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Journal articles on the topic 'Ubiquitine ligases'

Author: Grafiati

Published: 23 November 2024

Last updated: 31 July 2025

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1

de Palma, Luigi, Mario Marinelli, Matteo Pavan, and Alessandro Orazi. "Rôle des ubiquitine ligases MuRF1 et MAFbx dans l’atrophie musculaire chez l’homme." Revue du Rhumatisme 75, no. 1 (2008): 56–60. http://dx.doi.org/10.1016/j.rhum.2007.04.021.

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Reboud-Ravaux, Michèle. "Dégradation induite des protéines par des molécules PROTAC et stratégies apparentées : développements à visée thérapeutique." Biologie Aujourd’hui 215, no. 1-2 (2021): 25–43. http://dx.doi.org/10.1051/jbio/2021007.

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Alors que, pour la plupart, les médicaments actuels sont de petites molécules inhibant l’action d’une protéine en bloquant un site d’interaction, la dégradation ciblée des protéines, découverte il y a une vingtaine d’années via les petites molécules PROTAC, connaît aujourd’hui un très grand développement, aussi bien au niveau universitaire qu’industriel. Cette dégradation ciblée permet de contrôler la concentration intracellulaire d’une protéine spécifique comme peuvent le faire les techniques basées sur les acides nucléiques (oligonucléotides antisens, ARNsi, CRISPR-Cas9). Les molécules PROTA

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Dumétier, Baptiste, Aymeric Zadoroznyj, and Laurence Dubrez. "IAP-Mediated Protein Ubiquitination in Regulating Cell Signaling." Cells 9, no. 5 (2020): 1118. http://dx.doi.org/10.3390/cells9051118.

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Over the last decade, the E3-ubiquitine ligases from IAP (Inhibitor of Apoptosis) family have emerged as potent regulators of immune response. In immune cells, they control signaling pathways driving differentiation and inflammation in response to stimulation of tumor necrosis factor receptor (TNFR) family, pattern-recognition receptors (PRRs), and some cytokine receptors. They are able to control the activity, the cellular fate, or the stability of actors of signaling pathways, acting at different levels from components of receptor-associated multiprotein complexes to signaling effectors and

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Taillandier, Daniel. "Contrôle des voies métaboliques par les enzymes E3 ligases : une opportunité de ciblage thérapeutique." Biologie Aujourd’hui 215, no. 1-2 (2021): 45–57. http://dx.doi.org/10.1051/jbio/2021006.

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Depuis sa découverte, le Système Ubiquitine Protéasome (UPS) est reconnu pour son rôle majeur dans le contrôle de la plupart des voies métaboliques de la cellule. Outre son rôle primordial dans la dégradation des protéines, il intervient aussi dans l’adressage, la signalisation ou la réparation de l’ADN, ce qui en fait un acteur incontournable de l’homéostasie cellulaire. Bien que d’autres systèmes de contrôles existent dans la cellule, l’UPS est souvent considéré comme le chef d’orchestre. Au vu de son importance, toute dérégulation de l’UPS entraîne des désordres plus ou moins sévères pour l

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Lee, Jaeseok, Youngjun Lee, Young Mee Jung, Ju Hyun Park, Hyuk Sang Yoo, and Jongmin Park. "Discovery of E3 Ligase Ligands for Target Protein Degradation." Molecules 27, no. 19 (2022): 6515. http://dx.doi.org/10.3390/molecules27196515.

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Target protein degradation has emerged as a promising strategy for the discovery of novel therapeutics during the last decade. Proteolysis-targeting chimera (PROTAC) harnesses a cellular ubiquitin-dependent proteolysis system for the efficient degradation of a protein of interest. PROTAC consists of a target protein ligand and an E3 ligase ligand so that it enables the target protein degradation owing to the induced proximity with ubiquitin ligases. Although a great number of PROTACs has been developed so far using previously reported ligands of proteins for their degradation, E3 ligase ligand

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Wang, Xiangyi S., Jenny Jiou, Anthony Cerra, et al. "The RBR E3 ubiquitin ligase HOIL-1 can ubiquitinate diverse non-protein substrates in vitro." Life Science Alliance 8, no. 6 (2025): e202503243. https://doi.org/10.26508/lsa.202503243.

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HOIL-1 is a RING-between-RING-family E3 ubiquitin ligase and a component of the linear ubiquitin chain assembly complex. Although most E3 ubiquitin ligases conjugate ubiquitin to protein lysine sidechains, HOIL-1 has also been reported to ubiquitinate hydroxyl groups in protein serine and threonine sidechains and glucosaccharides, such as glycogen and its building block maltose, in vitro. However, HOIL-1 substrate specificity is currently poorly defined. Here, we show that HOIL-1 is unable to ubiquitinate lysine but can efficiently ubiquitinate serine and a variety of model and physiologically

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Del Prete, Dolores, Richard C. Rice, Anjali M. Rajadhyaksha, and Luciano D'Adamio. "Amyloid Precursor Protein (APP) May Act as a Substrate and a Recognition Unit for CRL4CRBN and Stub1 E3 Ligases Facilitating Ubiquitination of Proteins Involved in Presynaptic Functions and Neurodegeneration." Journal of Biological Chemistry 291, no. 33 (2016): 17209–27. http://dx.doi.org/10.1074/jbc.m116.733626.

