A Breakthrough in Protein Degradation Research

Protein degradation is an essential process by which cells dispose of unwanted proteins, such as proteins that are no longer needed, or damaged proteins. The major route by which the cell degrades unwanted proteins is the Ubiquitin-Proteasome system (UPS) in which proteins are targeted for proteasomal degradation by ubiquitin. In vitro experiments demonstrated that a small number of proteins can undergo ubiquitin-independent proteasomal degradation (UbInPD), but little is known about the molecular mechanisms driving degradation in this pathway. In a groundbreaking work, published in the prestigious "Molecular Cell" journal, an international team of researchers led by Dr. Itay Koren from the Mina and Everard Goodman Faculty of Life Sciences at Bar-Ilan University showed that an UbInPD is more prevalent than currently appreciated. The researchers identified thousands of specific sequences that target promote UbInPD, and proteins that promote this pathway. In addition, researchers identified 69 proteins that are subject to UbInPD, among them proteins that control key processes in cells. Dr. Koren's work shows that the ubiquitin-independent proteasomal degradation pathway performs both regulatory and protein quality control functions and is a significant milestone in understanding the processes that control protein degradation in the cell.

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