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Autore: Grafiati

Pubblicato: 15 giugno 2024

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1

Hipp, Mark Steffen, Birte Kalveram, Shahri Raasi, Marcus Groettrup e Gunter Schmidtke. "FAT10, a Ubiquitin-Independent Signal for Proteasomal Degradation". Molecular and Cellular Biology 25, n. 9 (1 maggio 2005): 3483–91. http://dx.doi.org/10.1128/mcb.25.9.3483-3491.2005.

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ABSTRACT FAT10 is a small ubiquitin-like modifier that is encoded in the major histocompatibility complex and is synergistically inducible by tumor necrosis factor alpha and gamma interferon. It is composed of two ubiquitin-like domains and possesses a free C-terminal diglycine motif that is required for the formation of FAT10 conjugates. Here we show that unconjugated FAT10 and a FAT10 conjugate were rapidly degraded by the proteasome at a similar rate. Fusion of FAT10 to the N terminus of very long-lived proteins enhanced their degradation rate as potently as fusion with ubiquitin did. FAT10-green fluorescent protein fusion proteins were not cleaved but entirely degraded, suggesting that FAT10-specific deconjugating enzymes were not present in the analyzed cell lines. Interestingly, the prevention of ubiquitylation of FAT10 by mutation of all lysines or by expression in ubiquitylation-deficient cells did not affect FAT10 degradation. Thus, conjugation with FAT10 is an alternative and ubiquitin-independent targeting mechanism for degradation by the proteasome, which, in contrast to polyubiquitylation, is cytokine inducible and irreversible.

2

Schnell, Leonie, Alina Zubrod, Nicola Catone, Johanna Bialas e Annette Aichem. "Tumor necrosis factor mediates USE1-independent FAT10ylation under inflammatory conditions". Life Science Alliance 6, n. 11 (21 agosto 2023): e202301985. http://dx.doi.org/10.26508/lsa.202301985.

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The ubiquitin-like modifier FAT10 is up-regulated in many different cell types by IFNγ and TNFα (TNF) and directly targets proteins for proteasomal degradation. FAT10 gets covalently conjugated to its conjugation substrates by the E1 activating enzyme UBA6, the E2 conjugating enzyme USE1, and E3 ligases including Parkin. To date, USE1 was supposed to be the only E2 enzyme for FAT10ylation, and we show here that a knockout of USE1 strongly diminished FAT10 conjugation. Remarkably, under inflammatory conditions in the presence of TNF, FAT10 conjugation appears to be independent of USE1. We report on the identification of additional E2 conjugating enzymes, which were previously not associated with FAT10. We confirm their capacity to be charged with FAT10 onto their active site cysteine, and to rescue FAT10 conjugation in the absence of USE1. This finding strongly widens the field of FAT10 research by pointing to multiple, so far unknown pathways for the conjugation of FAT10, disclosing novel possibilities for pharmacological interventions to regulate FAT10 conjugation under inflammatory conditions and/or viral infections.

3

Jia, Yue, Ping Ji e Samuel W. French. "The Role of FAT10 in Alcoholic Hepatitis Pathogenesis". Biomedicines 8, n. 7 (1 luglio 2020): 189. http://dx.doi.org/10.3390/biomedicines8070189.

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FAT10 expression is highly up-regulated by pro-inflammatory cytokines IFNγ and TNFα in all cell types and tissues. Increased FAT10 expression may induce increasing mitotic non-disjunction and chromosome instability, leading to tumorigenesis. In this review, we summarized others’ and our work on FAT10 expression in liver biopsy samples from patients with alcoholic hepatitis (AH). FAT10 is essential to maintain the function of liver cell protein quality control and Mallory–Denk body (MDB) formation. FAT10 overexpression in AH leads to balloon degeneration and MDB aggregation formation, all of which is prevented in fat10-/- mice. FAT10 causes the proteins’ accumulation, overexpression, and forming MDBs through modulating 26s proteasome’s proteases. The pathway that increases FAT10 expression includes TNFα/IFNγ and the interferon sequence response element (ISRE), followed by NFκB and STAT3, which were all up-regulated in AH. FAT10 was only reported in human and mouse specimens but plays critical role for the development of alcoholic hepatitis. Flavanone derivatives of milk thistle inhibit TNFα/IFNγ, NFκB, and STAT3, then inhibit the expression of FAT10. NFκB is the key nodal hub of the IFNα/TNFα-response genes. Studies on Silibinin and other milk thistle derivatives to treat AH confirms that overexpressed FAT10 is the major key molecule in these networks.