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The amyloid precursor protein (APP), whose mutations cause Alzheimer disease, plays an important in vivo role and facilitates transmitter release. Because the APP cytosolic region (ACR) is essential for these functions, we have characterized its brain interactome. We found that the ACR interacts with proteins that regulate the ubiquitin-proteasome system, predominantly with the E3 ubiquitin-protein ligases Stub1, which binds the NH2 terminus of the ACR, and CRL4CRBN, which is formed by Cul4a/b, Ddb1, and Crbn, and interacts with the COOH terminus of the ACR via Crbn. APP shares essential funct

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Catlett, Jerrel Lewis, Zhijie Deng, Youngeun Lee, Yan Xiong, Husnu Ü. Kaniskan, and Jian Jin. "Abstract 3758: Discovery of a bridged proteolysis targeting chimera (PROTAC) recruiting the SPOP E3 ubiquitin ligase for targeted protein degradation." Cancer Research 85, no. 8_Supplement_1 (2025): 3758. https://doi.org/10.1158/1538-7445.am2025-3758.

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Abstract Proteolysis Targeting Chimeras (PROTACs) are promising therapeutic modalities for eliminating disease-causing proteins, particularly in oncology. However, the widespread applicability of PROTAC technology is limited by the paucity of suitable E3 ubiquitin ligases available for targeted protein degradation (TPD) despite the existence of over 600 such ligases in the human genome. Many E3 ligases lack small-molecule ligands, rendering them inaccessible to recruitment by traditional PROTAC design methodology. To overcome this challenge, we instead leverage a high-affinity binder of the hi

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Kim, Jong Hum, Seok Keun Cho, Tae Rin Oh, Moon Young Ryu, Seong Wook Yang, and Woo Taek Kim. "MPSR1 is a cytoplasmic PQC E3 ligase for eliminating emergent misfolded proteins in Arabidopsis thaliana." Proceedings of the National Academy of Sciences 114, no. 46 (2017): E10009—E10017. http://dx.doi.org/10.1073/pnas.1713574114.

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Ubiquitin E3 ligases are crucial for eliminating misfolded proteins before they form cytotoxic aggregates that threaten cell fitness and survival. However, it remains unclear how emerging misfolded proteins in the cytoplasm can be selectively recognized and eliminated by E3 ligases in plants. We found that Misfolded Protein Sensing RING E3 ligase 1 (MPSR1) is an indispensable E3 ligase required for plant survival after protein-damaging stress. Under no stress, MPSR1 is prone to rapid degradation by the 26S proteasome, concealing its protein quality control (PQC) E3 ligase activity. Upon proteo

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Windheim, Mark, Mark Peggie, and Philip Cohen. "Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology." Biochemical Journal 409, no. 3 (2008): 723–29. http://dx.doi.org/10.1042/bj20071338.

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RING (really interesting new gene) and U-box E3 ligases bridge E2 ubiquitin-conjugating enzymes and substrates to enable the transfer of ubiquitin to a lysine residue on the substrate or to one of the seven lysine residues of ubiquitin for polyubiquitin chain elongation. Different polyubiquitin chains have different functions. Lys48-linked chains target proteins for proteasomal degradation, and Lys63-linked chains function in signal transduction, endocytosis and DNA repair. For this reason, chain topology must be tightly controlled. Using the U-box E3 ligase CHIP [C-terminus of the Hsc (heat-s

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Qian, Hao, Ying Zhang, Boquan Wu, et al. "Structure and function of HECT E3 ubiquitin ligases and their role in oxidative stress." Journal of Translational Internal Medicine 8, no. 2 (2020): 71–79. http://dx.doi.org/10.2478/jtim-2020-0012.

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AbstractUbiquitination is a modification after protein transcription that plays a vital role in maintaining the homeostasis of the cellular environment. The Homologous to E6AP C-terminus (HECT) family E3 ubiquitin ligases are a kind of E3 ubiquitin ligases with a C-terminal HECT domain that mediates the binding of ubiquitin to substrate proteins and a variable-length N-terminal extension. HECT-ubiquitinated ligases can be divided into three categories: NEDD4 superfamily, HERC superfamily, and other HECT superfamilies. HECT ubiquitin ligase plays an essential role in the development of many hum

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Tracz, Michał, Ireneusz Górniak, Andrzej Szczepaniak, and Wojciech Białek. "E3 Ubiquitin Ligase SPL2 Is a Lanthanide-Binding Protein." International Journal of Molecular Sciences 22, no. 11 (2021): 5712. http://dx.doi.org/10.3390/ijms22115712.

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The SPL2 protein is an E3 ubiquitin ligase of unknown function. It is one of only three types of E3 ligases found in the outer membrane of plant chloroplasts. In this study, we show that the cytosolic fragment of SPL2 binds lanthanide ions, as evidenced by fluorescence measurements and circular dichroism spectroscopy. We also report that SPL2 undergoes conformational changes upon binding of both Ca2+ and La3+, as evidenced by its partial unfolding. However, these structural rearrangements do not interfere with SPL2 enzymatic activity, as the protein retains its ability to auto-ubiquitinate in

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Ashitomi, Honoka, Tadashi Nakagawa, Makiko Nakagawa, and Toru Hosoi. "Cullin-RING Ubiquitin Ligases in Neurodevelopment and Neurodevelopmental Disorders." Biomedicines 13, no. 4 (2025): 810. https://doi.org/10.3390/biomedicines13040810.

