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Cellular Function of TRIM E3 Ubiquitin Ligases in Health and...
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Cellular Function of TRIM E3 Ubiquitin Ligases in Health and Disease

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cellular Pathology".

Deadline for manuscript submissions: closed (31 March 2021) | Viewed by 33048

Special Issue Editors

Prof. Dr. Germana Meroni

E-Mail Website
Guest Editor
Department of Life Sciences, University of Trieste, Via L. Giorgieri, 5, 34127 Trieste, Italy
Interests: genetic diseases; TRIM E3 ubiquitin ligases; ubiquitination
Special Issues, Collections and Topics in MDPI journals
Dr. Solange Desagher

E-Mail Website
Guest Editor
Institute of Molecular Genetics of Montpellier, CNRS-University of Montpellier, 34293 Montpellier, France
Interests: neuronal apoptosis; Parkinson’s disease; TRIM E3 ubiquitin ligases; ubiquitin–proteasome system; SUMO

Special Issue Information

Dear Colleagues,

The field of the Tripartite Motif (TRIM) family has progressively attracted increasing interest during the last two decades. The presence of a distinctive amino-terminal module composed of a RING, B-box(es) and Coiled-coil domains was employed for the first time as a family back in 2001 and for the mining of novel, at that time unrecognized, family members. In the following years, several reports demonstrated that the shared TRIM proteins’ domain composition is associated with their involvement in the ubiquitination process. Indeed, TRIM proteins act as E3 ubiquitin ligases for the specific recognition of to-be-modified substrates. Notably, TRIM family members are implicated in many clinically relevant physiological processes and in various pathological conditions. Today, many efforts are directed toward the prospect of recognizing TRIM proteins/functions as therapeutic targets. To make this possible, it is time now to take a step forward, tackling the TRIM deep role in diverse cellular processes.

To set where we are in the field of cellular function of TRIM E3 ubiquitin ligase, we aim at collecting articles in this Special Issue of Cells, and we therefore invite your contributions, either in the form of original research articles or reviews, addressing this specific topic.

Prof. Dr. Germana Meroni
Dr. Solange Desagher
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cells is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • E3 ubiquitin ligases
  • Proteasome
  • SUMO
  • Autophagy
  • Cell cycle
  • Apoptosis
  • RNA binding
  • Viral restriction
  • Developmental syndromes
  • Cancer

Published Papers (9 papers)

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Editorial

Jump to: Research, Review

3 pages, 195 KiB  
Editorial
Cellular Function of TRIM E3 Ubiquitin Ligases in Health and Disease
by Germana Meroni and Solange Desagher
Cells 2022, 11(2), 250; https://0-doi-org.brum.beds.ac.uk/10.3390/cells11020250 - 12 Jan 2022
Cited by 11 | Viewed by 1414
Abstract
The field of the Tripartite Motif (TRIM) family has progressively attracted increasing interest during the last two decades [...] Full article
(This article belongs to the Special Issue Cellular Function of TRIM E3 Ubiquitin Ligases in Health and Disease)

Research

Jump to: Editorial, Review

18 pages, 12563 KiB  
Article
UBE2L3, a Partner of MuRF1/TRIM63, Is Involved in the Degradation of Myofibrillar Actin and Myosin
by Dulce Peris-Moreno, Mélodie Malige, Agnès Claustre, Andrea Armani, Cécile Coudy-Gandilhon, Christiane Deval, Daniel Béchet, Pierre Fafournoux, Marco Sandri, Lydie Combaret, Daniel Taillandier and Cécile Polge
Cells 2021, 10(8), 1974; https://0-doi-org.brum.beds.ac.uk/10.3390/cells10081974 - 03 Aug 2021
Cited by 9 | Viewed by 3353
Abstract
The ubiquitin proteasome system (UPS) is the main player of skeletal muscle wasting, a common characteristic of many diseases (cancer, etc.) that negatively impacts treatment and life prognosis. Within the UPS, the E3 ligase MuRF1/TRIM63 targets for degradation several myofibrillar proteins, including the [...] Read more.
The ubiquitin proteasome system (UPS) is the main player of skeletal muscle wasting, a common characteristic of many diseases (cancer, etc.) that negatively impacts treatment and life prognosis. Within the UPS, the E3 ligase MuRF1/TRIM63 targets for degradation several myofibrillar proteins, including the main contractile proteins alpha-actin and myosin heavy chain (MHC). We previously identified five E2 ubiquitin-conjugating enzymes interacting with MuRF1, including UBE2L3/UbcH7, that exhibited a high affinity for MuRF1 (KD = 50 nM). Here, we report a main effect of UBE2L3 on alpha-actin and MHC degradation in catabolic C2C12 myotubes. Consistently UBE2L3 knockdown in Tibialis anterior induced hypertrophy in dexamethasone (Dex)-treated mice, whereas overexpression worsened the muscle atrophy of Dex-treated mice. Using combined interactomic approaches, we also characterized the interactions between MuRF1 and its substrates alpha-actin and MHC and found that MuRF1 preferentially binds to filamentous F-actin (KD = 46.7 nM) over monomeric G-actin (KD = 450 nM). By contrast with actin that did not alter MuRF1–UBE2L3 affinity, binding of MHC to MuRF1 (KD = 8 nM) impeded UBE2L3 binding, suggesting that differential interactions prevail with MuRF1 depending on both the substrate and the E2. Our data suggest that UBE2L3 regulates contractile proteins levels and skeletal muscle atrophy. Full article
(This article belongs to the Special Issue Cellular Function of TRIM E3 Ubiquitin Ligases in Health and Disease)
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Review

