Evidence map›Paper›PMID 41725076›Full record

ArticleProtein science : a publication of the Protein Society2026

Phosphorylation disrupts the interaction between the intrinsically disordered region of the oncogenic NDRG1 and lipid vesicles.

Noemi Carosella, Chiara Pastorello, Jehan Waeytens, Ylenia Beniamino, Valentina Roncassaglia, Lucrezia Serra, Vincent Raussens, Elisabetta Mileo, Stefano Ciurli, Barbara Zambelli

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 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

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

10 authors.

Noemi CarosellaLaboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, Bologna, Italy.
Chiara PastorelloAix-Marseille Univ, CNRS, BIP, Bioénergétique et Ingénierie des Protéines, Marseille, France.
Jehan WaeytensRD3-Pharmacognosy, Bioanalysis and Drug Discovery Unit, Faculty of Pharmacy, Université Libre de Bruxelles, Bruxelles, Belgium.
Ylenia BeniaminoLaboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, Bologna, Italy.
Valentina RoncassagliaLaboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, Bologna, Italy.
Lucrezia SerraLaboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, Bologna, Italy.
Vincent RaussensStructure et Fonction des Membranes Biologiques, Université libre de Bruxelles, Bruxelles, Belgium.
Elisabetta MileoAix-Marseille Univ, CNRS, BIP, Bioénergétique et Ingénierie des Protéines, Marseille, France.
Stefano CiurliLaboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, Bologna, Italy.
Barbara ZambelliLaboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, Bologna, Italy.ORCID https://orcid.org/0000-0002-3876-0051

Funding

Fondazione Cassa di Risparmio in Bologna 2022.0053Fondazione del Monte di Bologna e Ravenna 2021.0520
6 · The paper itself

Abstract

NDRG1 is a multifunctional regulatory human protein implicated in crucial cellular processes and acting as a central hub of a cancer-related interactome. In lung cancer, increased NDRG1 expression is associated with resistance to chemotherapy and is linked to the cellular response to nickel, a known tumor driver in air pollution. Although NDRG1 has been extensively studied in relation to cancer and lipid vesicle recycling, its precise molecular mechanisms remain poorly defined. To address this gap, the present work shifts the focus from previous cellular-level investigations into a molecular-level study of NDRG1, dissecting the effects of phosphorylation, metal binding, and lipid interactions. Specifically, we investigated the C-terminal intrinsically disordered region of the protein that is a key regulatory hub and an attractive target for drug development. Employing a multimodal approach, which combines circular dichroism (CD), nuclear magnetic resonance (NMR), electron paramagnetic resonance (EPR), Fourier-transform infrared spectroscopy (FT-IR), and isothermal titration calorimetry (ITC), we developed a mechanistic rationale for how phosphorylation modulates protein subcellular localization, lipid trafficking and storage, acting as a molecular switch that toggles NDRG1 between membrane-bound, adhesion-supporting states and soluble, signaling-competent conformations with metal-binding activity. These insights open potential opportunities for therapeutic intervention in nickel and pollution-driven lung cancer.

Indexed as

Cell Cycle ProteinsIntracellular Signaling Peptides and ProteinsIntrinsically Disordered ProteinsHumansNickelN-myc Downstream-Regulated Gene 1 ProteinPhosphorylationProtein BindingCell Cycle ProteinsIntracellular Signaling Peptides and ProteinsIntrinsically Disordered ProteinsNickelN-myc Downstream-Regulated Gene 1 Proteinintrinsically disordered regionlung cancermembrane bindingNDRG1nickel‐driven carcinogenesis

Identifiers

PMID41725076
PMCPMC12928042

What OpenQuestion holds

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LicenceCC BY
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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.