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Ubiquitination is a dynamic and tightly regulated post-translational modification essential for modulating protein stability, trafficking, and function to preserve cellular homeostasis. This process is orchestrated through a hierarchical enzymatic cascade involving three key enzymes: the E1 ubiquitin-activating enzyme, the E2 ubiquitin-conjugating enzyme, and the E3 ubiquitin ligase. The final step of ubiquitination is catalyzed by the E3 ubiquitin ligase, which facilitates the transfer of ubiquitin from the E2 enzyme to the substrate, thereby dictating which proteins undergo ubiquitination. E

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Kelley, Dior R. "E3 Ubiquitin Ligases: Key Regulators of Hormone Signaling in Plants." Molecular & Cellular Proteomics 17, no. 6 (2018): 1047–54. http://dx.doi.org/10.1074/mcp.mr117.000476.

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Ubiquitin-mediated control of protein stability is central to most aspects of plant hormone signaling. Attachment of ubiquitin to target proteins occurs via an enzymatic cascade with the final step being catalyzed by a family of enzymes known as E3 ubiquitin ligases, which have been classified based on their protein domains and structures. Although E3 ubiquitin ligases are conserved among eukaryotes, in plants they are well-known to fulfill unique roles as central regulators of phytohormone signaling, including hormone perception and regulation of hormone biosynthesis. This review will highlig

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Martin-Serrano, Juan, Scott W. Eastman, Wayne Chung, and Paul D. Bieniasz. "HECT ubiquitin ligases link viral and cellular PPXY motifs to the vacuolar protein-sorting pathway." Journal of Cell Biology 168, no. 1 (2004): 89–101. http://dx.doi.org/10.1083/jcb.200408155.

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Many enveloped viruses exploit the class E vacuolar protein-sorting (VPS) pathway to bud from cells, and use peptide motifs to recruit specific class E VPS factors. Homologous to E6AP COOH terminus (HECT) ubiquitin ligases have been implicated as cofactors for PPXY motif–dependent budding, but precisely which members of this family are responsible, and how they access the VPS pathway is unclear. Here, we show that PPXY-dependent viral budding is unusually sensitive to inhibitory fragments derived from specific HECT ubiquitin ligases, namely WWP1 and WWP2. We also show that WWP1, WWP2, or Itch

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Marblestone, Jeffrey G., K. G. Suresh Kumar, Michael J. Eddins, et al. "Novel Approach for Characterizing Ubiquitin E3 Ligase Function." Journal of Biomolecular Screening 15, no. 10 (2010): 1220–28. http://dx.doi.org/10.1177/1087057110380456.

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The ubiquitin-proteasome system is central to the regulation of numerous cellular events, and dysregulation may lead to disease pathogenesis. E3 ubiquitin ligases typically function in concert with E1 and E2 enzymes to recruit specific substrates, thereby coordinating their ubiquitylation and subsequent proteasomal degradation or cellular activity. E3 ligases have been implicated in a wide range of pathologies, and monitoring their activity in a rapid and cost-effective manner would be advantageous in drug discovery. The relative lack of high-throughput screening (HTS)–compliant E3 ligase assa

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Yoshida, Yukiko, Yasushi Saeki, Arisa Murakami, et al. "A comprehensive method for detecting ubiquitinated substrates using TR-TUBE." Proceedings of the National Academy of Sciences 112, no. 15 (2015): 4630–35. http://dx.doi.org/10.1073/pnas.1422313112.

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The identification of substrates for ubiquitin ligases has remained challenging, because most substrates are either immediately degraded by the proteasome or processed by deubiquitinating enzymes (DUBs) to remove polyubiquitin. Although a methodology that enables detection of ubiquitinated proteins using ubiquitin Lys-ε-Gly-Gly (diGly) remnant antibodies and MS has been developed, it is still insufficient for identification and characterization of the ubiquitin-modified proteome in cells overexpressing a particular ubiquitin ligase. Here, we show that exogenously expressed trypsin-resistant ta

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Ibarra, Rebeca, Heather R. Borror, Bryce Hart, Richard G. Gardner, and Gary Kleiger. "The San1 Ubiquitin Ligase Avidly Recognizes Misfolded Proteins through Multiple Substrate Binding Sites." Biomolecules 11, no. 11 (2021): 1619. http://dx.doi.org/10.3390/biom11111619.

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Cellular homeostasis depends on robust protein quality control (PQC) pathways that discern misfolded proteins from functional ones in the cell. One major branch of PQC involves the controlled degradation of misfolded proteins by the ubiquitin-proteasome system. Here ubiquitin ligases must recognize and bind to misfolded proteins with sufficient energy to form a complex and with an adequate half-life to achieve poly-ubiquitin chain formation, the signal for protein degradation, prior to its dissociation from the ligase. It is not well understood how PQC ubiquitin ligases accomplish these tasks.

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Horn-Ghetko, Daniel, David T. Krist, J. Rajan Prabu, et al. "Ubiquitin ligation to F-box protein targets by SCF–RBR E3–E3 super-assembly." Nature 590, no. 7847 (2021): 671–76. http://dx.doi.org/10.1038/s41586-021-03197-9.

