Academia Sinica researchers earlier this week announced a breakthrough in understanding how the human body fights off defective proteins that cause Alzheimer’s and Parkinson’s diseases, and amyotrophic lateral sclerosis (ALS).
In 2015, researchers found that the protein CRL2 plays a “quality control” role in the body’s protein turnover regulation, as it finds and dismantles flawed proteins, said Yen Hsueh-chi (顏雪琪), an associate research fellow at Academia Sinica’s Institute of Molecular Biology.
Yen and her fellow researchers had their work published in last month’s issue of the journal Molecular Cell.
Photo: Wu Hsin-tien, Taipei Times
“Forty-five percent of the human body consists of proteins, which govern cellular structures, gene regulation, metabolic catalysis, signal transduction and immune recognition, among other biological functions,” she said.
Defective proteins, which stem from flawed production or environmental stimuli, are the cause for several neurological diseases, and various processes are developed by the body to identity and remove them, Yen said.
In 2008, a team comprised of Harvard University’s Stephen Elledge, Yen and her colleges developed a technique to profile the body’s protein stability, which led to their discovery in 2015 that CRL2 is one of the few quality-control proteins, she said.
Photo provided by Academia Sinica
Further research has shed light on the mechanism that CRL2 uses to recognize and eliminate defective genes, which they decided to name DesCEND, or destruction via C-end degrons, Yen said.
CRL2 has special receptors that enable it to recognize the characteristic C-termini of aberrant proteins, or C-end degrons, which are then marked and broken down into harmless peptides or amino acids, she said, adding that C-end degrons contain unusual peptide segments, which are comprised of six to 10 amino acids.
Variations in the amino acid sequence of the C-end degrons of defective proteins lead to different rates of protein regulation, Yen said.
Knowledge of this phenomenon could potentially improve the precision of artificially induced protein degradation when utilized in protein engineering, she said.
The researchers discovered that CRL2 also breaks down normal proteins that share the same C-end degrons as defective proteins, Yen said, adding that they have begun work to understand the biological function of this process.
Additional reporting by CNA
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