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14 pages, 875 KiB  
Review
TRIM22. A Multitasking Antiviral Factor
by Isabel Pagani, Guido Poli and Elisa Vicenzi
Cells 2021, 10(8), 1864; https://0-doi-org.brum.beds.ac.uk/10.3390/cells10081864 - 23 Jul 2021
Cited by 19 | Viewed by 4219
Abstract
Viral invasion of target cells triggers an immediate intracellular host defense system aimed at preventing further propagation of the virus. Viral genomes or early products of viral replication are sensed by a number of pattern recognition receptors, leading to the synthesis and production [...] Read more.
Viral invasion of target cells triggers an immediate intracellular host defense system aimed at preventing further propagation of the virus. Viral genomes or early products of viral replication are sensed by a number of pattern recognition receptors, leading to the synthesis and production of type I interferons (IFNs) that, in turn, activate a cascade of IFN-stimulated genes (ISGs) with antiviral functions. Among these, several members of the tripartite motif (TRIM) family are antiviral executors. This article will focus, in particular, on TRIM22 as an example of a multitarget antiviral member of the TRIM family. The antiviral activities of TRIM22 against different DNA and RNA viruses, particularly human immunodeficiency virus type 1 (HIV-1) and influenza A virus (IAV), will be discussed. TRIM22 restriction of virus replication can involve either direct interaction of TRIM22 E3 ubiquitin ligase activity with viral proteins, or indirect protein–protein interactions resulting in control of viral gene transcription, but also epigenetic effects exerted at the chromatin level. Full article
(This article belongs to the Special Issue Cellular Function of TRIM E3 Ubiquitin Ligases in Health and Disease)
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19 pages, 1657 KiB  
Review
TRIMming Down Hormone-Driven Cancers: The Biological Impact of TRIM Proteins on Tumor Development, Progression and Prognostication
by Eleonora Pauletto, Nils Eickhoff, Nuno A. Padrão, Christine Blattner and Wilbert Zwart
Cells 2021, 10(6), 1517; https://0-doi-org.brum.beds.ac.uk/10.3390/cells10061517 - 16 Jun 2021
Cited by 11 | Viewed by 3134
Abstract
The tripartite motif (TRIM) protein family is attracting increasing interest in oncology. As a protein family based on structure rather than function, a plethora of biological activities are described for TRIM proteins, which are implicated in multiple diseases including cancer. With hormone-driven cancers [...] Read more.
The tripartite motif (TRIM) protein family is attracting increasing interest in oncology. As a protein family based on structure rather than function, a plethora of biological activities are described for TRIM proteins, which are implicated in multiple diseases including cancer. With hormone-driven cancers being among the leading causes of cancer-related death, TRIM proteins have been described to portrait tumor suppressive or oncogenic activities in these tumor types. This review describes the biological impact of TRIM proteins in relation to hormone receptor biology, as well as hormone-independent mechanisms that contribute to tumor cell biology in prostate, breast, ovarian and endometrial cancer. Furthermore, we point out common functions of TRIM proteins throughout the group of hormone-driven cancers. An improved understanding of the biological impact of TRIM proteins in cancer may pave the way for improved prognostication and novel therapeutics, ultimately improving cancer care for patients with hormone-driven cancers. Full article
(This article belongs to the Special Issue Cellular Function of TRIM E3 Ubiquitin Ligases in Health and Disease)
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28 pages, 2758 KiB  
Review
To Ubiquitinate or Not to Ubiquitinate: TRIM17 in Cell Life and Death
by Meenakshi Basu-Shrivastava, Alina Kozoriz, Solange Desagher and Iréna Lassot
Cells 2021, 10(5), 1235; https://0-doi-org.brum.beds.ac.uk/10.3390/cells10051235 - 18 May 2021
Cited by 7 | Viewed by 3145
Abstract
TRIM17 is a member of the TRIM family, a large class of RING-containing E3 ubiquitin-ligases. It is expressed at low levels in adult tissues, except in testis and in some brain regions. However, it can be highly induced in stress conditions which makes [...] Read more.
