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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Herrador, Antonio Haguenauer-tsapis, Rosine Léon, Sébastien Vincent, Olivier |
| Description | Author Affiliation: Herrador A ( Instituto de Investigaciones Biomédicas, Consejo Superior de Investigaciones Científicas-Universidad Autónoma de Madrid (CSIC-UAM), 28029 Madrid, Spain.) |
| Abstract | The length of the ubiquitin chain on a substrate dictates various functional outcomes, yet little is known about its regulation in vivo. The yeast arrestin-related protein Rim8/Art9 is monoubiquitinated in vivo by the Rsp5 ubiquitin ligase. This also requires Vps23, a protein that displays an ubiquitin-E2 variant (UEV) domain. Here, we report that binding of the UEV domain to Rim8 interferes with ubiquitin chain elongation and directs Rim8 monoubiquitination. We propose that Vps23 UEV competes with Rsp5 HECT N-lobe for binding to the first conjugated ubiquitin, thereby preventing polyubiquitination. These findings reveal a novel mechanism to control ubiquitin chain length on substrates in vivo. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 23 |
| Volume Number | 288 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2013-06-07 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Endosomal Sorting Complexes Required For Transport Metabolism Intracellular Signaling Peptides And Proteins Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Ubiquitin-Protein Ligase Complexes Ubiquitin Ubiquitination Physiology Genetics Protein Structure, Tertiary Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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