaki Matsunami
Keiko Abe
The University of Tokyo · JPDuke Medical Center · USDuke University Hospital · US

Funding

Molecular Mechanisms Underlying Odorant RecognitionR01DC005782 · NIDCD · DUKE UNIVERSITY · PI MATSUNAMI, HIROAKI · 2002 to 2012
$3.5M
The in vivo roles of PKD1L3 and PKD2L1 in sour taste detectionR21DC008967 · NIDCD · DUKE UNIVERSITY · PI MATSUNAMI, HIROAKI · 2007 to 2008
$426k
NIDCD NIH HHS R01 DC005782NIDCD NIH HHS R21 DC008967
6 · The paper itself

Abstract

The polycystic kidney disease 1-like 3 (PKD1L3) and polycystic kidney disease 2-like 1 (PKD2L1) proteins have been proposed to form heteromers that function as sour taste receptors in mammals. Here, we show that PKD1L3 and PKD2L1 interact through their transmembrane domains, and not through the coiled-coil domain, by coimmunoprecipitation experiments using a series of deletion mutants. Deletion mutants lacking the critical interaction region were not transported to the cell surface and remained in the cytoplasm, whereas PKD1L3 and PKD2L1 proteins were expressed at the cell surface when both are transfected. Calcium imaging analysis revealed that neither the coiled-coil domain nor the EF-hand domain located in the C-terminal cytoplasmic tail of PKD2L1 was required for response on stimulation with an acidic solution. Finally, PKD2L1 did not localize to the taste pore but was distributed throughout the cytoplasm in taste cells of circumvallate and foliate papillae in PKD1L3(-/-) mice, whereas it localized to the taste pore in wild-type mice. Collectively, these results suggest that the interaction between PKD1L3 and PKD2L1 through their transmembrane domains is essential for proper trafficking of the channels to the cell surface in taste cells of circumvallate and foliate papillae and in cultured cells.

Indexed as

Calcium ChannelsCell LineHumansImmunoprecipitationIn Situ HybridizationIon ChannelsMembrane ProteinsProtein BindingReceptors, Cell SurfaceTaste BudsCalcium ChannelsIon ChannelsMembrane ProteinsPKD1L3 protein, humanPKD2L1 protein, humanReceptors, Cell Surface

Identifiers

PMID20538909
PMCPMC2996907
OpenAlexW2001171232

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.