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AbstractE3 ligases are typically classified by hallmark domains such as RING and RBR, which are thought to specify unique catalytic mechanisms of ubiquitin transfer to recruited substrates1,2. However, rather than functioning individually, many neddylated cullin–RING E3 ligases (CRLs) and RBR-type E3 ligases in the ARIH family—which together account for nearly half of all ubiquitin ligases in humans—form E3–E3 super-assemblies3–7. Here, by studying CRLs in the SKP1–CUL1–F-box (SCF) family, we show how neddylated SCF ligases and ARIH1 (an RBR-type E3 ligase) co-evolved to ubiquitylate diverse s

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Sievers, Quinlan, Jessica Gasser, Glenn Cowley, John G. Doench, Eric Fischer, and Benjamin L. Ebert. "Genome-Scale Screen Reveals Genes Required for Lenalidomide-Mediated Degradation of Aiolos By CRL4-CRBN." Blood 128, no. 22 (2016): 5139. http://dx.doi.org/10.1182/blood.v128.22.5139.5139.

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Abstract Lenalidomide exerts its therapeutic effects in the malignancy multiple myeloma by facilitating the degradation of the transcription factors Ikaros (IKZF1) and Aiolos (IKZF3) by the CRL4-CRBN E3 ubiquitin ligase. In the following study we utilized a positive selection, genome-scale CRISPR-Cas9 screen in the lenalidomide-sensitive myeloma cell line, MM1S, to further our understanding of the molecular machinery which regulates and is required for lenalidomide-mediated modulation of CRL4-CRBN. The gRNAs demonstrating the greatest enrichment following selection with lenalidomide belong to

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Wang, Jinnan, Tianye Zhang, Aizhu Tu, et al. "Genome-Wide Identification and Analysis of APC E3 Ubiquitin Ligase Genes Family in Triticum aestivum." Genes 15, no. 3 (2024): 271. http://dx.doi.org/10.3390/genes15030271.

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E3 ubiquitin ligases play a pivotal role in ubiquitination, a crucial post-translational modification process. Anaphase-promoting complex (APC), a large cullin-RING E3 ubiquitin ligase, regulates the unidirectional progression of the cell cycle by ubiquitinating specific target proteins and triggering plant immune responses. Several E3 ubiquitin ligases have been identified owing to advancements in sequencing and annotation of the wheat genome. However, the types and functions of APC E3 ubiquitin ligases in wheat have not been reported. This study identified 14 members of the APC gene family i

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Saravanan, Konda Mani, Muthu Kannan, Prabhakar Meera, Nagaraj Bharathkumar, and Thirunavukarasou Anand. "E3 ligases: a potential multi-drug target for different types of cancers and neurological disorders." Future Medicinal Chemistry 14, no. 3 (2022): 187–201. http://dx.doi.org/10.4155/fmc-2021-0157.

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Ubiquitylation is a posttranslational modification of proteins that is necessary for a variety of cellular processes. E1 ubiquitin activating enzyme, E2 ubiquitin conjugating enzyme, and E3 ubiquitin ligase are all involved in transferring ubiquitin to the target substrate to regulate cellular function. The objective of this review is to provide an overview of different aspects of E3 ubiquitin ligases that can lead to major biological system failure in several deadly diseases. The first part of this review covers the important characteristics of E3 ubiquitin ligases and their classification ba

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Bhaduri, Utsa, and Giuseppe Merla. "Ubiquitination, Biotech Startups, and the Future of TRIM Family Proteins: A TRIM-Endous Opportunity." Cells 10, no. 5 (2021): 1015. http://dx.doi.org/10.3390/cells10051015.

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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 phar

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Rothweiler, Elisabeth M., Paul E. Brennan, and Kilian V. M. Huber. "Covalent fragment-based ligand screening approaches for identification of novel ubiquitin proteasome system modulators." Biological Chemistry 403, no. 4 (2022): 391–402. http://dx.doi.org/10.1515/hsz-2021-0396.

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Abstract Ubiquitination is a key regulatory mechanism vital for maintenance of cellular homeostasis. Protein degradation is induced by E3 ligases via attachment of ubiquitin chains to substrates. Pharmacological exploitation of this phenomenon via targeted protein degradation (TPD) can be achieved with molecular glues or bifunctional molecules facilitating the formation of ternary complexes between an E3 ligase and a given protein of interest (POI), resulting in ubiquitination of the substrate and subsequent proteolysis by the proteasome. Recently, the development of novel covalent fragment sc

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Sung, George. "Similar but Different: RBR E3 Ligases and their Domains that are Crucial for Function." McGill Science Undergraduate Research Journal 12, no. 1 (2017): 50–53. http://dx.doi.org/10.26443/msurj.v12i1.45.

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Background: The E3 ubiquitin ligases can be subdivided into four distinct types (RING, HECT, U-box, and RBR type) based on their domain architecture and ubiquitin transfer mechanism. Recent structures of different RBR E3 ligases have been solved showing enzymes in their autoinhibited state. The only exception is HOIP/ HOIL-1L which was recently solved in its “active” conformation. This review discusses the structural and functional characteristics of three different members of the RBR E3 ubiquitin ligase family: Parkin, HOIP/HOIL-1L, and HHARI. Methods: Searches were performed using PubMed. Se

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Rittinger, Katrin. "Ubiquitin-dependent regulation of immune and inflammatory signaling pathways." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C241. http://dx.doi.org/10.1107/s2053273314097587.

