A No-Brainer! The Therapeutic Potential of TRIM Proteins in Viral and Central Nervous System Diseases

Tripartite motif (TRIM) proteins comprise an important class of E3 ubiquitin ligases that regulate numerous biological processes including protein expression, cellular signaling pathways, and innate immunity. This ubiquitous participation in fundamental aspects of biology has made TRIM proteins a fo...

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Published inViruses Vol. 17; no. 4; p. 562
Main Authors Hage, Adam, Janes, Mikhaila, Best, Sonja M.
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 14.04.2025
MDPI
Subjects
Animals
Apoptosis
Autophagy
Care and treatment
Central nervous system
Central nervous system diseases
Central Nervous System Diseases - drug therapy
Central Nervous System Diseases - therapy
CNS diseases
CRISPR
Disease
Drug development
E3 ubiquitin ligase
Enzymes
Genomes
Health aspects
Humans
Immunity (Disease)
Immunity, Innate
Innate immunity
Ligases
Medical research
Medicine, Experimental
Nervous system
Neurodegenerative diseases
Neurosciences
Pathogens
Physiological aspects
PROTAC
protein degradation
Proteins
Review
Signal Transduction
tripartite motif (TRIM)
Tripartite Motif Proteins - genetics
Tripartite Motif Proteins - metabolism
Tripartite Motif Proteins - therapeutic use
Ubiquitin
Ubiquitin-Protein Ligases - metabolism
Viral infections
Virus diseases
Virus Diseases - drug therapy
Viruses
West Nile virus
United States
disease therapeutic
innate immunity
PROTAC
CNS diseases
trim-away
tripartite motif (TRIM)
E3 ubiquitin ligase
protein degradation
ubiquitin
virus infection
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Abstract Tripartite motif (TRIM) proteins comprise an important class of E3 ubiquitin ligases that regulate numerous biological processes including protein expression, cellular signaling pathways, and innate immunity. This ubiquitous participation in fundamental aspects of biology has made TRIM proteins a focus of study in many fields and has illuminated the negative impact they exert when functioning improperly. Disruption of TRIM function has been linked to the success of various pathogens and separately to the occurrence and development of several neurodegenerative diseases, making TRIM proteins an appealing candidate to study for novel therapeutic approaches. Here, we review the current findings on TRIM proteins that demonstrate their analogous properties in the distinct fields of viral infection and central nervous system (CNS) disorders. We also examine recent advancements in drug development and targeted protein degradation as potential strategies for TRIM-mediated therapeutic treatments and discuss the implications these technologies have on future research directions.
AbstractList Tripartite motif (TRIM) proteins comprise an important class of E3 ubiquitin ligases that regulate numerous biological processes including protein expression, cellular signaling pathways, and innate immunity. This ubiquitous participation in fundamental aspects of biology has made TRIM proteins a focus of study in many fields and has illuminated the negative impact they exert when functioning improperly. Disruption of TRIM function has been linked to the success of various pathogens and separately to the occurrence and development of several neurodegenerative diseases, making TRIM proteins an appealing candidate to study for novel therapeutic approaches. Here, we review the current findings on TRIM proteins that demonstrate their analogous properties in the distinct fields of viral infection and central nervous system (CNS) disorders. We also examine recent advancements in drug development and targeted protein degradation as potential strategies for TRIM-mediated therapeutic treatments and discuss the implications these technologies have on future research directions.
Tripartite motif (TRIM) proteins comprise an important class of E3 ubiquitin ligases that regulate numerous biological processes including protein expression, cellular signaling pathways, and innate immunity. This ubiquitous participation in fundamental aspects of biology has made TRIM proteins a focus of study in many fields and has illuminated the negative impact they exert when functioning improperly. Disruption of TRIM function has been linked to the success of various pathogens and separately to the occurrence and development of several neurodegenerative diseases, making TRIM proteins an appealing candidate to study for novel therapeutic approaches. Here, we review the current findings on TRIM proteins that demonstrate their analogous properties in the distinct fields of viral infection and central nervous system (CNS) disorders. We also examine recent advancements in drug development and targeted protein degradation as potential strategies for TRIM-mediated therapeutic treatments and discuss the implications these technologies have on future research directions.Tripartite motif (TRIM) proteins comprise an important class of E3 ubiquitin ligases that regulate numerous biological processes including protein expression, cellular signaling pathways, and innate immunity. This ubiquitous participation in fundamental aspects of biology has made TRIM proteins a focus of study in many fields and has illuminated the negative impact they exert when functioning improperly. Disruption of TRIM function has been linked to the success of various pathogens and separately to the occurrence and development of several neurodegenerative diseases, making TRIM proteins an appealing candidate to study for novel therapeutic approaches. Here, we review the current findings on TRIM proteins that demonstrate their analogous properties in the distinct fields of viral infection and central nervous system (CNS) disorders. We also examine recent advancements in drug development and targeted protein degradation as potential strategies for TRIM-mediated therapeutic treatments and discuss the implications these technologies have on future research directions.
Audience Academic
Author Hage, Adam
Janes, Mikhaila
Best, Sonja M.
AuthorAffiliation Innate Immunity and Pathogenesis Section, Laboratory of Neurological Infections and Immunity, Division of Intramural Research, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA; mikhaila.janes@nih.gov (M.J.); sbest@niaid.nih.gov (S.M.B.)
AuthorAffiliation_xml – name: Innate Immunity and Pathogenesis Section, Laboratory of Neurological Infections and Immunity, Division of Intramural Research, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA; mikhaila.janes@nih.gov (M.J.); sbest@niaid.nih.gov (S.M.B.)
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Issue 4
Keywords disease therapeutic
innate immunity
PROTAC
CNS diseases
trim-away
tripartite motif (TRIM)
E3 ubiquitin ligase
protein degradation
ubiquitin
virus infection
Language English
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Snippet Tripartite motif (TRIM) proteins comprise an important class of E3 ubiquitin ligases that regulate numerous biological processes including protein expression,...
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StartPage 562
SubjectTerms Animals
Apoptosis
Autophagy
Care and treatment
Central nervous system
Central nervous system diseases
Central Nervous System Diseases - drug therapy
Central Nervous System Diseases - therapy
CNS diseases
CRISPR
Disease
Drug development
E3 ubiquitin ligase
Enzymes
Genomes
Health aspects
Humans
Immunity (Disease)
Immunity, Innate
Innate immunity
Ligases
Medical research
Medicine, Experimental
Nervous system
Neurodegenerative diseases
Neurosciences
Pathogens
Physiological aspects
PROTAC
protein degradation
Proteins
Review
Signal Transduction
tripartite motif (TRIM)
Tripartite Motif Proteins - genetics
Tripartite Motif Proteins - metabolism
Tripartite Motif Proteins - therapeutic use
Ubiquitin
Ubiquitin-Protein Ligases - metabolism
Viral infections
Virus diseases
Virus Diseases - drug therapy
Viruses
West Nile virus
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Title A No-Brainer! The Therapeutic Potential of TRIM Proteins in Viral and Central Nervous System Diseases
URI https://www.ncbi.nlm.nih.gov/pubmed/40285004
https://www.proquest.com/docview/3194648557
https://www.proquest.com/docview/3195784518
https://pubmed.ncbi.nlm.nih.gov/PMC12031127
https://doaj.org/article/5b4b63ad1b8e4615b2df6b28dc9fda5e
Volume 17
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