The UFM1 system: Working principles, cellular functions, and pathophysiology

Komatsu, Masaaki; Inada, Toshifumi; Noda, Nobuo N.

doi:10.1016/j.molcel.2023.11.034

Cited by 6 publications

(2 citation statements)

References 103 publications

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“…UFMylation has predominantly been linked to roles in endoplasmic reticulum (ER) homeostasis, fatty acid metabolism, autophagy, neurodevelopment, and liver development [ 263 , 264 , 267 , 268 ]. A major substrate for UFMylation is the 60S ribosomal subunit RPL26, which occurs on stalled ribosomes at the ER.…”

Section: Ulps In Genome Stabilitymentioning

confidence: 99%

DoUBLing up: ubiquitin and ubiquitin-like proteases in genome stability

Foster,

Wang,

Schmidt

2024

Biochemical Journal

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Maintaining stability of the genome requires dedicated DNA repair and signalling processes that are essential for the faithful duplication and propagation of chromosomes. These DNA damage response (DDR) mechanisms counteract the potentially mutagenic impact of daily genotoxic stresses from both exogenous and endogenous sources. Inherent to these DNA repair pathways is the activity of protein factors that instigate repair processes in response to DNA lesions. The regulation, coordination, and orchestration of these DDR factors is carried out, in a large part, by post-translational modifications, such as phosphorylation, ubiquitylation, and modification with ubiquitin-like proteins (UBLs). The importance of ubiquitylation and UBLylation with SUMO in DNA repair is well established, with the modified targets and downstream signalling consequences relatively well characterised. However, the role of dedicated erasers for ubiquitin and UBLs, known as deubiquitylases (DUBs) and ubiquitin-like proteases (ULPs) respectively, in genome stability is less well established, particularly for emerging UBLs such as ISG15 and UFM1. In this review, we provide an overview of the known regulatory roles and mechanisms of DUBs and ULPs involved in genome stability pathways. Expanding our understanding of the molecular agents and mechanisms underlying the removal of ubiquitin and UBL modifications will be fundamental for progressing our knowledge of the DDR and likely provide new therapeutic avenues for relevant human diseases, such as cancer.

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Section: Ulps In Genome Stabilitymentioning

confidence: 99%

DoUBLing up: ubiquitin and ubiquitin-like proteases in genome stability

Foster,

Wang,

Schmidt

2024

Biochemical Journal

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“…UFMylation, a post-translational modification akin to ubiquitination, plays a crucial role in various biological functions, with its dysregulation linked to several human diseases, including cancer ( 141 , 142 ). Mice lacking the UFMylation E3 ligase UFL1 specifically in T cells demonstrated superior tumor suppression.…”

Section: Pd-1 and Pd-l1 Are Regulated By Ptmsmentioning

confidence: 99%

PTMs of PD-1/PD-L1 and PROTACs application for improving cancer immunotherapy

Ren,

Wang,

Liu

et al. 2024

Front. Immunol.

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Immunotherapy has been developed, which harnesses and enhances the innate powers of the immune system to fight disease, particularly cancer. PD-1 (programmed death-1) and PD-L1 (programmed death ligand-1) are key components in the regulation of the immune system, particularly in the context of cancer immunotherapy. PD-1 and PD-L1 are regulated by PTMs, including phosphorylation, ubiquitination, deubiquitination, acetylation, palmitoylation and glycosylation. PROTACs (Proteolysis Targeting Chimeras) are a type of new drug design technology. They are specifically engineered molecules that target specific proteins within a cell for degradation. PROTACs have been designed and demonstrated their inhibitory activity against the PD-1/PD-L1 pathway, and showed their ability to degrade PD-1/PD-L1 proteins. In this review, we describe how PROTACs target PD-1 and PD-L1 proteins to improve the efficacy of immunotherapy. PROTACs could be a novel strategy to combine with radiotherapy, chemotherapy and immunotherapy for cancer patients.

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UFMylation: An integral post-translational modification for the regulation of proteostasis and cellular functions

Wang,

Lv,

et al. 2024

Pharmacology & Therapeutics

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The UFM1 system: Working principles, cellular functions, and pathophysiology

Cited by 6 publications

References 103 publications

DoUBLing up: ubiquitin and ubiquitin-like proteases in genome stability

DoUBLing up: ubiquitin and ubiquitin-like proteases in genome stability

PTMs of PD-1/PD-L1 and PROTACs application for improving cancer immunotherapy

UFMylation: An integral post-translational modification for the regulation of proteostasis and cellular functions

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