Evidence map›Paper›PMID 20164195›Full record

ArticleThe Journal of biological chemistry2010

The phospholipid-binding protein SESTD1 is a novel regulator of the transient receptor potential channels TRPC4 and TRPC5.

Susanne Miehe, Andrea Bieberstein, Isabelle Arnould, Orhia Ihdene, Hartmut Rütten, Carsten Strübing

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.1field-weighted citation impact, top 15% 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

32 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
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  6. Pharmacogenomics of Lithium Response in Bipolar Disorder.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  7. Article
  8. Review
  9. TRP Channels Regulation of Rho GTPases in Brain Context and Diseases.Frontiers in cell and developmental biology · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Critical roles of Gi/o proteins and phospholipase C-δ1 in the activation of receptor-operated TRPC4 channels.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Article
  18. Article
  19. Review
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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

6 authors at 2 institutions in 2 countries.

Susanne MieheTherapeutic Department of Cardiovascular Diseases, Sanofi-Aventis Deutschland GmbH, Industriepark Hoechst, Frankfurt am Main, Germany.
Andrea Bieberstein
Isabelle Arnould
Orhia Ihdene
Hartmut Rütten
Carsten Strübing
Sanofi (Germany) · DESanofi (France) · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TRPC4 and TRPC5 are two closely related members of the mammalian transient receptor potential cation channel family that have been implicated in important physiological functions, such as growth cone guidance and smooth muscle contraction. To further unravel the role of TRPC4 and TRPC5 in these processes in vivo, detailed information about the molecular composition of native channel complexes and their association with cellular signaling networks is needed. We therefore searched a human aortic cDNA library for novel TRPC4-interacting proteins using a modified yeast two-hybrid assay. This screen identified SESTD1, a previously uncharacterized protein containing a lipid-binding SEC14-like domain as well as spectrin-type cytoskeleton interaction domains. SESTD1 was found to associate with TRPC4 and TRPC5 via the channel's calmodulin- and inositol 1,4,5-trisphosphate receptor-binding domain. In functional studies, we demonstrate that SESTD1 binds several phospholipid species in vitro and is essential for efficient receptor-mediated activation of TRPC5. Notably, phospholipid binding to SESTD1 was Ca(2+)-dependent. Because TRPC4 and -5 conduct Ca(2+), SESTD1-channel signaling may be bidirectional and also couple TRPC activity to lipid signaling through SESTD1. The modulation of TRPC channel function by specific lipid-binding proteins, such as SESTD1, adds another facet to the complex regulation of these channels complementary to the previously described effects of direct channel-phospholipid interaction.

Indexed as

Amino Acid SequenceBinding SitesCalcium SignalingCarrier ProteinsGene LibraryHumansIn Vitro TechniquesMolecular Sequence DataPhospholipidsProtein Structure, TertiaryRecombinant Fusion ProteinsRNA, MessengerTRPC Cation ChannelsTwo-Hybrid System TechniquesCarrier ProteinsPhospholipidsRecombinant Fusion ProteinsRNA, MessengerSESTD1 protein, humanTRPC4 ion channelTRPC5 protein, humanTRPC Cation Channels

Identifiers

PMID20164195
PMCPMC2852980
OpenAlexW1992432457

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.