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Modification of proteins with ubiquitin is a key mechanism for the regulation of a wide range of cellular functions. The outcome of the modification is determined by the way ubiquitin molecules are linked to each other. Linear (M1-linked) ubiquitin chains play an important role in the regulation of immune and inflammatory signaling pathways and contribute to the activation of NF-κB. They are synthesized by the E3 ubiquitin ligase LUBAC (linear ubiquitin chain assembly complex) that is composed of at least three subunits named HOIL-1L, HOIP and SHARPIN. LUBAC belongs to the RBR (RING-inbetween-

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Conway, James A., Grant Kinsman, and Edgar R. Kramer. "The Role of NEDD4 E3 Ubiquitin–Protein Ligases in Parkinson’s Disease." Genes 13, no. 3 (2022): 513. http://dx.doi.org/10.3390/genes13030513.

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Parkinson’s disease (PD) is a debilitating neurodegenerative disease that causes a great clinical burden. However, its exact molecular pathologies are not fully understood. Whilst there are a number of avenues for research into slowing, halting, or reversing PD, one central idea is to enhance the clearance of the proposed aetiological protein, oligomeric α-synuclein. Oligomeric α-synuclein is the main constituent protein in Lewy bodies and neurites and is considered neurotoxic. Multiple E3 ubiquitin-protein ligases, including the NEDD4 (neural precursor cell expressed developmentally downregul

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Pu, Zuo-Xian, Jun-Li Wang, Yu-Yang Li, et al. "A Bacterial Platform for Studying Ubiquitination Cascades Anchored by SCF-Type E3 Ubiquitin Ligases." Biomolecules 14, no. 10 (2024): 1209. http://dx.doi.org/10.3390/biom14101209.

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Ubiquitination is one of the most important post-translational modifications in eukaryotes. The ubiquitination cascade includes ubiquitin-activating enzymes (E1), ubiquitin-conjugating enzymes (E2), and ubiquitin ligases (E3). The E3 ligases, responsible for substrate recognition, are the most abundant and varied proteins in the cascade and the most studied. SKP1-CUL1-F-Box (SCF)-type E3 ubiquitin ligases are multi-subunit RING (Really Interesting New Gene) E3 ubiquitin ligases, composed of CUL1 (Cullin 1), RBX1 (RING BOX 1), SKP1 (S-phase Kinase-associated Protein 1), and F-box proteins. In v

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Zhu, Liguo, Ying Li, Longyuan Zhou, et al. "Role of RING-Type E3 Ubiquitin Ligases in Inflammatory Signalling and Inflammatory Bowel Disease." Mediators of Inflammation 2020 (August 10, 2020): 1–10. http://dx.doi.org/10.1155/2020/5310180.

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Ubiquitination is a three-step enzymatic cascade for posttranslational protein modification. It includes the ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3). RING-type E3 ubiquitin ligases catalyse the posttranslational proteolytic and nonproteolytic functions in various physiological and pathological processes, such as inflammation-associated signal transduction. Resulting from the diversity of substrates and functional mechanisms, RING-type ligases regulate microbe recognition and inflammation by being involved in multiple inflammatory signallin

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Spratt, Donald E., Helen Walden, and Gary S. Shaw. "RBR E3 ubiquitin ligases: new structures, new insights, new questions." Biochemical Journal 458, no. 3 (2014): 421–37. http://dx.doi.org/10.1042/bj20140006.

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The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain enzymes. This unique family of E3 ligases includes parkin, whose dysfunction is linked to the pathogenesis of early-onset Parkinson's disease, and HOIP (HOIL-1-interacting protein) and HOIL-1 (haem-oxidized IRP2 ubiquitin ligase 1), members of the LUBAC (linear ubiquitin chain assembly complex). The RBR E3 ligases share common features with both the larger RING and HECT (homologous with E6-associated protein C-terminus) E3 ligase fam

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Giardina, Sarah F., Elena Valdambrini, Michael Peel, et al. "Cure-PROs: Next-generation targeted protein degraders." Journal of Clinical Oncology 41, no. 16_suppl (2023): e15101-e15101. http://dx.doi.org/10.1200/jco.2023.41.16_suppl.e15101.

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e15101 Background: Many proteins, including transcription factors and scaffolding proteins, are not amenable to targeting by traditional small molecule inhibitors due to the lack of a well-defined binding pocket or active site. Proteolysis-Targeting Chimeras (PROTACs) are a new class of hetero-bifunctional molecules that bind both a target protein and an E3 ubiquitin ligase, bringing the two into proximity for appending ubiquitin, and subsequently marking the target protein for proteasomal degradation. Currently, thirteen PROTACs are in clinical trials for oncology indications. However, the cl

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Tan, Xu, and Ning Zheng. "Hormone signaling through protein destruction: a lesson from plants." American Journal of Physiology-Endocrinology and Metabolism 296, no. 2 (2009): E223—E227. http://dx.doi.org/10.1152/ajpendo.90807.2008.

