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A Comprehensive Atlas of E3 Ubiquitin Ligase Mutations in Neurological Disorders
Frontiers in Genetics, 2018 Protein ubiquitination is a posttranslational modification that plays an integral part in mediating diverse cellular functions. The process of protein ubiquitination requires an enzymatic cascade that consists of a ubiquitin activating enzyme (E1 ...
Arlene J. George +4 more
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Structural Diversity of Ubiquitin E3 Ligase
Molecules, 2021 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 ...
Sachiko Toma-Fukai, Toshiyuki Shimizu
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Cryo-EM structure of the human COP1-DET1 ubiquitin ligase complex [PDF]
Nature CommunicationsUbiquitin modifications regulate fundamental cellular activities by modulating protein stability and function. The ubiquitin ligase COP1, which is present across species from plants to humans, plays a crucial role in the ubiquitination of developmental ...
Shan Wang +4 more
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SCF ubiquitin ligase-targeted therapies [PDF]
Nature Reviews Drug Discovery, 2014 The clinical successes of proteasome inhibitors for the treatment of cancer have highlighted the therapeutic potential of targeting this protein degradation system. However, proteasome inhibitors prevent the degradation of numerous proteins, which may cause adverse effects.
Jeffrey R. Skaar, J. Pagan, M. Pagano
semanticscholar +4 more sources
The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
Nature, 2015 Protein aggregates and damaged organelles are tagged with ubiquitin chains to trigger selective autophagy. To initiate mitophagy, the ubiquitin kinase PINK1 phosphorylates ubiquitin to activate the ubiquitin ligase parkin, which builds ubiquitin chains ...
Michael Lazarou +2 more
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Cullin-RING Ubiquitin Ligase Regulatory Circuits: a Quarter Century Beyond the F-box Hypothesis.
Annual Review of Biochemistry, 2021 Cullin-RING ubiquitin ligases (CRLs) are dynamic modular platforms that regulate myriad biological processes through target-specific ubiquitylation. Our knowledge of this system emerged from the F-box hypothesis, posited a quarter century ago: Numerous ...
J. Harper, B. Schulman
semanticscholar +1 more source
Emerging roles of the HECT E3 ubiquitin ligases in gastric cancer
Pathology and Oncology Research, 2023 Gastric cancer (GC) is one of the most pernicious gastrointestinal tumors with extraordinarily high incidence and mortality. Ubiquitination modification of cellular signaling proteins has been shown to play important roles in GC tumorigenesis ...
Aiqin Sun +5 more
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Ubiquitin-protein ligases [PDF]
Journal of Cell Science, 2004 Post-translational covalent tagging of proteins with the 76-residue protein ubiquitin (Ub) serves many functions. Polyubiquitylated proteins are directed to the large multi-component, multi-catalytic protease the 26S proteasome.
P A, Robinson, H C, Ardley
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HERC Ubiquitin Ligases in Cancer [PDF]
Cancers, 2020 HERC proteins are ubiquitin E3 ligases of the HECT family. The HERC subfamily is composed of six members classified by size into large (HERC1 and HERC2) and small (HERC3–HERC6). HERC family ubiquitin ligases regulate important cellular processes, such as neurodevelopment, DNA damage response, cell proliferation, cell migration, and immune responses ...
Joan Sala-Gaston +7 more
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Self‐regulating ubiquitin ligases [PDF]
The EMBO Journal, 2017 Occasional auto‐modification of ubiquitin ligases typically leads to their proteasomal destruction, but new findings published in The EMBO Journal now show that in the case of Rsp5/Nedd4, auto‐ubiquitylation instead triggers oligomerization and concomitant reduction of ligase activity. This novel mechanism therefore creates silenced ligases that remain
Spencer Hill, Gary Kleiger
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