The role of cysteine oxidation in DJ-1 function and dysfunction

Research output: Contribution to journalArticle

172 Citations (Scopus)

Abstract

DJ-1 is a member of the large and functionally diverse DJ-1/PfpI superfamily and has homologs in nearly all organisms. Because of its connection to parkinsonism and cancer, human DJ-1 has been intensely studied for over a decade. The current view is that DJ-1 is a multifunctional oxidative stress response protein that defends cells against reactive oxygen species and mitochondrial damage, although the details of its biochemical function remain unclear. A conserved cysteine residue in DJ-1 (Cys106) is both functionally essential and subject to oxidation to the cysteine-sulfinate and cysteine-sulfonate. Consequently, the oxidative modification of Cys106 has been proposed to allow DJ-1 to act as a sensor of cellular redox homeostasis and to participate in cytoprotective signaling pathways in the cell. This review explores the current evidence for the role of cysteine oxidation in DJ-1 function, with emphasis on emerging models for how oxidative modification may regulate DJ-1's protective function and also contribute to dysfunction and disease.

Original languageEnglish (US)
Pages (from-to)111-122
Number of pages12
JournalAntioxidants and Redox Signaling
Volume15
Issue number1
DOIs
StatePublished - Jul 1 2011

Fingerprint

Cysteine
Oxidation
Parkinsonian Disorders
Heat-Shock Proteins
Oxidation-Reduction
Reactive Oxygen Species
Oxidative Stress
Homeostasis
Oxidative stress
Neoplasms
Sensors
Proteins
cysteine sulfonate
cysteine sulfinic acid

ASJC Scopus subject areas

  • Physiology
  • Biochemistry
  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology

Cite this

The role of cysteine oxidation in DJ-1 function and dysfunction. / Wilson, Mark A.

In: Antioxidants and Redox Signaling, Vol. 15, No. 1, 01.07.2011, p. 111-122.

Research output: Contribution to journalArticle

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