Scientists have made a potentially "life-changing" discovery that could lead to new drugs for treating Parkinson's disease.
Researchers at the Walter and Eliza Hall Institute in Australia have revealed for the first time the structure of the PINK1 protein and how it binds to mitochondria.
This breakthrough solves a decades-long mystery about how PINK1 mutations affect brain cells in Parkinson's disease.
The neurological condition affects around 153,000 Britons and is the fastest-growing neurodegenerative condition in the world.
PINK1 is particularly linked to young-onset Parkinson's Disease
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The findings, published in the journal Science, explain how PINK1 works in four distinct steps.
First, PINK1 senses mitochondrial damage. Then, it attaches to damaged mitochondria.
Once attached, it links to a protein called Parkin so that the damaged mitochondria can be recycled.
In people with Parkinson's and a PINK1 mutation, this process fails, allowing toxins to accumulate in brain cells, eventually killing them.
Brain cells need significant energy and are especially sensitive to this damage.
"This is a significant milestone for research into Parkinson's. It is incredible to finally see PINK1 and understand how it binds to mitochondria," said Professor David Komander, corresponding author on the study.
"Our structure reveals many new ways to change PINK1, essentially switching it on, which will be life-changing for people with Parkinson's," he added.
Dr Sylvie Callegari, lead author, noted this is the first time human PINK1 has been seen docked to damaged mitochondria.
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Becky Jones from Parkinson's UK called the research "encouraging" for developing treatments that could slow or stop Parkinson's progression.
PINK1 has been particularly linked to young-onset Parkinson's Disease, which affects people under the age of 50.
Until now, researchers have been unable to visualise the protein or understand how it works.
There is currently no cure for Parkinson's, although medicine, physiotherapy and surgery can help manage symptoms.
