Evidence map›Paper›PMID 42378087›Full record

ArticleCell reports2026

TUSC3 serves as a rate-limiting gatekeeper of a glycan-mediated ER triage checkpoint for BMP4/Dpp.

Antonio Galeone, Emilio Solazzo, Francesco Lavezzari, Seung Yeop Han, Gaia Consonni, Bruna My, Riccardo Rizzo, Giuseppe Gigli, Hamed Jafar-Nejad, Thomas Vaccari

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Antonio GaleoneInstitute of Nanotechnology, National Research Council (CNR-NANOTEC), Lecce, 73100, Italy, Tecnomed Puglia - Tecnopolo per la medicina di precisione (Biotech Lecce Hub), 73100 Lecce, Italy. Electronic address: antonio.galeone@cnr.it.
Emilio SolazzoInstitute of Nanotechnology, National Research Council (CNR-NANOTEC), Lecce, 73100, Italy, Tecnomed Puglia - Tecnopolo per la medicina di precisione (Biotech Lecce Hub), 73100 Lecce, Italy; Department of Mathematics and Physics, University of Salento, 73100 Lecce, Italy.
Francesco LavezzariDepartment of Biosciences, University of Milan, 20133 Milan, Italy.
Seung Yeop HanDepartment of Molecular & Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA.
Gaia ConsonniDepartment of Biosciences, University of Milan, 20133 Milan, Italy.
Bruna MyDepartment of Mathematics and Physics, University of Salento, 73100 Lecce, Italy.
Riccardo RizzoInstitute of Nanotechnology, National Research Council (CNR-NANOTEC), Lecce, 73100, Italy, Tecnomed Puglia - Tecnopolo per la medicina di precisione (Biotech Lecce Hub), 73100 Lecce, Italy.
Giuseppe GigliInstitute of Nanotechnology, National Research Council (CNR-NANOTEC), Lecce, 73100, Italy, Tecnomed Puglia - Tecnopolo per la medicina di precisione (Biotech Lecce Hub), 73100 Lecce, Italy; Experimental Medicine Department, University of Salento, 73100 Lecce, Italy.
Hamed Jafar-NejadDepartment of Molecular & Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA; Genetics & Genomic Graduate Program, Baylor College of Medicine, Houston, TX 77030, USA; Development, Disease Models & Therapeutics Graduate Program, Baylor College of Medicine, Houston, TX 77030, USA. Electronic address: hamedj@bcm.edu.
Thomas VaccariDepartment of Biosciences, University of Milan, 20133 Milan, Italy. Electronic address: thomas.vaccari@unimi.it.

Funding

Roles of Glycosylation and Deglycosylation During Animal DevelopmentR35GM130317 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI Hamed Jafar-Nejad · 2019 to 2026
$3.7M
NIGMS NIH HHS R35 GM130317
6 · The paper itself

Abstract

Trimming of the three glucose residues decorating nascent N-glycoproteins is a critical step for their entry into the endoplasmic reticulum quality control (ERQC) and recognition by ER chaperones. However, the functional relevance of the second glucose (G2) and the regulatory step upstream of its removal by glucosidase II (GCS2) remain poorly understood. Here, we report that TUSC3, a component of the oligosaccharyltransferase (OST) complex, regulates G2 to G1 trimming on N-glycosylated bone morphogenetic protein 4 (BMP4) and its Drosophila homolog Dpp to promote their ERQC entry. Loss- and gain-of-function genetic experiments and biochemical assays in mammalian cells and flies indicate that TUSC3 serves as a dosage-sensitive gatekeeper that influences the decision between proper folding and secretion versus elimination by ER-associated degradation for the BMP4 molecules, thereby tuning BMP signaling. Together, these data reveal an unrecognized role for an OST component in early glycoprotein maturation, relevant to a major developmental signaling pathway.

Indexed as

Bone Morphogenetic Protein 4Drosophila ProteinsEndoplasmic ReticulumMembrane ProteinsPolysaccharidesAnimalsDrosophila melanogasterGlycosylationHexosyltransferasesHumansSignal TransductionBone Morphogenetic Protein 4dolichyl-diphosphooligosaccharide - protein glycotransferasedpp protein, DrosophilaDrosophila ProteinsHexosyltransferasesMembrane ProteinsPolysaccharidesBMP signalingCP: cell biologydeglycosylationDrosophilaendoplasmic reticulumER-associated degradationglucosidase IIglycosylationoligosaccharyltransferase complexOST complexquality controlTUSC3

Identifiers

PMID42378087
PMCPMC13528205

What OpenQuestion holds

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Registered trials

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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.