Evidence map›Paper›PMID 24292069›Full record

ArticleNature chemical biology2014

Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine.

Xinxin Gao, Rami N Hannoush

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

94 citing papers in PubMed, 162 citations in OpenAlex.

  1. Review
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  7. Structural basis for Porcupine inhibition.Communications chemistry · 2025
    Article
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  9. Article
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  13. Post-translational modifications in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2024
    Review
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  15. Article
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34 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Xinxin GaoDepartment of Early Discovery Biochemistry, Genentech, Inc., San Francisco, California, USA.
Rami N HannoushDepartment of Early Discovery Biochemistry, Genentech, Inc., San Francisco, California, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Wnts are secreted palmitoylated glycoproteins that are important in embryonic development and human cancers. Here we report a method for imaging the palmitoylated form of Wnt proteins with subcellular resolution using clickable bioorthogonal fatty acids and in situ proximity ligation. Palmitoylated Wnt3a is visualized throughout the secretory pathway and trafficks to multivesicular bodies that act as export sites in secretory cells. We establish that glycosylation is not required for Wnt3a palmitoylation, which is necessary but not sufficient for Wnt3a secretion. Wnt3a is palmitoylated by fatty acids 13-16 carbons in length at Ser209 but not at Cys77, consistent with a slow turnover rate. We find that porcupine (PORCN) itself is palmitoylated, demonstrating what is to our knowledge the first example of palmitoylation of an MBOAT protein, and this modification partially regulates Wnt palmitoylation and signaling. Our data reveal the role of O-palmitoylation in Wnt signaling and suggest another layer of cellular control over PORCN function and Wnt secretion.

Indexed as

AcyltransferasesExosomesGlycosylationHumansMembrane ProteinsPalmitic AcidsWnt ProteinsAcyltransferasesMembrane ProteinsPalmitic AcidsPORCN protein, humanWnt Proteins

Identifiers

PMID24292069
OpenAlexW2064990000

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.