TRIM17 is a member of the TRIM family, a large class of RING-containing E3 ubiquitin-ligases. It is expressed at low levels in adult tissues, except in testis and in some brain regions. However, it can be highly induced in stress conditions which makes it a putative stress sensor required for the triggering of key cellular responses. As most TRIM members, TRIM17 can act as an E3 ubiquitin-ligase and promote the degradation by the proteasome of substrates such as the antiapoptotic protein MCL1. Intriguingly, TRIM17 can also prevent the ubiquitination of other proteins and stabilize them, by binding to other TRIM proteins and inhibiting their E3 ubiquitin-ligase activity. This duality of action confers several pivotal roles to TRIM17 in crucial cellular processes such as apoptosis, autophagy or cell division, but also in pathological conditions as diverse as Parkinson’s disease or cancer. Here, in addition to recent data that endorse this duality, we review what is currently known from public databases and the literature about TRIM17 gene regulation and expression, TRIM17 protein structure and interactions, as well as its involvement in cell physiology and human disorders. Full article
(This article belongs to the Special Issue Cellular Function of TRIM E3 Ubiquitin Ligases in Health and Disease)
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14 pages, 1706 KiB  
Review
Ubiquitination, Biotech Startups, and the Future of TRIM Family Proteins: A TRIM-Endous Opportunity
by Utsa Bhaduri and Giuseppe Merla
Cells 2021, 10(5), 1015; https://0-doi-org.brum.beds.ac.uk/10.3390/cells10051015 - 25 Apr 2021
Cited by 14 | Viewed by 4920
Abstract
Ubiquitination is a post-translational modification that has pivotal roles in protein degradation and diversified cellular processes, and for more than two decades it has been a subject of interest in the biotech or biopharmaceutical industry. Tripartite motif (TRIM) family proteins are known to [...] Read more.
Ubiquitination is a post-translational modification that has pivotal roles in protein degradation and diversified cellular processes, and for more than two decades it has been a subject of interest in the biotech or biopharmaceutical industry. Tripartite motif (TRIM) family proteins are known to have proven E3 ubiquitin ligase activities and are involved in a multitude of cellular and physiological events and pathophysiological conditions ranging from cancers to rare genetic disorders. Although in recent years many kinds of E3 ubiquitin ligases have emerged as the preferred choices of big pharma and biotech startups in the context of protein degradation and disease biology, from a surface overview it appears that TRIM E3 ubiquitin ligases are not very well recognized yet in the realm of drug discovery. This article will review some of the blockbuster scientific discoveries and technological innovations from the world of ubiquitination and E3 ubiquitin ligases that have impacted the biopharma community, from biotech colossuses to startups, and will attempt to evaluate the future of TRIM family proteins in the province of E3 ubiquitin ligase-based drug discovery. Full article
(This article belongs to the Special Issue Cellular Function of TRIM E3 Ubiquitin Ligases in Health and Disease)
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21 pages, 4638 KiB  
Review
TRIM32 and Malin in Neurological and Neuromuscular Rare Diseases
by Lorena Kumarasinghe, Lu Xiong, Maria Adelaida Garcia-Gimeno, Elisa Lazzari, Pascual Sanz and Germana Meroni
Cells 2021, 10(4), 820; https://0-doi-org.brum.beds.ac.uk/10.3390/cells10040820 - 06 Apr 2021
Cited by 10 | Viewed by 3404
Abstract
Tripartite motif (TRIM) proteins are RING E3 ubiquitin ligases defined by a shared domain structure. Several of them are implicated in rare genetic diseases, and mutations in TRIM32 and TRIM-like malin are associated with Limb-Girdle Muscular Dystrophy R8 and Lafora disease, respectively. These [...] Read more.
Tripartite motif (TRIM) proteins are RING E3 ubiquitin ligases defined by a shared domain structure. Several of them are implicated in rare genetic diseases, and mutations in TRIM32 and TRIM-like malin are associated with Limb-Girdle Muscular Dystrophy R8 and Lafora disease, respectively. These two proteins are evolutionary related, share a common ancestor, and both display NHL repeats at their C-terminus. Here, we revmniew the function of these two related E3 ubiquitin ligases discussing their intrinsic and possible common pathophysiological pathways. Full article
(This article belongs to the Special Issue Cellular Function of TRIM E3 Ubiquitin Ligases in Health and Disease)
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Graphical abstract

