Arrestin-related trafficking adaptors (ARTs) undergo a K63 linked di-ubiquitin modification to promote Rsp5 E3 ligase recruitment and enhance cargo protein ubiquitination.

A structural element of mRNA exit channel protein Rps5 performs a critical role in start codon recognition during translation initiation by stabilizing initiator tRNA binding to the pre-initiation complex.

The small subunit ribosomal protein uS7/Rps5 interacts with translation initiation factor eIF2α to stabilize first the open, and then the closed conformation of the pre-initiation complex to promote accurate start codon selection in vivo.

Ubiquitin ligase adaptors target the selective clearance of misfolded plasma membrane proteins.

Ubp15 regulates the ubiquitylation of the export adaptor Mex67.

A novel regulatory step in the endocytic pathway, which occurs post-internalization, takes place at the trans-Golgi network and involves the arrestin-related protein Rod1 and the ubiquitin ligase Rsp5.

Structural studies reveal the mechanism by which a HECT E3 ubiquitin ligase carries out E2-to-E3-to-substrate ubiquitin transfer and prioritizes target lysines for ubiquitination.

Maintenance of ubiquitin homeostasis is essential for proper control of the size of postsynaptic density and the growth of specialized membrane structure.

The Toxoplasma parasite requires an enzyme called ASP5 to cleave proteins for export into host cells.