Ubiquitylation is a dynamic regulatory signal that affects
                 the activity, localization and fate determination of proteins.
                 The characterized roles of ubiquitin include acting as a
                 sorting signal to direct protein to degradation in the
                 proteasome or in the lysosome, trafficking in the endocytic and
                 biosynthetic pathways, regulating vesicle and virus budding
                 machinery, modifying histones, regulating transcriptional
                 machinery and controlling intranuclear localization.
                 Ubiquitylated proteins are recognized by ubiquitin binding
                 domains that transmit the information conferred by the new
                 structure of the ubiquitylated protein. Our lab is taking a
                 structural and biophysical approaches to understanding the
                 molecular mechanism of ubiquitin recognition.