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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
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The intrinsically disordered protein NUPR1 binds to phospholipids.

Matías Estaras1, Bruno Rizzuti2,3, A Marcela Giudici4

  • 1Centre de Recherche en Cancérologie de Marseille (CRCM), INSERM U1068, CNRS UMR 7258, Aix-Marseille Université and Institut Paoli-Calmettes, Parc Scientifique et Technologique de Luminy, Equipe labélisée Ligue Nationale contre le cancer, Marseille, France.

Protein Science : a Publication of the Protein Society
|July 21, 2025
PubMed
Summary

Nuclear protein 1 (NUPR1), an intrinsically disordered protein, interacts with lipids like phosphatidylserine (PS) and phosphatidylinositol biphosphate (PIP2). This binding, confirmed in vitro and in silico, suggests roles in membrane organelle stability and cellular signaling.

Keywords:
NMRbiolayer interferometryintrinsically disordered proteinmolecular dockingprotein‐lipid interactionsproximity ligation assay

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Nuclear protein 1 (NUPR1) is an intrinsically disordered protein (IDP) known to interact with proteins and nucleic acids.
  • NUPR1 plays a role in cellular responses to stress.
  • The conformational flexibility of NUPR1 suggests potential interactions with other biomolecules, including lipids.

Purpose of the Study:

  • To investigate whether NUPR1 interacts with lipids.
  • To characterize the binding of NUPR1 to specific phospholipids.
  • To explore the potential biological implications of NUPR1-lipid interactions.

Main Methods:

  • Proximity ligation assay (PLA) in MiaPaCa-2 cells to verify in cellulo binding.
  • In vitro binding assays using nuclear magnetic resonance (NMR) and biolayer interferometry (BLI).
  • In silico modeling to analyze NUPR1-lipid interactions on membrane surfaces.

Main Results:

  • Binding of NUPR1 to phosphatidylserine (PS) and phosphatidylinositol biphosphate (PIP2) was confirmed in cellulo.
  • In vitro experiments validated NUPR1 binding to PS and a PS/phosphatidylcholine (PC) mixture.
  • In silico analysis revealed mostly non-specific membrane surface association with preferred binding sites near Ala33 and Thr68.

Conclusions:

  • NUPR1 unambiguously binds to lipids, including PS and PIP2.
  • These findings suggest NUPR1 may contribute to the stability of membrane organelles.
  • NUPR1-lipid interactions could play a role in modulating cellular signaling pathways.