Reuven Wiener Lab

To date, besides ubiquitin (UB) that can modify a target protein with mono or poly-ubiquitin chains with varying linkages and length, more than dozen different UBLs are found to be encoded in human genome, thereby significantly increase the repertoire of protein modifications. Not surprisingly, improper regulation of these modifications has been observed in many human diseases including cancer, Alzheimer's disease, Parkinson's disease and viral infections. My lab is interested in the molecular mechanisms governing Ub and UBL conjugation to cellular proteins. More than 900 enzymes are involved in deposition or removal of Ub/UBL from target proteins, and only little is known about their specificity, activity and interaction network. Besides Ub, UBLs can also covalently modify target proteins. To date, less is known about UBLs and even less is known about the UBL called ubiquitin-fold modifier 1 (UFM1). Currently, our understanding of protein modification by UFM1 (UFMylation) is like a jigsaw puzzle with many missing pieces, and in some cases it is not even clear whether these pieces of data are in the right place.
We use X-ray crystallography, enzymology, cell biology, biochemistry and a variety of biophysical methods in order to provide structural and functional data required for understanding the molecular mechanisms underlying the function of these enzymes.