Results 21 to 30 of about 133,567 (215)
Adaptors as the regulators of HECT ubiquitin ligases [PDF]
Cell Death & Differentiation, 2021 The HECT (homologous to E6AP C-terminus) ubiquitin ligases (E3s) are a small family of highly conserved enzymes involved in diverse cellular functions and pathological conditions. Characterised by a C-terminal HECT domain that accepts ubiquitin from E2 ubiquitin conjugating enzymes, these E3s regulate key signalling pathways.
Sonia Shalini Shah, Sharad Kumar
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The HIV1 protein Vpr acts to enhance constitutive DCAF1-dependent UNG2 turnover. [PDF]
PLoS ONE, 2012 The HIV1 protein Vpr assembles with and acts through an ubiquitin ligase complex that includes DDB1 and cullin 4 (CRL4) to cause G2 cell cycle arrest and to promote degradation of both uracil DNA glycosylase 2 (UNG2) and single-strand selective mono ...
Xiaoyun Wen +4 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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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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Dysregulation of ubiquitin ligases in cancer [PDF]
Drug Resistance Updates, 2015 Ubiquitin ligases (UBLs) are critical components of the ubiquitin proteasome system (UPS), which governs fundamental processes regulating normal cellular homeostasis, metabolism, and cell cycle in response to external stress signals and DNA damage. Among multiple steps of the UPS system required to regulate protein ubiquitination and stability, UBLs ...
Ze'ev Ronai, Jianfei Qi
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Tag Team Ubiquitin Ligases [PDF]
Cell, 2016 Cullin-RING (CRL) and RING1-IBR-RING2 (RBR) are two distinct types of ubiquitin ligases. In this issue, Scott et al. show that CRLs activate the RBR enzyme ARIH1 to initiate ubiquitin chains on CRL substrates, thereby marking an unexpected and important advance in our understanding of both enzymes.
Gary Kleiger +2 more
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Ubiquitin Ligation without a Ligase [PDF]
Developmental Cell, 2007 Classically, ubiquitination requires three enzymes acting in sequence: E1, E2, and E3. E3 ubiquitin ligases typically provide substrate specificity. An article in Molecular Cell (Hoeller et al., 2007) now describes the E3-independent monoubiquitination of certain proteins. The mechanism has interesting parallels to SUMO ligation.
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FBXL17/spastin axis as a novel therapeutic target of hereditary spastic paraplegia
Cell & Bioscience, 2022 Background Spastin significantly influences microtubule regulation in neurons and is implicated in the pathogenesis of hereditary spastic paraplegia (HSP). However, post-translational regulation of the spastin protein remains nebulous.
Hyun Mi Kang +10 more
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Ubiquitin Ligases in Cholesterol Metabolism
Diabetes & Metabolism Journal, 2014 To maintain cholesterol homeostasis, the processes of cholesterol metabolism are regulated at multiple levels including transcription, translation, and enzymatic activity. Recently, the regulation of protein stability of some key players in cholesterol metabolism has been characterized.
Bao-Liang Song, Wei Jiang
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Linear ubiquitin chains: enzymes, mechanisms and biology [PDF]
Open Biology, 2017 Ubiquitination is a versatile post-translational modification that regulates a multitude of cellular processes. Its versatility is based on the ability of ubiquitin to form multiple types of polyubiquitin chains, which are recognized by specific ...
Katrin Rittinger, Fumiyo Ikeda
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