&lt;em&gt;In Vitro&lt;/em&gt; Analysis of E3 Ubiquitin Ligase Function

Müller, Leonie; Kutzner, Carl Elias; Balaji, Vishnu; Hoppe, Thorsten

doi:10.3791/62393-v

Cited by 2 publications

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“…20,21 Protein ubiquitination modification is a process in which three different types of enzymes, E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme, and E3 ubiquitin ligase, connect ubiquitin to the substrate through a three-step cascade reaction (Figure 1B). 22,23 In the first step, E1 catalyzes the formation of a thioester bond between the C-terminal glycine residue of ubiquitin and the cysteine residue in the active site of E1 in an ATPdependent manner. Then, the activated ubiquitin is transferred from E1 to E2.…”

Section: Ub I Qu Itin -Prote a Some Sys Temmentioning

confidence: 99%

The ubiquitin‐proteasome system in melanin metabolism

Shi

Guo

Xiao

et al. 2022

J of Cosmetic Dermatology

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Background The ubiquitin‐proteasome system (UPS) is a highly conserved way of regulating intracellular protein balance. UPS mediates proteolysis and disruption of variation or misfolding, while finely regulating proteins involved in differentiation and other biological processes. Aims The aim of this review is to systematically introduce UPS as a key regulator of melanin metabolism. Methods Systematic search and retrospective review were performed on the published data. Results Melanocyte‐inducing transcription factor (MITF) is a substrate of the ubiquitin ligase VCHL1 and acts as a transcription factor to regulate the expression of key enzymes in melanin synthesis such as tyrosinase (TYR). The rate‐limiting enzyme TYR is modified by the ubiquitin ligase Hrd1 during melanosynthesis. Melanin itself is also regulated by multiple ubiquitin ligases including Fbp1 and Vhl. By regulating the ubiquitination modification to target each link of melanin synthesis, it plays an important role in correcting the disorder of melanin metabolism. A number of chemical agents have been proven to inhibit the activity of ubiquitin ligase. Conclusions Drugs targeting E3 ligase and deubiquitinating enzymes have great potential in the treatment of melanin metabolism disorders.

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Section: Ub I Qu Itin -Prote a Some Sys Temmentioning

confidence: 99%

The ubiquitin‐proteasome system in melanin metabolism

Shi

Guo

Xiao

et al. 2022

J of Cosmetic Dermatology

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E3 ubiquitin ligase-dependent regulatory mechanism of TRIM family in carcinogenesis

Zhang,

Chen

et al. 2023

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<p style="text-align: justify;">Tripartite motif-containing (TRIM) proteins consist of over 80 proteins, the majority of which exhibit E3 ubiquitin ligase activity. E3 ligases have a critical role in various cellular processes by specifically recognizing and ubiquitinating substrate proteins to promote their proteasomal degradation or alter their activities. Numerous studies have indicated that TRIMs are involved in carcinogenesis through various mechanisms. However, the regulatory mechanisms delimitating TRIMs’ function as E3 ligases has not yet been specifically addressed in a previous review article. In this review, we focus on recent advancements in understanding how certain TRIMs function solely as E3 ligases during cancer cell proliferation, apoptosis, and metastasis. We comprehensively summarize the target proteins of TRIMs involved in disordered signaling pathways such as Wnt/β-catenin, PI3K/AKT, NF-κB, p53, ERK, and STAT3, as well as those regulating the cell cycle and glycolysis. Following ubiquitination modification by TRIM E3 ligases, these target proteins either undergo proteasome-mediating degradation, maintain steady levels, or get activated/inactivated. This review provides a foundation for the development of E3 ligase-based cancer treatments.</p>

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<em>In Vitro</em> Analysis of E3 Ubiquitin Ligase Function

Cited by 2 publications

References 0 publications

The ubiquitin‐proteasome system in melanin metabolism

The ubiquitin‐proteasome system in melanin metabolism

E3 ubiquitin ligase-dependent regulatory mechanism of TRIM family in carcinogenesis

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