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Ubiquitin-dependent protein degradation has emerged as a major pathway regulating eukaryotic biology. By employing a variety of ubiquitin ligases to target specific cellular proteins, the ubiquitin-proteasome system controls physiological processes in a highly regulated fashion. Recent studies on a plant hormone auxin have unveiled a novel paradigm of signal transduction in which ubiquitin ligases function as hormone receptors. Perceived by the F-box protein subunit of the SCFTIR1 ubiquitin ligase, auxin directly promotes the recruitment of a family of transcriptional repressors for ubiquitina

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Cooper, Jonathan A., Tomonori Kaneko, and Shawn S. C. Li. "Cell Regulation by Phosphotyrosine-Targeted Ubiquitin Ligases." Molecular and Cellular Biology 35, no. 11 (2015): 1886–97. http://dx.doi.org/10.1128/mcb.00098-15.

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Three classes of E3 ubiquitin ligases, members of the Cbl, Hakai, and SOCS-Cul5-RING ligase families, stimulate the ubiquitination of phosphotyrosine-containing proteins, including receptor and nonreceptor tyrosine kinases and their phosphorylated substrates. Because ubiquitination frequently routes proteins for degradation by the lysosome or proteasome, these E3 ligases are able to potently inhibit tyrosine kinase signaling. Their loss or mutational inactivation can contribute to cancer, autoimmunity, or endocrine disorders, such as diabetes. However, these ligases also have biological functi

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Zhang, Ting, Yue Xu, Yanfen Liu, and Yihong Ye. "gp78 functions downstream of Hrd1 to promote degradation of misfolded proteins of the endoplasmic reticulum." Molecular Biology of the Cell 26, no. 24 (2015): 4438–50. http://dx.doi.org/10.1091/mbc.e15-06-0354.

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Eukaryotic cells eliminate misfolded proteins from the endoplasmic reticulum (ER) via a conserved process termed ER-associated degradation (ERAD). Central regulators of the ERAD system are membrane-bound ubiquitin ligases, which are thought to channel misfolded proteins through the ER membrane during retrotranslocation. Hrd1 and gp78 are mammalian ubiquitin ligases homologous to Hrd1p, an ubiquitin ligase essential for ERAD in Saccharomyces cerevisiae. However, the functional relevance of these proteins to Hrd1p is unclear. In this paper, we characterize the gp78-containing ubiquitin ligase co

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Ganesan, Ishaar P., and Hiroaki Kiyokawa. "A Perspective on Therapeutic Targeting Against Ubiquitin Ligases to Stabilize Tumor Suppressor Proteins." Cancers 17, no. 4 (2025): 626. https://doi.org/10.3390/cancers17040626.

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The loss of functions of tumor suppressor (TS) genes plays a key role in not only tumor initiation but also tumor progression leading to poor prognosis. While therapeutic inhibition of oncogene-encoded kinases has shown clinical success, restoring TS functions remains challenging due to conceptual and technical limitations. E3 ubiquitin ligases that ubiquitinate TS proteins for accelerated degradation in cancers emerge as promising therapeutic targets. Unlike proteasomal inhibitors with a broad spectrum, inhibitors of an E3 ligase would offer superior selectivity and efficacy in enhancing expr

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Li, Zhongyan, Jingting Wan, Shangfu Li, et al. "Multi-Omics Characterization of E3 Regulatory Patterns in Different Cancer Types." International Journal of Molecular Sciences 25, no. 14 (2024): 7639. http://dx.doi.org/10.3390/ijms25147639.

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Ubiquitination, a post-translational modification, refers to the covalent attachment of ubiquitin molecules to substrates. This modification plays a critical role in diverse cellular processes such as protein degradation. The specificity of ubiquitination for substrates is regulated by E3 ubiquitin ligases. Dysregulation of ubiquitination has been associated with numerous diseases, including cancers. In our study, we first investigated the protein expression patterns of E3 ligases across 12 cancer types. Our findings indicated that E3 ligases tend to be up-regulated and exhibit reduced tissue

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Fredrickson, Eric K., Joel C. Rosenbaum, Melissa N. Locke, Thomas I. Milac, and Richard G. Gardner. "Exposed hydrophobicity is a key determinant of nuclear quality control degradation." Molecular Biology of the Cell 22, no. 13 (2011): 2384–95. http://dx.doi.org/10.1091/mbc.e11-03-0256.

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Protein quality control (PQC) degradation protects the cell by preventing the toxic accumulation of misfolded proteins. In eukaryotes, PQC degradation is primarily achieved by ubiquitin ligases that attach ubiquitin to misfolded proteins for proteasome degradation. To function effectively, PQC ubiquitin ligases must distinguish misfolded proteins from their normal counterparts by recognizing an attribute of structural abnormality commonly shared among misfolded proteins. However, the nature of the structurally abnormal feature recognized by most PQC ubiquitin ligases is unknown. Here we demons

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Lukashchuk, Natalia, and Karen H. Vousden. "Ubiquitination and Degradation of Mutant p53." Molecular and Cellular Biology 27, no. 23 (2007): 8284–95. http://dx.doi.org/10.1128/mcb.00050-07.

