Olivier Coux

TL;DR: Major advances have been achieved recently in knowledge about the molecular organization of the 20S and 19S particles, their subunits, the proteasome's role in MHC-class 1 antigen presentation, and regulators of its activities.

TL;DR: The lid subunits share sequence motifs with components of the COP9/signalosome complex and eIF3, suggesting that these functionally diverse particles have a common evolutionary ancestry.

TL;DR: Recombinant Mcb1 protein bound multiubiquitin chains in vitro and, like its plant and animal counterparts, exhibited a binding preference for longer chains, suggesting that Mcb 1 is not the sole factor involved in ubiquitin recognition by the 26S proteasome and thatMcb1 may interact with only a subset of ubiquitinated substrates.

TL;DR: A new type of ATP-dependent protease is isolated from Escherichia coli that encodes two proteins: HslV, a 19-kDa protein similar to proteasome beta subunits, and HslU, a 50- kDa protein related to the ATPase ClpX, which appears to form a complex in which ATP hydrolysis by HSlU is essential for peptide hydrolyisation by the proteasomesome-like component HSlV.

TL;DR: The p53-associated factor E4F1 is identified, a ubiquitously expressed zinc-finger protein first identified as a cellular target of the viral oncoprotein E1A, as an atypical ubiquitin E3 ligase for p53 that modulates its effector functions without promoting proteolysis.