Evidence map›Paper›PMID 26054340›Full record

ArticleCell communication and signaling : CCS2015

The importance of claudin-7 palmitoylation on membrane subdomain localization and metastasis-promoting activities.

Sarah Heiler, Wei Mu, Margot Zöller, Florian Thuma

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Cell communication and signaling : CCS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.2field-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

39 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
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  6. Review
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  9. Article
  10. Review
  11. The role of claudins in homeostasis.Nature reviews. Nephrology · 2023
    Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Claudins as biomarkers of differential diagnosis and prognosis of tumors.Journal of cancer research and clinical oncology · 2021
    Review
  18. Review
  19. The desmosome as a model for lipid raft driven membrane domain organization.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Sarah HeilerDepartment of Tumor Cell Biology, University Hospital of Surgery, Im Neuenheimer Feld 365, 69120, Heidelberg, Germany. Sarah.Heiler@uni-heidelberg.de.
Wei MuDepartment of Tumor Cell Biology, University Hospital of Surgery, Im Neuenheimer Feld 365, 69120, Heidelberg, Germany. Wei.Mu@uni-heidelberg.de.
Margot ZöllerDepartment of Tumor Cell Biology, University Hospital of Surgery, Im Neuenheimer Feld 365, 69120, Heidelberg, Germany. m.zoeller@uni-hd.de.
Florian ThumaDepartment of Tumor Cell Biology, University Hospital of Surgery, Im Neuenheimer Feld 365, 69120, Heidelberg, Germany. Florian.Thuma@uni-heidelberg.de.
Heidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundClaudin-7 (cld7), a tight junction (TJ) component, is also found basolaterally and in the cytoplasm. Basolaterally located cld7 is enriched in glycolipid-enriched membrane domains (GEM), where it associates with EpCAM (EpC). The conditions driving cld7 out of TJ into GEM, which is associated with a striking change in function, were not defined. Thus, we asked whether cld7 serines or palmitoylation affect cld7 location and protein, particularly EpCAM, associations.

resultsHEK cells were transfected with EpCAM and wild type cld7 or cld7, where serine phopsphorylation or the palmitoylation sites (AA184, AA186) (cld7(mPalm)) were mutated. Exchange of individual serine phosphorylation sites did not significantly affect the GEM localization and the EpCAM association. Instead, cld7(mPalm) was poorly recruited into GEM. This has consequences on migration and invasiveness as palmitoylated cld7 facilitates integrin and EpCAM recruitment, associates with cytoskeletal linker proteins and cooperates with MMP14, CD147 and TACE, which support motility, matrix degradation and EpCAM cleavage. On the other hand, only cld7(mPalm) associates with TJ proteins.

conclusionCld7 palmitoylation prohibits TJ integration and fosters GEM recruitment. Via associated molecules, palmitoylated cld7 supports motility and invasion.

Indexed as

Cell MovementLipoylationAntigens, NeoplasmCell AdhesionCell Adhesion MoleculesCell LineClaudinsEpithelial Cell Adhesion MoleculeHumansMembrane MicrodomainsMutationNeoplasm MetastasisTight JunctionsTransfectionAntigens, NeoplasmCell Adhesion MoleculesClaudinsCLDN7 protein, humanEPCAM protein, humanEpithelial Cell Adhesion Molecule

Identifiers

PMID26054340
PMCPMC4459675
OpenAlexW1530044518

What OpenQuestion holds

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LicenceCC BY
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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.