Ubiquitin-like modification dependent proteasomal degradation and disease therapy

Many proteins have been identified subject to ubiquitin (Ub)-independent proteasome degradation (UbIPD), a process mediated by Ub-like (UBL) proteins.UBL-conjugates can be processed by 19S proteasomes by mechanisms different from Ub-conjugates and by proteasome activator 28γ, which was previously th...

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Veröffentlicht in:Trends in molecular medicine Jg. 30; H. 11; S. 1061 - 1075
Hauptverfasser: Wang, Tiantian, Jiang, Jie, Zhang, Xue, Ke, Xisong, Qu, Yi
Format: Journal Article
Sprache:Englisch
Veröffentlicht: England Elsevier Ltd 01.11.2024
Schlagworte:
Animals
Humans
muscle wasting diseases
neurodegenerative diseases
Neurodegenerative Diseases - drug therapy
Neurodegenerative Diseases - metabolism
proteasomal degradation
Proteasome Endopeptidase Complex - metabolism
proteasome regulators
Protein Processing, Post-Translational
Proteolysis - drug effects
ubiquitin-like modification
ubiquitin-like proteasome system
Ubiquitination - drug effects
Ubiquitins - metabolism
neurodegenerative diseases
proteasome regulators
ubiquitin-like modification
proteasomal degradation
ubiquitin-like proteasome system
muscle wasting diseases
ISSN:1471-4914, 1471-499X, 1471-499X
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Abstract Many proteins have been identified subject to ubiquitin (Ub)-independent proteasome degradation (UbIPD), a process mediated by Ub-like (UBL) proteins.UBL-conjugates can be processed by 19S proteasomes by mechanisms different from Ub-conjugates and by proteasome activator 28γ, which was previously thought to work as an activator of UbIPD.Ub and UBLs coordinate proteasome degradation to maintain protein homeostasis.UBL proteins, enzymes and modification substrates are tightly associated with proteostasis in muscle and neurodegenerative diseases. Although it is believed that ubiquitin (Ub) modification is required for protein degradation in the proteasome system (UPS), several proteins are subject to Ub-independent proteasome degradation, and in many cases ubiquitin-like (UBL) modifications, including neddylation, FAT10ylation, SUMOylation, ISGylation, and urmylation, are essential instead. In this Review, we focus on UBL-dependent proteasome degradation (UBLPD), on proteasome regulators especially shuttle factors and receptors, as well as potential competition and coordination with UPS. We propose that there is a distinct UBL–proteasome system (UBLPS) that might be underestimated in protein degradation. Finally, we investigate the association of UBLPD with muscle wasting and neurodegenerative diseases in which the proteasome is abnormally activated and impaired, respectively, and suggest strategies to modulate UBLPD for disease therapy. Although it is believed that ubiquitin (Ub) modification is required for protein degradation in the proteasome system (UPS), several proteins are subject to Ub-independent proteasome degradation, and in many cases ubiquitin-like (UBL) modifications, including neddylation, FAT10ylation, SUMOylation, ISGylation, and urmylation, are essential instead. In this Review, we focus on UBL-dependent proteasome degradation (UBLPD), on proteasome regulators especially shuttle factors and receptors, as well as potential competition and coordination with UPS. We propose that there is a distinct UBL–proteasome system (UBLPS) that might be underestimated in protein degradation. Finally, we investigate the association of UBLPD with muscle wasting and neurodegenerative diseases in which the proteasome is abnormally activated and impaired, respectively, and suggest strategies to modulate UBLPD for disease therapy.
AbstractList Many proteins have been identified subject to ubiquitin (Ub)-independent proteasome degradation (UbIPD), a process mediated by Ub-like (UBL) proteins.UBL-conjugates can be processed by 19S proteasomes by mechanisms different from Ub-conjugates and by proteasome activator 28γ, which was previously thought to work as an activator of UbIPD.Ub and UBLs coordinate proteasome degradation to maintain protein homeostasis.UBL proteins, enzymes and modification substrates are tightly associated with proteostasis in muscle and neurodegenerative diseases. Although it is believed that ubiquitin (Ub) modification is required for protein degradation in the proteasome system (UPS), several proteins are subject to Ub-independent proteasome degradation, and in many cases ubiquitin-like (UBL) modifications, including neddylation, FAT10ylation, SUMOylation, ISGylation, and urmylation, are essential instead. In this Review, we focus on UBL-dependent proteasome degradation (UBLPD), on proteasome regulators especially shuttle factors and receptors, as well as potential competition and coordination with UPS. We propose that there is a distinct UBL–proteasome system (UBLPS) that might be underestimated in protein degradation. Finally, we investigate the association of UBLPD with muscle wasting and neurodegenerative diseases in which the proteasome is abnormally activated and impaired, respectively, and suggest strategies to modulate UBLPD for disease therapy. Although it is believed that ubiquitin (Ub) modification is required for protein degradation in the proteasome system (UPS), several proteins are subject to Ub-independent proteasome degradation, and in many cases ubiquitin-like (UBL) modifications, including neddylation, FAT10ylation, SUMOylation, ISGylation, and urmylation, are essential instead. In this Review, we focus on UBL-dependent proteasome degradation (UBLPD), on proteasome regulators especially shuttle factors and receptors, as well as potential competition and coordination with UPS. We propose that there is a distinct UBL–proteasome system (UBLPS) that might be underestimated in protein degradation. Finally, we investigate the association of UBLPD with muscle wasting and neurodegenerative diseases in which the proteasome is abnormally activated and impaired, respectively, and suggest strategies to modulate UBLPD for disease therapy.
