Deubiquitinase USP33 is negatively regulated by β-TrCP through ubiquitin-dependent proteolysis

Cheng, Qiao; Yuan, Yukang; Li, Lemin; Guo, Tingting; Miao, Ying; Ren, Ying; Liu, Jin; Feng, Qian; Wang, Xiaofang; Zhao, Peng; Zuo, Yibo; Qian, Liping; Zhang, Liting; Zheng, Hui

doi:10.1016/j.yexcr.2017.05.011

Cited by 4 publications

(1 citation statement)

References 20 publications

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“…For example, although CDC25A, CDC25B, and CReP are ubiquitinated and degraded by β‐TrCP, their degrons are not phosphorylated (Kanemori et al, 2005; Loveless et al, 2015). In addition, β‐TrCP‐mediated USP33 proteasomal degradation is independent of the classical β‐TrCP‐binding motif (Cheng et al, 2017). These nonclassical degradation targets have no consensus motifs known to date.…”

Section: Discussionmentioning

confidence: 99%

Novel targets of β‐TrCP cooperatively accelerate carbohydrate and fatty acid consumption

Joo

D'Alessandro

et al. 2023

Journal Cellular Physiology

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Cellular energy is primarily produced from glucose and fat through glycolysis and fatty acid oxidation (FAO) followed by the tricarboxylic acid cycle in mitochondria; energy homeostasis is carefully maintained via numerous feedback pathways. In this report, we uncovered a new master regulator of carbohydrate and lipid metabolism. When ubiquitin E3 ligase β‐TrCP2 was inducibly knocked out in β‐TrCP1 knockout adult mice, the resulting double knockout mice (DKO) lost fat mass rapidly. Biochemical analyses of the tissues and cells from β‐TrCP2 KO and DKO mice revealed that glycolysis, FAO, and lipolysis were dramatically upregulated. The absence of β‐TrCP2 increased the protein stability of metabolic rate‐limiting enzymes including 6‐phosphofructo‐2‐kinase/fructose‐2,6‐bisphosphatase (PFKFB3), adipose triglyceride lipase (ATGL), carnitine palmitoyltransferase 1A (CPT1A), and carnitine/acylcarnitine translocase (CACT). Our data suggest that β‐TrCP is a potential regulator for total energy homeostasis by simultaneously controlling glucose and fatty acid metabolism and that targeting β‐TrCP could be an effective strategy to treat obesity and other metabolic disorders.

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Section: Discussionmentioning

confidence: 99%

Novel targets of β‐TrCP cooperatively accelerate carbohydrate and fatty acid consumption

Joo

D'Alessandro

et al. 2023

Journal Cellular Physiology

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Coupling Conjugation and Deconjugation Activities to Achieve Cellular Ubiquitin Dynamics

Nielsen

MacGurn

2020

Trends in Biochemical Sciences

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Friend or foe? Reciprocal regulation between E3 ubiquitin ligases and deubiquitinases

Bolhuis,

Emanuele,

Brown

2024

Biochemical Society Transactions

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Protein ubiquitination is a post-translational modification that entails the covalent attachment of the small protein ubiquitin (Ub), which acts as a signal to direct protein stability, localization, or interactions. The Ub code is written by a family of enzymes called E3 Ub ligases (∼600 members in humans), which can catalyze the transfer of either a single ubiquitin or the formation of a diverse array of polyubiquitin chains. This code can be edited or erased by a different set of enzymes termed deubiquitinases (DUBs; ∼100 members in humans). While enzymes from these distinct families have seemingly opposing activities, certain E3–DUB pairings can also synergize to regulate vital cellular processes like gene expression, autophagy, innate immunity, and cell proliferation. In this review, we highlight recent studies describing Ub ligase-DUB interactions and focus on their relationships.

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Deubiquitinase USP33 is negatively regulated by β-TrCP through ubiquitin-dependent proteolysis

Cited by 4 publications

References 20 publications

Novel targets of β‐TrCP cooperatively accelerate carbohydrate and fatty acid consumption

Novel targets of β‐TrCP cooperatively accelerate carbohydrate and fatty acid consumption

Coupling Conjugation and Deconjugation Activities to Achieve Cellular Ubiquitin Dynamics

Friend or foe? Reciprocal regulation between E3 ubiquitin ligases and deubiquitinases

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