Related Experiment Video

Updated: Feb 24, 2026

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes
08:49

Fluorescence-Based Measurements of Phosphatidylserine/Phosphatidylinositol 4-Phosphate Exchange Between Membranes

Published on: March 14, 2021

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

Noemi Carosella1, Chiara Pastorello2,3, Jehan Waeytens4

  • 1Laboratory of Bioinorganic Chemistry, Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, Bologna, Italy.

Protein Science : a Publication of the Protein Society
|February 23, 2026
PubMed

Insights

NDRG1 protein phosphorylation acts as a molecular switch, controlling its location and function. This discovery offers new therapeutic avenues for nickel and pollution-induced lung cancer.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • NDRG1 protein is crucial in cellular processes and cancer.
  • Its role in lung cancer is linked to chemotherapy resistance and nickel exposure.
  • Precise molecular mechanisms of NDRG1, especially its C-terminal region, are not fully understood.

Purpose of the Study:

  • To investigate the molecular mechanisms of NDRG1, focusing on phosphorylation, metal binding, and lipid interactions.
  • To dissect the function of the C-terminal intrinsically disordered region of NDRG1.
  • To understand how NDRG1 acts as a molecular switch.

Main Methods:

  • Circular Dichroism (CD)
  • Nuclear Magnetic Resonance (NMR)
  • Electron Paramagnetic Resonance (EPR)
  • Fourier-Transform Infrared Spectroscopy (FT-IR)
  • Isothermal Titration Calorimetry (ITC)

Main Results:

  • Phosphorylation modulates NDRG1's subcellular localization and lipid interactions.
  • NDRG1 functions as a molecular switch, toggling between membrane-bound and soluble states.
  • Metal binding influences NDRG1's signaling-competent conformations.

Conclusions:

  • Phosphorylation is a key regulator of NDRG1 function, impacting lipid trafficking and subcellular localization.
  • NDRG1's C-terminal region is critical for its role as a molecular switch.
  • These findings provide a mechanistic basis for therapeutic interventions in nickel and pollution-driven lung cancer.
Keywords:
NDRG1intrinsically disordered regionlung cancermembrane bindingnickel‐driven carcinogenesis

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