Main description:

Protein posttranslational modification with peptide tags ubiquitin or small ubiquitin-like modifier (SUMO) orchestrate multiple cellular events to ensure normal physiology. These simple enzymatic activities maintain homeostasis of protein modification and normal cell function. This book addresses major proteases - ubiquitin and/or SUMO proteases - involved in posttranslational modification of proteins. Themes reviewed include the difficulty of assigning substrate specificity to the individual de-ubiquitylases (DUBs), selectivity for processing ubiquitin poly-chains, and defining substrate profiles for the different SUMO proteases.

Contents:

Methods for Ubiquitin Proteases. Evaluating the Substrate Specificity of DUBs. Processing of Poly-Ubiquitin Chains and Impact on Cell Signaling. Studies on Posttranslational Modification of DUBs and Enzymatic activity. Allosteric Regulation of DUB Activity. Orchestrated Recruitment of Multiple DUBs for S-phase Progression. Natural Compounds for Inhibition of DUB Activity in Cancer Cells. Methods for SUMO Proteases. Strategies for Evaluating the Substrate Specificity of SENPs. A Study on Enzyme Kinetics of SENP. Defining the Function of DeSI Family Members. Evaluating SUMO Protease Activity at Adheren Junctions in C. elegans. SENP1-regulated NF kappa B Signal in Type-1 Diabetes Progression. Identifying Small Molecule Inhibitors for SENPs.