Evidence map›Paper›PMID 41507312›Full record

ArticleCommunications biology2026

Scube2 primes Dispatched and ADAM10-mediated Shh release by recruiting HDL acceptors to the plasma membrane.

J Puschmann, G Steffes, J Froese, D Manikowski, K Ehring, J Wittke, C Garbers, S V Wegner, K Grobe

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Emerging evidence for a cooperative pathway of Hedgehog release.Nature reviews. Molecular cell biology · 2026
    Article
  2. Review
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.

J PuschmannInstitute of Physiological Chemistry and Pathobiochemistry, University of Münster, Münster, Germany.
G SteffesInstitute of Neuro- and Behavioral Biology, University of Münster, Münster, Germany.
J FroeseInstitute of Physiological Chemistry and Pathobiochemistry, University of Münster, Münster, Germany.
D ManikowskiInstitute of Physiological Chemistry and Pathobiochemistry, University of Münster, Münster, Germany.
K EhringInstitute of Physiological Chemistry and Pathobiochemistry, University of Münster, Münster, Germany.
J WittkeInstitute of Physiological Chemistry and Pathobiochemistry, University of Münster, Münster, Germany.
C GarbersInstitute of Clinical Biochemistry, Hannover Medical School, Hannover, Germany.ORCID http://orcid.org/0000-0003-4939-6950
S V WegnerInstitute of Physiological Chemistry and Pathobiochemistry, University of Münster, Münster, Germany.ORCID http://orcid.org/0000-0002-9072-0858
K GrobeInstitute of Physiological Chemistry and Pathobiochemistry, University of Münster, Münster, Germany. kgrobe@uni-muenster.de.ORCID http://orcid.org/0000-0002-8385-5877

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) 386797833Deutsche Forschungsgemeinschaft (German Research Foundation) GR1748/9-1Deutsche Forschungsgemeinschaft (German Research Foundation) INST 216/1163-1 FUGGDeutsche Forschungsgemeinschaft (German Research Foundation) SFB1348
6 · The paper itself

Abstract

Sonic hedgehog (Shh) morphogens are lipidated proteins that firmly attach to the outer plasma membrane (PM) of the cells that produce them. The process by which Shh is solubilized requires the transmembrane protein Dispatched1 (Disp), the soluble glycoprotein Scube2, the proteolytic removal of lipidated peptide termini, and the use of soluble lipoproteins (LPPs) as Shh transporters. However, their molecular interplay remains controversial. Here, we demonstrate that A Disintegrin and Metalloproteinase 10, Scube2, and Disp act synergistically to remove Shh from the PM and transfer it to LPP acceptors. We also demonstrate physical Scube2 interactions with LPPs and that these interactions increase Shh release. Finally, we demonstrate that Scube2 strongly binds to heparan sulfate (HS) on cell surfaces. These findings reveal Scube2's previously unknown role in binding low-abundance, soluble LPP carriers for Shh and recruiting these carriers to HS-rich Shh release sites at the PM to enhance morphogen release.

Indexed as

Amyloid Precursor Protein SecretasesCalcium-Binding ProteinsCell MembraneHedgehog ProteinsMembrane ProteinsAdaptor Proteins, Signal TransducingAnimalsHeparan SulfateHumansMiceAdaptor Proteins, Signal TransducingAmyloid Precursor Protein SecretasesCalcium-Binding ProteinsHedgehog ProteinsHeparan SulfateMembrane ProteinsSCUBE2 protein, humanSHH protein, human

Identifiers

PMID41507312
PMCPMC12881369

What Socratic holds

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LicenceCC BY
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 Socratic graph.