Classification and interaction modes of 40 rice E2 ubiquitin-conjugating enzymes with 17 rice ARM-U-box E3 ubiquitin ligases

2014 ◽  
Vol 444 (4) ◽  
pp. 575-580 ◽  
Author(s):  
Hansol Bae ◽  
Woo Taek Kim
Keyword(s):  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Conjugating Enzymes ◽  
Ubiquitin Conjugating Enzymes

scholarly journals E3 ubiquitin ligase components in GtoPdb v.2021.3

2021 ◽  
Vol 2021 (3) ◽  
Author(s):  
Elena Faccenda ◽  
Robert Layfield
Keyword(s):  
Cell Cycle Progression ◽  
Protein Complexes ◽  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Post Translational Modification ◽  
Protein Substrates ◽  
Cellular Processes ◽  
Ubiquitin Molecule ◽  
E2 Enzymes ◽  
Ubiquitin Conjugating Enzymes

Ubiquitination (a.k.a. ubiquitylation) is a protein post-translational modification that typically requires the sequential action of three enzymes: E1 (ubiquitin-activating enzymes), E2 (ubiquitin-conjugating enzymes), and E3 (ubiquitin ligases) [19]. Ubiquitination of proteins can target them for proteasomal degradation, or modulate cellular processes including cell cycle progression, transcriptional regulation, DNA repair and signal transduction. E3 ubiquitin ligases, of which there are >600 in humans, are a family of highly heterogeneous proteins and protein complexes that recruit ubiquitin-loaded E2 enzymes to mediate transfer of the ubiquitin molecule from the E2 to protein substrates. Target substrate specificity is determined by a substrate recognition subunit within the E3 complex.

scholarly journals Pex2 and Pex12 Function as Protein-Ubiquitin Ligases in Peroxisomal Protein Import

2009 ◽  
Vol 29 (20) ◽  
pp. 5505-5516 ◽  
Author(s):  
Harald W. Platta ◽  
Fouzi El Magraoui ◽  
Bastian E. Bäumer ◽  
Daniel Schlee ◽  
Wolfgang Girzalsky ◽  
...  
Keyword(s):  
Matrix Protein ◽  
Protein Import ◽  
Ubiquitin Ligases ◽  
Receptor Protein ◽  
Receptor Complex ◽  
Peroxisomal Protein ◽  
Cargo Receptor ◽  
Conjugating Enzymes ◽  
Ubiquitin Conjugating Enzymes ◽  
Import Receptor

ABSTRACT The PTS1-dependent peroxisomal matrix protein import is facilitated by the receptor protein Pex5 and can be divided into cargo recognition in the cytosol, membrane docking of the cargo-receptor complex, cargo release, and recycling of the receptor. The final step is controlled by the ubiquitination status of Pex5. While polyubiquitinated Pex5 is degraded by the proteasome, monoubiquitinated Pex5 is destined for a new round of the receptor cycle. Recently, the ubiquitin-conjugating enzymes involved in Pex5 ubiquitination were identified as Ubc4 and Pex4 (Ubc10), whereas the identity of the corresponding protein-ubiquitin ligases remained unknown. Here we report on the identification of the protein-ubiquitin ligases that are responsible for the ubiquitination of the peroxisomal protein import receptor Pex5. It is demonstrated that each of the three RING peroxins Pex2, Pex10, and Pex12 exhibits ubiquitin-protein isopeptide ligase activity. Our results show that Pex2 mediates the Ubc4-dependent polyubiquitination whereas Pex12 facilitates the Pex4-dependent monoubiquitination of Pex5.

scholarly journals E3 ubiquitin ligase components (version 2019.5) in the IUPHAR/BPS Guide to Pharmacology Database

2019 ◽  
Vol 2019 (5) ◽  
Author(s):  
Elena Faccenda ◽  
Robert Layfield
Keyword(s):  
Cell Cycle Progression ◽  
Protein Complexes ◽  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Post Translational Modification ◽  
Protein Substrates ◽  
Cellular Processes ◽  
Ubiquitin Molecule ◽  
E2 Enzymes ◽  
Ubiquitin Conjugating Enzymes

