Article
Release of ubiquitin-charged Cdc34-S - Ub from the RING domain is essential for ubiquitination of the SCF(Cdc4)-bound substrate Sic1.
Cell - 5 Sept 2003
Deffenbaugh Andrew E, Scaglione K Matthew, Zhang Lingxiao, Moore Johnnie M, Buranda Tione, Sklar Larry A, Skowyra Dorota
Abstract excerpt
The S. cerevisiae SCF(Cdc4) is a prototype of RING-type SCF E3s, which recruit substrates for polyubiquitination by the Cdc34 ubiquitin-conjugating enzyme. Current models propose that Cdc34 ubiquitinates the substrate while remaining bound to the RING domain. In contrast, we found that the formation of a ubiquitin thiol ester regulates the Cdc34/SCF(Cdc4) binding equilibrium by increasing the dissociation rate...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.