Short Bio:
Aaron J. Ciechanover (born October 1, 1947, Haifa, British Protectorate of Palestine [now Haifa, Israel]) Israeli biochemist who shared the 2004 Nobel Prize for Chemistry with Avram Hershko and Irwin Rose for their joint discovery of the mechanism by which the cells of most living organisms cull unwanted proteins.
Ciechanover received an M.D. (1974) from Hebrew University–Hadassah Medical School in Jerusalem and a D.Sc. (1981) from the Technion–Israel Institute of Technology in Haifa, where he was taught by Hershko. In 1977 Ciechanover joined the faculty at the Technion, where he held a variety of academic positions.
In the late 1970s and early ’80s, Ciechanover, Hershko, and Rose worked together at the Fox Chase Cancer Center in Philadelphia, where much of their prizewinning research was done. The process that they discovered involves a series of carefully orchestrated steps by which cells degrade, or destroy, the proteins that no longer serve any useful purpose. In the first step a molecule called ubiquitin (from the Latin ubique, meaning “everywhere,” because it occurs in so many different cells and organisms) attaches to a protein targeted for destruction and accompanies it to a proteasome—essentially a sac of powerful enzymes that break the protein into its component amino acids. The outer membrane of the proteasome admits only proteins carrying a ubiquitin molecule, which detaches before entering the proteasome and is reused.
Ciechanover, Hershko, and Rose also demonstrated that ubiquitin-mediated protein degradation helps control a number of other critical biochemical processes, including cell division, the repair of defects in DNA, and gene transcription, the process in which genes use their coded instructions to manufacture a protein. Diseases such as cystic fibrosis result when the protein-degradation system does not work normally, and researchers hoped to use the findings to develop drugs against such illnesses.
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