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Dynamic communication between atoms within folded proteins is potentially important for function, but its measurement has been a challenge. Now, a combined NMR and modelling study provides insights on the presence and strengths of such correlations.

The ESCRT-I, -II, and -III complexes act sequentially to sort monoubiquitinated transmembrane proteins into multivesicular bodies for targeted degradation in the lysosome. Two papers published in a recent issue of Cell provide insights into the structural organization and functional interactions of the ESCRT-I complex and ESCRT-II GLUE domain.

In comparison with previous studies, a new crystal structure of a HECT ubiquitin ligase catalytic domain has revealed the structural basis of the conformational flexibility of the enzyme and provides insights into the mechanism underlying the ubiquitin transfer reaction in the polyubiquitination pathway.

The first crystal structures have been obtained for a UBP domain both alone and in complex with ubiquitin aldehyde, thus providing a framework for structural conservation throughout the UBP protease family. Comparison of the structures provides substantial insight into ubiquitin-mediated activation of UBP protease activity, a process that potentially regulates substrate-dependent ubiquitin deconjugation.