Mol Cell: Reveals the molecular mechanisms by which cells collect and discard damaged proteins

16, 2020 // -- In a recent study published in the international journal Molecular Cell, scientists from the University of Massachusetts, Amster, and others revealed the molecular mechanisms of UCH37 enzyme-regulating cell waste treatment systems;
researchers say a large protease called proteases is primarily responsible for degrading the vast majority of proteins in cells, possibly consisting of up to 40 proteins, and researchers knew more than 20 years ago that enzyme UCH37 is a regulatory enzyme associated with proteases, but no one knows exactly how it works. Photo Source: CC0 Public Domain proves that the key to the whole process is a complex modification process for a small protein called ubibin, which, in addition to being able to modify other proteins, can self-modify to form a wider chain, some of which have broader branches, and the researchers found that enzyme UCH37 removes branch points from the chain and allows the degradation process to continue; Researcher Eric Strieter said the findings could help develop new cancer therapies because cancer cells need proteases to grow and multiply, and in essence, many cancer cells are addicted to protease function, and cells produce proteins at such a rate that they make mistakes that if they are not cleared in time, the cells will not function properly because UCH37 can help remove proteins. It may therefore be added as a useful therapeutic target to protease inhibitors that have been successfully used in clinical practice.
researchers say they must come up with a way to produce multiple ubigan chains to represent potential diversity in cells, and that using this new Ubigan chain library could help researchers query the activity of UCH37 in a controlled environment, and that the series of experiments provides the first clue that the enzyme may be doing something very unique. Another new method developed by
researchers could use mass spectrometry to describe the structural properties of ubiquitin chains in complex mixtures, perhaps to show that the activity they found using the substation library may also exist in more uneven mixtures; The
researchers say the UCH37 may not have functioned as expected, nor prevented the degradation process, but rather removed fulc points from the ubigan chain to help degrade proteins, and we may think that by removing the degradation signal, the degradation process may not be the case;
() Original source: Kirandeep K.Deol, Sean O. Crowe, Jiale Du, et al, Proteasome-Bound UCH37/UCHL5 Debranches Ubiquitin Chains to Promoter Angel Cell (2020). DOI: 10.1016/j.molcel.2020.10.017