Ubiquitylation in immu

cancer: from molecular therapeutic implication iki iti 20 duction that allows a rapid and cellul et al, 2010). The addition of chemical moieties the structure, localization, activity and thereby the function of the modified protein. Once a protein is modified by a post-cular complexes in cesses of assembly central core of the signal transduction machinery driving various cellular functions. Recent studies have revealed that n the acid polypeptide of the family of ubiquitin-like (UBL) proteins, to the target proteins was linked to their degradation via the conjugated either as a monomer or as polyubiquitin chains of various kinds (Ikeda & Dikic, 2008). Similar to other PTMs such and usually inducible event. Conjugation of ubiquitin to a substrate protein leads to various consequences in the cell such the proteasome inhibitor bortezomib (PS-341) in treating Review Ubiquitylation in immunity and cancer uit most crucial post-translational modifications controlling virtually all cellular pro-cesses. What was once regarded as a mere signal for protein degradation has turned out to be a major regulator of molecular signalling networks. Deregulation of ubiquitin signalling is closely associated with various human pathologies. Here, we summarize the current knowledge of ubiquitin signalling in immune deficiencies and cancer as well as the available therapeutic strategies targeting the ubiquiti