Ubiquitination (a.k.a. ubiquitylation) is a protein post-translational modification that typically requires the sequential action of three enzymes: E1 (ubiquitin-activating enzymes), E2 (ubiquitin-conjugating enzymes), and E3 (ubiquitin ligases) [16]. Ubiquitination of proteins can target them for proteasomal degradation, or modulate cellular processes including cell cycle progression, transcriptional regulation, DNA repair and signal transduction. E3 ubiquitin ligases, of which there are >600 in humans, are a family of highly heterogeneous proteins and protein complexes that recruit ubiquitin-loaded E2 enzymes to mediate transfer of the ubiquitin molecule from the E2 to protein substrates. Target substrate specificity is determined by a substrate recognition subunit within the E3 complex.

scholarly journals Reconstitution of human CMG helicase ubiquitylation by CUL2LRR1 and multiple E2 enzymes

2021 ◽  
Author(s):  
Thanh Thi Le ◽  
Johanna Ainsworth ◽  
Cristian Polo Rivera ◽  
Thomas Macartney ◽  
Karim Labib
Keyword(s):  
Dna Replication ◽  
Ubiquitin Ligases ◽  
Human Cells ◽  
Ubiquitin Chain ◽  
Human Proteins ◽  
Mouse Cells ◽  
Conjugating Enzymes ◽  
E2 Enzymes ◽  
Ubiquitin Conjugating Enzymes

Cullin ubiquitin ligases drive replisome disassembly during DNA replication termination.  In worm, frog and mouse cells, CUL2LRR1 is required to ubiquitylate the MCM7 subunit of the CMG helicase.  Here we show that cullin ligases also drive CMG-MCM7 ubiquitylation in human cells, thereby making the helicase into a substrate for the p97 unfoldase.  Using purified human proteins, including a panel of E2 ubiquitin conjugating enzymes, we have reconstituted CMG helicase ubiquitylation, dependent upon neddylated CUL2LRR1.  The reaction is highly specific to CMG-MCM7 and requires the LRR1 substrate targeting subunit, since replacement of LRR1 with the alternative CUL2 adaptor VHL switches ubiquitylation from CMG-MCM7 to HIF1.  CUL2LRR1 firstly drives monoubiquitylation of CMG-MCM7 by the UBE2D class of E2 enzymes.  Subsequently, CUL2LRR1 activates UBE2R1/R2 or UBE2G1/G2 to extend a single K48-linked ubiquitin chain on CMG-MCM7.  Thereby, CUL2LRR1 converts CMG into a substrate for p97, which disassembles the ubiquitylated helicase during DNA replication termination.

Regulation of Epithelial-Mesenchymal Transition by E3 Ubiquitin Ligases and Deubiquitinase in Cancer

2016 ◽  
Vol 16 (2) ◽  
pp. 110-118 ◽  
Author(s):  
Yasumichi Inoue ◽  
Yuka Itoh ◽  
Koichi Sato ◽  
Fumihiro Kawasaki ◽  
Chihiro Sumita ◽  
...  
Keyword(s):  
Epithelial Mesenchymal Transition ◽  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Mesenchymal Transition

scholarly journals Ubiquitination, Biotech Startups, and the Future of TRIM Family Proteins: A TRIM-Endous Opportunity

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1015
Author(s):  
Utsa Bhaduri ◽  
Giuseppe Merla
Keyword(s):  
Drug Discovery ◽  
Protein Degradation ◽  
Ubiquitin Ligase ◽  
Genetic Disorders ◽  
E3 Ubiquitin Ligase ◽  
Ubiquitin Ligases ◽  
E3 Ubiquitin Ligases ◽  
Post Translational Modification ◽  
Disease Biology ◽  
The Future

Ubiquitination is a post-translational modification that has pivotal roles in protein degradation and diversified cellular processes, and for more than two decades it has been a subject of interest in the biotech or biopharmaceutical industry. Tripartite motif (TRIM) family proteins are known to have proven E3 ubiquitin ligase activities and are involved in a multitude of cellular and physiological events and pathophysiological conditions ranging from cancers to rare genetic disorders. Although in recent years many kinds of E3 ubiquitin ligases have emerged as the preferred choices of big pharma and biotech startups in the context of protein degradation and disease biology, from a surface overview it appears that TRIM E3 ubiquitin ligases are not very well recognized yet in the realm of drug discovery. This article will review some of the blockbuster scientific discoveries and technological innovations from the world of ubiquitination and E3 ubiquitin ligases that have impacted the biopharma community, from biotech colossuses to startups, and will attempt to evaluate the future of TRIM family proteins in the province of E3 ubiquitin ligase-based drug discovery.

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