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Related Experiment Video

Updated: Jun 4, 2025

Author Spotlight: Exploring Cellular Zinc Regulation Through ZnT1 Functionality

Author Spotlight: Exploring Cellular Zinc Regulation Through ZnT1 Functionality

Published on: June 2, 2023

The human zinc-binding cysteine proteome.

Nils Burger¹, Melanie J Mittenbühler¹, Haopeng Xiao¹

¹Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02215, USA; Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.

|January 1, 2025

Summary

This summary is machine-generated.

This study maps the human zinc-binding cysteine proteome, identifying 6,173 sites and revealing zinc

Keywords:

GSR cancer cysteine proteomics glutathione reductase zinc zinc-binding proteome

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Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Ion Mobility-Mass Spectrometry Techniques for Determining the Structure and Mechanisms of Metal Ion Recognition and Redox Activity of Metal Binding Oligopeptides

Published on: September 7, 2019

Area of Science:

Biochemistry
Proteomics
Molecular Biology

Background:

Zinc is a vital micronutrient regulating physiological processes, primarily via binding to protein cysteine residues.
The specific cysteine sites involved in zinc binding across the human proteome are largely uncharacterized.
Understanding zinc-protein interactions is crucial for modulating protein function and cellular processes.

Purpose of the Study:

To develop a comprehensive and quantitative map of the zinc-binding cysteine proteome (ZnCPT).
To identify and characterize novel zinc-binding cysteine sites within human proteins.
To explore the functional implications of zinc binding in various biological domains and disease contexts.

Main Methods:

Development of ZnCPT, a deep and quantitative proteomic mapping technique.
Systematic identification of cysteine residues involved in zinc binding across the human proteome.
Analysis of protein families and functional domains regulated by zinc binding.

Main Results:

Defined 6,173 zinc-binding cysteines, revealing widespread zinc modulation of protein function.
Identified protein families across major biological domains affected by constitutive or inducible zinc binding.
Discovered 52 cancer genetic dependencies influenced by zinc binding, including GSR-dependent lung cancers.

Conclusions:

ZnCPT provides a valuable resource for understanding zinc regulation of protein function.
Zinc binding plays a significant role in structural, enzymatic, and allosteric protein regulation.
The findings nominate malignancies sensitive to zinc-induced cytotoxicity and reveal a novel zinc-GSR interaction in lung cancer.