scholarly journals The ubiquitin-conjugating enzyme Ubc13-Mms2 cooperates with a family of FYVE-type-RING ubiquitin protein ligases in K63-polyubiquitylation at internal membranes

2019 ◽  
Author(s):  
Christian Renz ◽  
Vera Tröster ◽  
Thomas K. Albert ◽  
Olivier Santt ◽  
Susan C. Jacobs ◽  
...  
Keyword(s):  
Membrane Trafficking ◽  
Budding Yeast ◽  
Ring Finger ◽  
Multivesicular Body ◽  
Phenotypic Analysis ◽  
Nuclear Ring ◽  
Ubiquitin Conjugating Enzyme ◽  
Ring Finger Proteins ◽  
Inflammatory Signalling ◽  
Conjugating Enzyme

AbstractThe heterodimeric ubiquitin-conjugating enzyme (E2), Ubc13-Mms2, catalyses K63-specific polyubiquitylation in genome maintenance and inflammatory signalling. In budding yeast, the only ubiquitin protein ligase (E3) known to cooperate with Ubc13-Mms2 so far is a nuclear RING finger protein, Rad5, involved in the replication of damaged DNA. We have now identified a family of membrane-associated FYVE-(type)-RING finger proteins as cognate E3s for Ubc13-Mms2 in several species. We show that budding yeast Pib1, a FYVE-RING finger E3 associated with internal membranes, exhibits exquisite selectivity for Ubc13-Mms2 and cooperates with the E2 in the multivesicular body pathway. Phenotypic analysis indicates that the contribution of Ubc13-Mms2 to membrane trafficking goes beyond its cooperation with Pib1, suggesting an involvement with additional E3s in the endocytic compartment. These results widely implicate Ubc13-Mms2 in the regulation of membrane protein sorting.

scholarly journals E3 ligase activity of RING finger proteins that interact with Hip-2, a human ubiquitin-conjugating enzyme

FEBS Letters ◽  
2001 ◽  
Vol 503 (1) ◽  
pp. 61-64 ◽  
Author(s):  
Sun-Joo Lee ◽  
Ju-Youn Choi ◽  
Yong-Mo Sung ◽  
Hyewon Park ◽  
Hyangshuk Rhim ◽  
...  
Keyword(s):  
Ring Finger ◽  
E3 Ligase ◽  
Human Ubiquitin ◽  
Ubiquitin Conjugating Enzyme ◽  
Ring Finger Proteins ◽  
Conjugating Enzyme

scholarly journals Ube2W conjugates ubiquitin to α-amino groups of protein N-termini

2013 ◽  
Vol 453 (1) ◽  
pp. 137-145 ◽  
Author(s):  
Michael H. Tatham ◽  
Anna Plechanovová ◽  
Ellis G. Jaffray ◽  
Helena Salmen ◽  
Ronald T. Hay
Keyword(s):  
Ring Finger ◽  
Specific Protein ◽  
Cysteine Residue ◽  
Cellular Systems ◽  
Covalent Attachment ◽  
Amino Group ◽  
Ubiquitin Conjugating Enzyme ◽  
E2 Enzymes ◽  
Almost All ◽  
Conjugating Enzyme

The covalent attachment of the protein ubiquitin to intracellular proteins by a process known as ubiquitylation regulates almost all major cellular systems, predominantly by regulating protein turnover. Ubiquitylation requires the co-ordinated action of three enzymes termed E1, E2 and E3, and typically results in the formation of an isopeptide bond between the C-terminal carboxy group of ubiquitin and the ϵ-amino group of a target lysine residue. However, ubiquitin is also known to conjugate to the thiol of cysteine residue side chains and the α-amino group of protein N-termini, although the enzymes responsible for discrimination between different chemical groups have not been defined. In the present study, we show that Ube2W (Ubc16) is an E2 ubiquitin-conjugating enzyme with specific protein N-terminal mono-ubiquitylation activity. Ube2W conjugates ubiquitin not only to its own N-terminus, but also to that of the small ubiquitin-like modifier SUMO (small ubiquitin-related modifier) in a manner dependent on the SUMO-targeted ubiquitin ligase RNF4 (RING finger protein 4). Furthermore, N-terminal mono-ubiquitylation of SUMO-2 primes it for poly-ubiquitylation by the Ubc13–UEV1 (ubiquitin-conjugating enzyme E2 variant 1) heterodimer, showing that N-terminal ubiquitylation regulates protein fate. The description in the present study is the first of an E2-conjugating enzyme with N-terminal ubiquitylation activity, and highlights the importance of E2 enzymes in the ultimate outcome of E3-mediated ubiquitylation.

scholarly journals Deletion of the ubiquitin-conjugating enzyme Ubc2 confers resistance to methylmercury in budding yeast by promoting Whi2 degradation

2013 ◽  
Vol 38 (2) ◽  
pp. 301-303 ◽  
Author(s):  
Gi-Wook Hwang ◽  
Fujio Mastuyama ◽  
Tsutomu Takahashi ◽  
Jin-Yong Lee ◽  
Akira Naganuma
Keyword(s):  
Budding Yeast ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzyme

A Conserved Asparagine in a Ubiquitin Conjugating Enzyme Positions the Substrate for Nucleophilic Attack

2018 ◽  
Author(s):  
Walker M. Jones ◽  
Aaron G. Davis ◽  
R. Hunter Wilson ◽  
Katherine L. Elliott ◽  
Isaiah Sumner
Keyword(s):  
Molecular Dynamics ◽  
Quantum Mechanics ◽  
Molecular Mechanics ◽  
Reaction Rates ◽  
Nucleophilic Attack ◽  
Classical Molecular Dynamics ◽  
Ubiquitin Conjugating Enzyme ◽  
Conjugating Enzyme

We present classical molecular dynamics (MD), Born-Oppenheimer molecular dynamics (BOMD), and hybrid quantum mechanics/molecular mechanics (QM/MM) data. MD was performed using the GPU accelerated pmemd module of the AMBER14MD package. BOMD was performed using CP2K version 2.6. The reaction rates in BOMD were accelerated using the Metadynamics method. QM/MM was performed using ONIOM in the Gaussian09 suite of programs. Relevant input files for BOMD and QM/MM are available.

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