15 pages, 1618 KiB  
Review
Emerging Roles of TRIM8 in Health and Disease
by Flaviana Marzano, Luisa Guerrini, Graziano Pesole, Elisabetta Sbisà and Apollonia Tullo
Cells 2021, 10(3), 561; https://0-doi-org.brum.beds.ac.uk/10.3390/cells10030561 - 05 Mar 2021
Cited by 20 | Viewed by 3504
Abstract
The superfamily of TRIM (TRIpartite Motif-containing) proteins is one of the largest groups of E3 ubiquitin ligases. Among them, interest in TRIM8 has greatly increased in recent years. In this review, we analyze the regulation of TRIM8 gene expression and how it is [...] Read more.
The superfamily of TRIM (TRIpartite Motif-containing) proteins is one of the largest groups of E3 ubiquitin ligases. Among them, interest in TRIM8 has greatly increased in recent years. In this review, we analyze the regulation of TRIM8 gene expression and how it is involved in many cell reactions in response to different stimuli such as genotoxic stress and attacks by viruses or bacteria, playing a central role in the immune response and orchestrating various fundamental biological processes such as cell survival, carcinogenesis, autophagy, apoptosis, differentiation and inflammation. Moreover, we show how TRIM8 functions are not limited to ubiquitination, and contrasting data highlight its role either as an oncogene or as a tumor suppressor gene, acting as a “double-edged weapon”. This is linked to its involvement in the selective regulation of three pivotal cellular signaling pathways: the p53 tumor suppressor, NF-κB and JAK-STAT pathways. Lastly, we describe how TRIM8 dysfunctions are linked to inflammatory processes, autoimmune disorders, rare developmental and cardiovascular diseases, ischemia, intellectual disability and cancer. Full article
(This article belongs to the Special Issue Cellular Function of TRIM E3 Ubiquitin Ligases in Health and Disease)
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14 pages, 5672 KiB  
Review
MG53, A Tissue Repair Protein with Broad Applications in Regenerative Medicine
by Zhongguang Li, Liyang Wang, Huimin Yue, Bryan A. Whitson, Erin Haggard, Xuehong Xu and Jianjie Ma
Cells 2021, 10(1), 122; https://0-doi-org.brum.beds.ac.uk/10.3390/cells10010122 - 11 Jan 2021
Cited by 23 | Viewed by 3965
Abstract
Under natural conditions, injured cells can be repaired rapidly through inherent biological processes. However, in the case of diabetes, cardiovascular disease, muscular dystrophy, and other degenerative conditions, the natural repair process is impaired. Repair of injury to the cell membrane is an important [...] Read more.
Under natural conditions, injured cells can be repaired rapidly through inherent biological processes. However, in the case of diabetes, cardiovascular disease, muscular dystrophy, and other degenerative conditions, the natural repair process is impaired. Repair of injury to the cell membrane is an important aspect of physiology. Inadequate membrane repair function is implicated in the pathophysiology of many human disorders. Recent studies show that Mitsugumin 53 (MG53), a TRIM family protein, plays a key role in repairing cell membrane damage and facilitating tissue regeneration. Clarifying the role of MG53 and its molecular mechanism are important for the application of MG53 in regenerative medicine. In this review, we analyze current research dissecting MG53′s function in cell membrane repair and tissue regeneration, and highlight the development of recombinant human MG53 protein as a potential therapeutic agent to repair multiple-organ injuries. Full article
(This article belongs to the Special Issue Cellular Function of TRIM E3 Ubiquitin Ligases in Health and Disease)
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