The histone chaperone FACT and the deubiquitinating enzyme Ubp10 act in concert to remove ubiquitin from histone H2B in nucleosomes, and likely coordinate nucleosome assembly during DNA replication and transcription.
The IGF2 mRNA binding protein-2/IMP2, overexpressed in many common cancers, drives cancer cell proliferation by increasing the abundance of IGF2 and the oncogene HMGA1, which controls a network of effectors that enhance IGF2 action.
Building on previous work (Tang et al., 2015), novel ESCRT-III subunit Snf7 auto-activation mutants are used to reveal two parallel ubiquitin-dependent pathways during multivesicular endosome biogenesis.
Akt can regulate the ubiquitin-proteasome system by mediating phosphorylation and activation of USP14, which may have implications in the control of global proteostasis by growth factors and in tumorigenesis.
Proteasomes are protected from autophagic elimination upon carbon starvation by sequestration into cytoplasmic storage granules, which aid cell fitness by providing a cache of proteasomes that can be rapidly remobilized when carbon availability improves.