Although it is believed that ubiquitin (Ub) modification is required for protein degradation in the proteasome system (UPS), several proteins are subject to Ub-independent proteasome degradation, and in many cases ubiquitin-like (UBL) modifications, including neddylation, FAT10ylation, SUMOylation, ISGylation, and urmylation, are essential instead. In this Review, we focus on UBL-dependent proteasome degradation (UBLPD), on proteasome regulators especially shuttle factors and receptors, as well as potential competition and coordination with UPS. We propose that there is a distinct UBL-proteasome system (UBLPS) that might be underestimated in protein degradation. Finally, we investigate the association of UBLPD with muscle wasting and neurodegenerative diseases in which the proteasome is abnormally activated and impaired, respectively, and suggest strategies to modulate UBLPD for disease therapy.
Although it is believed that ubiquitin (Ub) modification is required for protein degradation in the proteasome system (UPS), several proteins are subject to Ub-independent proteasome degradation, and in many cases ubiquitin-like (UBL) modifications, including neddylation, FAT10ylation, SUMOylation, ISGylation, and urmylation, are essential instead. In this Review, we focus on UBL-dependent proteasome degradation (UBLPD), on proteasome regulators especially shuttle factors and receptors, as well as potential competition and coordination with UPS. We propose that there is a distinct UBL-proteasome system (UBLPS) that might be underestimated in protein degradation. Finally, we investigate the association of UBLPD with muscle wasting and neurodegenerative diseases in which the proteasome is abnormally activated and impaired, respectively, and suggest strategies to modulate UBLPD for disease therapy.Although it is believed that ubiquitin (Ub) modification is required for protein degradation in the proteasome system (UPS), several proteins are subject to Ub-independent proteasome degradation, and in many cases ubiquitin-like (UBL) modifications, including neddylation, FAT10ylation, SUMOylation, ISGylation, and urmylation, are essential instead. In this Review, we focus on UBL-dependent proteasome degradation (UBLPD), on proteasome regulators especially shuttle factors and receptors, as well as potential competition and coordination with UPS. We propose that there is a distinct UBL-proteasome system (UBLPS) that might be underestimated in protein degradation. Finally, we investigate the association of UBLPD with muscle wasting and neurodegenerative diseases in which the proteasome is abnormally activated and impaired, respectively, and suggest strategies to modulate UBLPD for disease therapy.
Author Ke, Xisong
Zhang, Xue
Qu, Yi
Wang, Tiantian
Jiang, Jie
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  surname: Jiang
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  givenname: Xue
  surname: Zhang
  fullname: Zhang, Xue
  organization: Center for Chemical Biology, Institute of Interdisciplinary Integrative Medicine Research, Shanghai University of Traditional Chinese Medicine, Shanghai, China
– sequence: 4
  givenname: Xisong
  surname: Ke
  fullname: Ke, Xisong
  email: xisongke@shutcm.edu.cn
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  givenname: Yi
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Issue 11
Keywords neurodegenerative diseases
proteasome regulators
ubiquitin-like modification
proteasomal degradation
ubiquitin-like proteasome system
muscle wasting diseases
Language English
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Snippet Many proteins have been identified subject to ubiquitin (Ub)-independent proteasome degradation (UbIPD), a process mediated by Ub-like (UBL)...
Although it is believed that ubiquitin (Ub) modification is required for protein degradation in the proteasome system (UPS), several proteins are subject to...
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SubjectTerms Animals
Humans
muscle wasting diseases
neurodegenerative diseases
Neurodegenerative Diseases - drug therapy
Neurodegenerative Diseases - metabolism
proteasomal degradation
Proteasome Endopeptidase Complex - metabolism
proteasome regulators
Protein Processing, Post-Translational
Proteolysis - drug effects
ubiquitin-like modification
ubiquitin-like proteasome system
Ubiquitination - drug effects
Ubiquitins - metabolism
Title Ubiquitin-like modification dependent proteasomal degradation and disease therapy
URI https://www.clinicalkey.com/#!/content/1-s2.0-S1471491424001278
https://dx.doi.org/10.1016/j.molmed.2024.05.005
https://www.ncbi.nlm.nih.gov/pubmed/38851992
https://www.proquest.com/docview/3065982346
Volume 30
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