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ABSTRACT While wild-type p53 is normally a rapidly degraded protein, mutant forms of p53 are stabilized and accumulate to high levels in tumor cells. In this study, we show that mutant and wild-type p53 proteins are ubiquitinated and degraded through overlapping but distinct pathways. While Mdm2 can drive the degradation of both mutant and wild-type p53, our data suggest that the ability of Mdm2 to function as a ubiquitin ligase is less important in the degradation of mutant p53, which is heavily ubiquitinated in an Mdm2-independent manner. Our initial attempts to identify ubiquitin ligases th

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Matsuhisa, Koji, Shinya Sato, and Masayuki Kaneko. "Identification of E3 Ubiquitin Ligase Substrates Using Biotin Ligase-Based Proximity Labeling Approaches." Biomedicines 13, no. 4 (2025): 854. https://doi.org/10.3390/biomedicines13040854.

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Ubiquitylation is a post-translational modification originally identified as the first step in protein degradation by the ubiquitin–proteasome system. Ubiquitylation is also known to regulate many cellular processes without degrading the ubiquitylated proteins. Substrate proteins are specifically recognized and ubiquitylated by ubiquitin ligases. It is necessary to identify the substrates for each ubiquitin ligase to understand the physiological and pathological roles of ubiquitylation. Recently, a promiscuous mutant of a biotin ligase derived from Escherichia coli, BioID, and its variants hav

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Antoniou, Nikolaos, Nefeli Lagopati, Dimitrios Ilias Balourdas, et al. "The Role of E3, E4 Ubiquitin Ligase (UBE4B) in Human Pathologies." Cancers 12, no. 1 (2019): 62. http://dx.doi.org/10.3390/cancers12010062.

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The genome is exposed daily to many deleterious factors. Ubiquitination is a mechanism that regulates several crucial cellular functions, allowing cells to react upon various stimuli in order to preserve their homeostasis. Ubiquitin ligases act as specific regulators and actively participate among others in the DNA damage response (DDR) network. UBE4B is a newly identified member of E3 ubiquitin ligases that appears to be overexpressed in several human neoplasms. The aim of this review is to provide insights into the role of UBE4B ubiquitin ligase in DDR and its association with p53 expression

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Fuseya, Yasuhiro, and Kazuhiro Iwai. "Biochemistry, Pathophysiology, and Regulation of Linear Ubiquitination: Intricate Regulation by Coordinated Functions of the Associated Ligase and Deubiquitinase." Cells 10, no. 10 (2021): 2706. http://dx.doi.org/10.3390/cells10102706.

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The ubiquitin system modulates protein functions by decorating target proteins with ubiquitin chains in most cases. Several types of ubiquitin chains exist, and chain type determines the mode of regulation of conjugated proteins. LUBAC is a ubiquitin ligase complex that specifically generates N-terminally Met1-linked linear ubiquitin chains. Although linear ubiquitin chains are much less abundant than other types of ubiquitin chains, they play pivotal roles in cell survival, proliferation, the immune response, and elimination of bacteria by selective autophagy. Because linear ubiquitin chains

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Mintis, Dimitris G., Anastasia Chasapi, Konstantinos Poulas, George Lagoumintzis, and Christos T. Chasapis. "Assessing the Direct Binding of Ark-Like E3 RING Ligases to Ubiquitin and Its Implication on Their Protein Interaction Network." Molecules 25, no. 20 (2020): 4787. http://dx.doi.org/10.3390/molecules25204787.

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The ubiquitin pathway required for most proteins’ targeted degradation involves three classes of enzymes: E1-activating enzyme, E2-conjugating enzyme, and E3-ligases. The human Ark2C is the single known E3 ligase that adopts an alternative, Ub-dependent mechanism for the activation of Ub transfer in the pathway. Its RING domain binds both E2-Ub and free Ub with high affinity, resulting in a catalytic active UbR-RING-E2-UbD complex formation. We examined potential changes in the conformational plasticity of the Ark2C RING domain and its ligands in their complexed form within the ubiquitin pathw

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Kelsall, Ian R., Jiazhen Zhang, Axel Knebel, J. Simon C. Arthur, and Philip Cohen. "The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells." Proceedings of the National Academy of Sciences 116, no. 27 (2019): 13293–98. http://dx.doi.org/10.1073/pnas.1905873116.

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The linear ubiquitin assembly complex (LUBAC) comprises 3 components: HOIP, HOIL-1, and Sharpin, of which HOIP and HOIL-1 are both members of the RBR subfamily of E3 ubiquitin ligases. HOIP catalyses the formation of Met1-linked ubiquitin oligomers (also called linear ubiquitin), but the function of the E3 ligase activity of HOIL-1 is unknown. Here, we report that HOIL-1 is an atypical E3 ligase that forms oxyester bonds between the C terminus of ubiquitin and serine and threonine residues in its substrates. Exploiting the sensitivity of HOIL-1–generated oxyester bonds to cleavage by hydroxyla

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Cabana, Valérie C., and Marc P. Lussier. "From Drosophila to Human: Biological Function of E3 Ligase Godzilla and Its Role in Disease." Cells 11, no. 3 (2022): 380. http://dx.doi.org/10.3390/cells11030380.

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The ubiquitin–proteasome system is of fundamental importance in all fields of biology due to its impact on proteostasis and in regulating cellular processes. Ubiquitination, a type of protein post-translational modification, involves complex enzymatic machinery, such as E3 ubiquitin ligases. The E3 ligases regulate the covalent attachment of ubiquitin to a target protein and are involved in various cellular mechanisms, including the cell cycle, cell division, endoplasmic reticulum stress, and neurotransmission. Because the E3 ligases regulate so many physiological events, they are also associa

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Ren, Jihui, Younghoon Kee, Jon M. Huibregtse, and Robert C. Piper. "Hse1, a Component of the Yeast Hrs-STAM Ubiquitin-sorting Complex, Associates with Ubiquitin Peptidases and a Ligase to Control Sorting Efficiency into Multivesicular Bodies." Molecular Biology of the Cell 18, no. 1 (2007): 324–35. http://dx.doi.org/10.1091/mbc.e06-06-0557.

