UMass Chemist Eric Strieter and his lab group have discovered how an enzyme known as UCH37 regulates a cell’s waste management system, a result they found “incredibly surprising.”

Strieter says, “It took us eight years to figure it out, and I’m very proud of this work. We had to develop a lot of new methods and tools to understand what this enzyme is doing.”

As he explains, a very large protease called a proteasome is responsible for degrading the vast majority of proteins in a cell; it may be made up of as many as 40 proteins. It has been known for more than 20 years that UCH37 is one of the regulatory enzymes that associates with the proteasome, he adds, “but no one understood what it was doing.” It turns out that the crux of the whole process, he adds, is how complicated modifications in a small protein called ubiquitin can be.

Writing this week in Molecular Cell, he and first author and Ph.D. candidate Kirandeep Deol, who led and conducted the experiments, with co-authors Sean Crowe, Jiale Du, Heather Bisbee and Robert Guenette, discuss how they answered the question. The work was supported by the NIH’s National Institute of General Medical Sciences.

This advance could eventually lead to a new cancer treatment, Strieter says, because cancer cells need the proteasome to grow and proliferate.