In vivo inhibition of SUMO activating E1-enzymes by pyrophosphate reveals a mode of integrating metabolism and stress tolerance that is conserved across kingdoms.
Co-evolving residue pairs in the different components of a protein complex almost always make contact across the protein–protein interface, thus providing powerful restraints for the modeling of protein complexes.
β-arrestins recruit Nedd4 ubiquitin E3 ligase to mGlu7 receptor and facilitate ubiquitination, endocytosis, ERK signaling, and stability of mGlu7 at presynaptic terminals.
The cancer-associated human ubiquitin ligase HUWE1 can adopt an auto-inhibited dimeric state, whose occupancy is regulated by competing intra- and intermolecular interactions of the dimerization region and by the tumor suppressor p14ARF.
In vertebrates, large regulatory landscapes sometimes behave as coherent regulatory units, which may explain the lack of effect sometimes observed when single enhancer sequences are deleted in isolation.
The presynaptic scaffolding protein Bassoon is involved in regulating neurotransmitter release by controlling synaptic vesicle pool size and vesicular protein turnover through increased ubiquitination and Parkin-dependent autophagy.