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Ubiquitinated integral membrane proteins are delivered to the interior of the lysosome/vacuole for degradation. This process relies on specific ubiquitination of potential cargo and recognition of that Ub-cargo by sorting receptors at multiple compartments. We show that the endosomal Hse1-Vps27 sorting receptor binds to ubiquitin peptidases and the ubiquitin ligase Rsp5. Hse1 is linked to Rsp5 directly via a PY element within its C-terminus and through a novel protein Hua1, which recruits a complex of Rsp5, Rup1, and Ubp2. The SH3 domain of Hse1 also binds to the deubiquitinating protein Ubp7.

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Wei, Wei, Jian-ye Chen, Ze-xiang Zeng, Jian-fei Kuang, Wang-jin Lu, and Wei Shan. "The Ubiquitin E3 Ligase MaLUL2 Is Involved in High Temperature-Induced Green Ripening in Banana Fruit." International Journal of Molecular Sciences 21, no. 24 (2020): 9386. http://dx.doi.org/10.3390/ijms21249386.

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Harvested banana fruit ripened under warm temperatures above 24 °C remain green peel, leading to severe economic loss. E3 ubiquitin-ligases, as the major components in the ubiquitination pathway, have been implicated to play important roles in temperature-stress responses. However, the molecular mechanism underlying high temperature-triggered stay-green ripening bananas in association with E3 ubiquitin-ligases, remains largely unknown. In this study, a RING-type E3 ubiquitin ligase termed MaLUL2, was isolated and characterized from banana fruit. The MaLUL2 gene contains 1095 nucleotides and en

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Márquez-Cantudo, Laura, Ana Ramos, Claire Coderch, and Beatriz de Pascual-Teresa. "Proteasomal Degradation of Zn-Dependent Hdacs: The E3-Ligases Implicated and the Designed Protacs that Enable Degradation." Molecules 26, no. 18 (2021): 5606. http://dx.doi.org/10.3390/molecules26185606.

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Protein degradation by the Ubiquitin-Proteasome System is one of the main mechanisms of the regulation of cellular proteostasis, and the E3 ligases are the key effectors for the protein recognition and degradation. Many E3 ligases have key roles in cell cycle regulation, acting as checkpoints and checkpoint regulators. One of the many important proteins involved in the regulation of the cell cycle are the members of the Histone Deacetylase (HDAC) family. The importance of zinc dependent HDACs in the regulation of chromatin packing and, therefore, gene expression, has made them targets for the

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Toma-Fukai, Sachiko, and Toshiyuki Shimizu. "Structural Diversity of Ubiquitin E3 Ligase." Molecules 26, no. 21 (2021): 6682. http://dx.doi.org/10.3390/molecules26216682.

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The post-translational modification of proteins regulates many biological processes. Their dysfunction relates to diseases. Ubiquitination is one of the post-translational modifications that target lysine residue and regulate many cellular processes. Three enzymes are required for achieving the ubiquitination reaction: ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3). E3s play a pivotal role in selecting substrates. Many structural studies have been conducted to reveal the molecular mechanism of the ubiquitination reaction. Recently, the structure

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Palomba, Tommaso, Giusy Tassone, Carmine Vacca, et al. "Exploiting ELIOT for Scaffold-Repurposing Opportunities: TRIM33 a Possible Novel E3 Ligase to Expand the Toolbox for PROTAC Design." International Journal of Molecular Sciences 23, no. 22 (2022): 14218. http://dx.doi.org/10.3390/ijms232214218.

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The field of targeted protein degradation, through the control of the ubiquitin–proteasome system (UPS), is progressing considerably; to exploit this new therapeutic modality, the proteolysis targeting chimera (PROTAC) technology was born. The opportunity to use PROTACs engaging of new E3 ligases that can hijack and control the UPS system could greatly extend the applicability of degrading molecules. To this end, here we show a potential application of the ELIOT (E3 LIgase pocketOme navigaTor) platform, previously published by this group, for a scaffold-repurposing strategy to identify new lig

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Oswald, Jessica, Mathew Constantine, Adedolapo Adegbuyi, Esosa Omorogbe, Anna J. Dellomo, and Elana S. Ehrlich. "E3 Ubiquitin Ligases in Gammaherpesviruses and HIV: A Review of Virus Adaptation and Exploitation." Viruses 15, no. 9 (2023): 1935. http://dx.doi.org/10.3390/v15091935.

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For productive infection and replication to occur, viruses must control cellular machinery and counteract restriction factors and antiviral proteins. Viruses can accomplish this, in part, via the regulation of cellular gene expression and post-transcriptional and post-translational control. Many viruses co-opt and counteract cellular processes via modulation of the host post-translational modification machinery and encoding or hijacking kinases, SUMO ligases, deubiquitinases, and ubiquitin ligases, in addition to other modifiers. In this review, we focus on three oncoviruses, Epstein–Barr viru

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