Current understanding of DJ-1 mutations leading to loss of function
The PARK7 gene is responsible for encoding the DJ-1 protein. DJ-1 is an oncogene, meaning it is a gene that can potentially cause cancer. That said, it is expressed in almost all cells and provides multiple intracellular functions. It can be noted that, DJ-1 protein provides extracellular protections, suggesting a role for DJ-1 as an anti-oxidative stress and molecular chaperone.
In particular, the DJ-1 protein can function as a means to protect cells from oxidative stress. Oxidative stress is the inability of a body to remove an accumulation of free radicals, where at high levels can harm cells (Ariga et al. 2013). The loss of DJ-1 protein in neuronal cells, increases the cell death through oxidative stress. In the presence of oxidative stress, the oxidized DJ-1 can disassociate from the mRNAs, allowing their translations. Whereas, DJ-1 generally binds to and restrain the mRNAs that translate factors interact with oxidative stress (Billia et al. 2012). Essentially, as DJ-1, a cytoplasmic protein, responds to growth factors by being transported from the cytoplasm into the nucleus. For it to undergo the nuclear …show more content…
On top of that, as a chaperone it may deliver specific proteins to proteasomes, where these unneeded proteins are degraded (Ariga et al. 2013). Mutated proteins tend to not properly fold due to the mismatch of specific amino acid sequences. For that reason, since a protein’s function is solely dependent on the shape of the protein, any type of mutations could alter the folding of a protein resulting in a non-functional or non-efficient protein. Knowing that, it can be said that mutated proteins, like DJ-1, are unstable and will eventually be broken down by proteasomes (Klein and Westenberger
The PARK7 gene is responsible for encoding the DJ-1 protein. DJ-1 is an oncogene, meaning it is a gene that can potentially cause cancer. That said, it is expressed in almost all cells and provides multiple intracellular functions. It can be noted that, DJ-1 protein provides extracellular protections, suggesting a role for DJ-1 as an anti-oxidative stress and molecular chaperone.
In particular, the DJ-1 protein can function as a means to protect cells from oxidative stress. Oxidative stress is the inability of a body to remove an accumulation of free radicals, where at high levels can harm cells (Ariga et al. 2013). The loss of DJ-1 protein in neuronal cells, increases the cell death through oxidative stress. In the presence of oxidative stress, the oxidized DJ-1 can disassociate from the mRNAs, allowing their translations. Whereas, DJ-1 generally binds to and restrain the mRNAs that translate factors interact with oxidative stress (Billia et al. 2012). Essentially, as DJ-1, a cytoplasmic protein, responds to growth factors by being transported from the cytoplasm into the nucleus. For it to undergo the nuclear …show more content…
On top of that, as a chaperone it may deliver specific proteins to proteasomes, where these unneeded proteins are degraded (Ariga et al. 2013). Mutated proteins tend to not properly fold due to the mismatch of specific amino acid sequences. For that reason, since a protein’s function is solely dependent on the shape of the protein, any type of mutations could alter the folding of a protein resulting in a non-functional or non-efficient protein. Knowing that, it can be said that mutated proteins, like DJ-1, are unstable and will eventually be broken down by proteasomes (Klein and Westenberger