Daniel J. Finley, PhD

Dr. Finley’s thesis showed that the ubiquitin pathway, which was scarcely known at the time, was the major mediator of selective protein degradation. These papers were recognized by Cell Press as among the 30 most influential ever published in that journal. He pioneered the study of ubiquitination in yeast, which further revolutionized the field. With Andreas Bachmair, he identified the first signal for ubiquitination. His lab discovered variant multiubiquitin chains, now a major area in the ubiquitin field, pioneered yeast proteasomes, and elucidated many aspects of this important complex. He discovered a set of proteasome-associated ubiquitin-chain-editing factors, a completely unexpected observation. He and his colleagues developed a chemical inhibitor of the proteasomal deubiquitinating enzyme USP14, the first specific inhibitor of a deubiquitinating enzyme and the first compound to enhance proteasome activity. He recently described global remodeling of the proteome in terminal differentiation, a novel, fundamental function of ubiquitination.