4.7 Review

Defining the S-Glutathionylation Proteome by Biochemical and Mass Spectrometric Approaches

Journal

ANTIOXIDANTS
Volume 11, Issue 11, Pages -

Publisher

MDPI
DOI: 10.3390/antiox11112272

Keywords

redox; redox proteomics; post-translational modification; S-glutathionylation; mass spectrometry

Funding

  1. NIH
  2. [R01 DK122160]
  3. [R01 HL139335]
  4. [U01 CA227544]

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Protein S-glutathionylation (SSG) is a reversible post-translational modification that plays a critical role in redox signaling and regulation. This review summarizes current biochemical and analytical approaches for characterizing SSG and highlights recent examples of the functional and structural consequences of SSG modifications. The article also discusses future directions for research and the potential of computational methods in accelerating functional discovery.
Protein S-glutathionylation (SSG) is a reversible post-translational modification (PTM) featuring the conjugation of glutathione to a protein cysteine thiol. SSG can alter protein structure, activity, subcellular localization, and interaction with small molecules and other proteins. Thus, it plays a critical role in redox signaling and regulation in various physiological activities and pathological events. In this review, we summarize current biochemical and analytical approaches for characterizing SSG at both the proteome level and at individual protein levels. To illustrate the mechanism underlying SSG-mediated redox regulation, we highlight recent examples of functional and structural consequences of SSG modifications. Finally, we discuss the analytical challenges in characterizing SSG and the thiol PTM landscape, future directions for understanding of the role of SSG in redox signaling and regulation and its interplay with other PTMs, and the potential role of computational approaches to accelerate functional discovery.

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