When targeting problem proteins involved in causing or spreading disease, a drug will often clog up a protein's active site so it can't function and wreak havoc.
Reviewed by Lily Ramsey, LLMOct 25 2023 New strategies for dealing with these proteins can send these proteins to different types of cellular protein degradation machinery such as a cell's lysosomes, which act like a protein wood chipper.
The ability to understand the biology of this process means we can use inherent biology that already exists, and harness it to treat disease. These insights offer a unique window into a new type of biology that we haven't really understood before." Stopping proteins from going rogue While proteins often do a body good, like help us digest our food or repair torn muscles, they can also be destructive.
These findings kicked off a new class of research and therapeutics, but exactly how the process worked wasn't clear. Researchers also noticed that it was difficult to predict when LYTACs would be highly successful or fail to perform as anticipated. They also identified proteins that block LYTACs from doing their job. LYTACs work by binding to certain receptors on the outside of the cell, which they use to shuttle bad proteins into lysosomes for degradation. However, the researchers saw that proteins bearing mannose 6-phosphates , sugars that decorate proteins destined for lysosomes, will take a seat on those receptors, meaning LYTACs have nowhere to bind.
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