DJ-1

DJ-1 is a protein that in humans is encoded by the PARK7 gene. It is a multifunctional protein that plays a role in various cellular processes, including cellular response to oxidative stress, cell proliferation, and mitochondrial function. Mutations in the PARK7 gene are associated with rare forms of Parkinson's disease.

Structure

The DJ-1 protein is a small, highly conserved protein of 189 amino acids. It has a unique structure consisting of a six-stranded beta-sheet sandwiched between eight alpha-helices. The protein has a single cysteine residue at position 106, which is sensitive to oxidative stress and plays a crucial role in the protein's function.

Function

DJ-1 plays a role in various cellular processes. It acts as a redox sensor and can protect cells from oxidative stress by undergoing a self-oxidation reaction. DJ-1 also regulates cell proliferation and survival, and it has been implicated in the regulation of transcription and mitochondrial function.

In the context of Parkinson's disease, DJ-1 is thought to play a protective role. It has been shown to prevent the aggregation of alpha-synuclein, a protein that forms toxic aggregates in the brains of Parkinson's patients. DJ-1 also protects neurons from death induced by oxidative stress and mitochondrial dysfunction, two key factors in the pathogenesis of Parkinson's disease.

Clinical significance

Mutations in the PARK7 gene, which encodes DJ-1, are associated with rare forms of early-onset Parkinson's disease. These mutations often result in a loss of function of the DJ-1 protein, leading to increased susceptibility to oxidative stress and mitochondrial dysfunction.

File:DJ-1 structure.png

Structure of the DJ-1 protein. The protein is shown in ribbon representation, with the alpha-helices in red and the beta-sheets in yellow. The cysteine residue at position 106 is shown in green.

See also

• Parkinson's disease
• Oxidative stress
• Mitochondrial dysfunction

References

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