Delving into the Latest Updates on Fox Run Management LLC with Synapse

Overview

A review.The selection of protein substrates for ubiquitination is commonly achieved by the specific interactions of E3 protein-ubiquitin ligases with both target proteins and E2 enzymes.The protein-protein interactions that confer selectivity to the ubiquitination machinery have many features in common with the modular protein interactions characteristic of signal transduction pathways.Notably, recruitment of a target protein into an E3 protein-ubiquitin ligase complex is often dependent on its phosphorylation on either serine/threonine or tyrosine residues.The authors discuss examples of phospho-dependent protein ubiquitination in signal transduction and the cell cycle, and suggest that viral proteins, such as the Epstein-Barr virus polypeptide LMP2A, can stimulate the ubiquitination of host cell proteins by serving as a scaffold to recruit protein-ubiquitin ligases and their substrates.The authors summarize recent data suggesting that multi-site phosphorylation of the yeast CDK inhibitor Sic1 is required for its binding to an E3 complex, and.Consequent destruction.Based on exptl. observation and theor. modeling, the authors argue that this requirement for multi-site phosphorylation of Sic1 during the G1 phase of the cell cycle yields a switch-like effect which is important for regulating entry into S phase.

100 Deals associated with Fox Run Management LLC

Login to view more data

100 Translational Medicine associated with Fox Run Management LLC

Login to view more data