Yuan Shi

TL;DR: The identification of a new ubiquitin receptor, Rpn13/ARM1, a known component of the proteasome, is reported, suggesting a coupling of chain recognition and disassembly at the prote asome.

TL;DR: The results indicate that proteasome subunit Rpn1 can recognize both ubiquitin and UBL domains of substrate shuttling factors that themselves bind ubiquit in and function as reversibly associated proteasomal Ubiquitin receptors.

TL;DR: The specificity of the proteasome can be regulated by rapid Ubiquitin chain removal, which resolves substrates based on a novel aspect of ubiquitin conjugate architecture.

TL;DR: Results indicate that UBE2O may function as a hybrid enzyme with both E2 and E3 (ubiquitin-ligating) activities in the reticulocyte–red blood cell transition, and that a major component of the specificity underlying differentiation-linked proteome remodeling appears to be carried by UBE1O itself.

TL;DR: It is reported that proteins with single chains of K48-linked ubiquitin are targeted for degradation almost exclusively through binding to Rpn10, and those targeted to the proteasome through a ubiquitIn-like domain are degraded most efficiently when bound by Rpn13 or Rpn1.