scholarly journals Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

EMBO Reports ◽  
2011 ◽  
Vol 12 (4) ◽  
pp. 342-349 ◽  
Author(s):  
Elena Maspero ◽  
Sara Mari ◽  
Eleonora Valentini ◽  
Andrea Musacchio ◽  
Alexander Fish ◽  
...  
Keyword(s):  
Chain Elongation ◽  
Ubiquitin Chain

scholarly journals Ubiquitin Chain Elongation: An Intriguing Strategy

2014 ◽  
Vol 56 (2) ◽  
pp. 189-191 ◽  
Author(s):  
Kazuhiro Iwai ◽  
Keiji Tanaka
Keyword(s):  
Chain Elongation ◽  
Ubiquitin Chain

scholarly journals A Mechanism for Protein Monoubiquitination Dependent on a trans-Acting Ubiquitin-binding Domain

2013 ◽  
Vol 288 (23) ◽  
pp. 16206-16211 ◽  
Author(s):  
Antonio Herrador ◽  
Sébastien Léon ◽  
Rosine Haguenauer-Tsapis ◽  
Olivier Vincent
Keyword(s):  
Chain Length ◽  
Ubiquitin Ligase ◽  
Functional Outcomes ◽  
Binding Domain ◽  
Chain Elongation ◽  
Related Protein ◽  
Ubiquitin Chain ◽  
Ubiquitin Binding ◽  
Ubiquitin Binding Domain

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.

scholarly journals A SnapShot of Ubiquitin Chain Elongation

2014 ◽  
Vol 289 (10) ◽  
pp. 7068-7081 ◽  
Author(s):  
Jordan Kovacev ◽  
Kenneth Wu ◽  
Donald E. Spratt ◽  
Robert A. Chong ◽  
Chan Lee ◽  
...  
Keyword(s):  
Chain Elongation ◽  
Ubiquitin Chain

scholarly journals RING domains act as both substrate and enzyme in a catalytic arrangement to drive self-anchored ubiquitination

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Leo Kiss ◽  
Dean Clift ◽  
Nadine Renner ◽  
David Neuhaus ◽  
Leo C. James
Keyword(s):  
Posttranslational Modifications ◽  
Substrate Binding ◽  
Cellular Level ◽  
Chemical Mechanism ◽  
Chain Elongation ◽  
Ubiquitin Chain ◽  
E3 Ligases ◽  
Physiological Processes ◽  
Ubiquitin Conjugation ◽  
Ring E3 Ligases

AbstractAttachment of ubiquitin (Ub) to proteins is one of the most abundant and versatile of all posttranslational modifications and affects outcomes in essentially all physiological processes. RING E3 ligases target E2 Ub-conjugating enzymes to the substrate, resulting in its ubiquitination. However, the mechanism by which a ubiquitin chain is formed on the substrate remains elusive. Here we demonstrate how substrate binding can induce a specific RING topology that enables self-ubiquitination. By analyzing a catalytically trapped structure showing the initiation of TRIM21 RING-anchored ubiquitin chain elongation, and in combination with a kinetic study, we illuminate the chemical mechanism of ubiquitin conjugation. Moreover, biochemical and cellular experiments show that the topology found in the structure can be induced by substrate binding. Our results provide insights into ubiquitin chain formation on a structural, biochemical and cellular level with broad implications for targeted protein degradation.

scholarly journals Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C

Cell ◽  
2016 ◽  
Vol 165 (6) ◽  
pp. 1440-1453 ◽  
Author(s):  
Nicholas G. Brown ◽  
Ryan VanderLinden ◽  
Edmond R. Watson ◽  
Florian Weissmann ◽  
Alban Ordureau ◽  
...  
Keyword(s):  
Chain Elongation ◽  
Ubiquitin Chain ◽  
Ring E3 ◽  
Dual Ring

Orchestra for assembly and fate of polyubiquitin chains

2005 ◽  
Vol 41 ◽  
pp. 1-14 ◽  
Author(s):  
Kuhlbrodt Kirsten ◽  
Mouysset Julien ◽  
Hoppe Thorsten
Keyword(s):  
Protein Degradation ◽  
Ubiquitin Ligase ◽  
Chain Elongation ◽  
Polyubiquitin Chain ◽  
Ubiquitin Chain ◽  
Polyubiquitin Chains ◽  
Intracellular Signals ◽  
Ubiquitin Binding ◽  
Ubiquitin Ligase E3 ◽  
Ubiquitin Conjugating Enzyme

Selective protein degradation by the 26 S proteasome usually requires a polyubiquitin chain attached to the protein substrate by three classes of enzymes: a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin ligase (E3). This reaction can produce different polyubiquitin chains that, depending on size and linkage type, can provide distinct intracellular signals. Interestingly, polyubiquitination is sometimes regulated by additional conjugation factors, called E4s (polyubiquitin chain conjugation factors). Yeast UFD2 (ubiquitin fusion degradation protein-2), the first E4 to be described, binds to the ubiquitin moieties of preformed conjugates and catalyses ubiquitin-chain elongation together with E1, E2, and E3. Recent studies have illustrated that the E4 enzyme UFD2 co-operates with an orchestra of ubiquitin-binding factors in an escort pathway to transfer and deliver polyubiquitinated substrates to the 26 S proteasome. Here we propose a model in which E4-dependent polyubiquitination pathways are modulated by different ubiquitin-binding proteins, using ataxin-3 as an example.

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