4

Mah, Mei Min, Nicola Roverato e Marcus Groettrup. "Regulation of Interferon Induction by the Ubiquitin-Like Modifier FAT10". Biomolecules 10, n. 6 (23 giugno 2020): 951. http://dx.doi.org/10.3390/biom10060951.

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The revelation that the human major histocompatibility complex (MHC) class I locus encodes a ubiquitin-like protein designated HLA-F adjacent transcript 10 (FAT10) or ubiquitin D (UBD) has attracted increasing attention to the function of this protein. Interestingly, the pro-inflammatory cytokines interferon (IFN)-γ and tumor necrosis factor (TNF) α synergize to strongly induce FAT10 expression, thereby suggesting a role of FAT10 in the immune response. Recent reports that FAT10 downregulates type I interferon production while it upregulates IFN-γ pose mechanistic questions on how FAT10 differentially regulates interferon induction. Several covalent and non-covalent binding partners of FAT10 involved in signal transduction pathways leading to IFN synthesis have been identified. After introducing FAT10, we review here recent insights into how FAT10 affects proteins in the interferon pathways, like the virus-responsive pattern recognition receptor RIG-I, the ubiquitin ligase ZNF598, and the deubiquitylating enzyme OTUB1. Moreover, we outline the consequences of FAT10 deficiency on interferon synthesis and viral expansion in mice and human cells. We discuss the need for covalent isopeptide linkage of FAT10 to the involved target proteins and the concomitant targeting for proteasomal degradation. After years of investigating the elusive biological functions of this fascinating ubiquitin-like modifier, we review the emerging evidence for a novel role of FAT10 in interferon regulation.

5

Arshad, Maria, Nazefah Abdul Hamid, Mun Chiang Chan, Fuad Ismail, Geok Chin Tan, Francesco Pezzella e Ka-Liong Tan. "NUB1 and FAT10 Proteins as Potential Novel Biomarkers in Cancer: A Translational Perspective". Cells 10, n. 9 (24 agosto 2021): 2176. http://dx.doi.org/10.3390/cells10092176.

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Cancer increases the global disease burden substantially, but it remains a challenge to manage it. The search for novel biomarkers is essential for risk assessment, diagnosis, prognosis, prediction of treatment response, and cancer monitoring. This paper examined NEDD8 ultimate buster-1 (NUB1) and F-adjacent transcript 10 (FAT10) proteins as novel biomarkers in cancer. This literature review is based on the search of the electronic database, PubMed. NUB1 is an interferon-inducible protein that mediates apoptotic and anti-proliferative actions in cancer, while FAT10 is a ubiquitin-like modifier that promotes cancer. The upregulated expression of both NUB1 and FAT10 has been observed in various cancers. NUB1 protein binds to FAT10 non-covalently to promote FAT10 degradation. An overexpressed FAT10 stimulates nuclear factor-kappa β, activates the inflammatory pathways, and induces the proliferation of cancer. The FAT10 protein interacts with the mitotic arrest deficient 2 protein, causing chromosomal instability and breast tumourigenesis. FAT10 binds to the proliferating cell nuclear antigen protein and inhibits the DNA damage repair response. In addition, FAT10 involves epithelial–mesenchymal transition, invasion, apoptosis, and multiplication in hepatocellular carcinoma. Our knowledge about them is still limited. There is a need to further develop NUB1 and FAT10 as novel biomarkers.

6

Canaan, Allon, Xiaofeng Yu, Carmen J. Booth, Jin Lian, Isaac Lazar, Serwa L. Gamfi, Katrina Castille et al. "FAT10/Diubiquitin-Like Protein-Deficient Mice Exhibit Minimal Phenotypic Differences". Molecular and Cellular Biology 26, n. 13 (1 luglio 2006): 5180–89. http://dx.doi.org/10.1128/mcb.00966-05.

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ABSTRACT The FAT10 gene encodes a diubiquitin-like protein containing two tandem head-to-tail ubiquitin-like domains. There is a high degree of similarity between murine and human FAT10 sequences at both the mRNA and protein levels. In various cell lines, FAT10 expression was shown to be induced by gamma interferon or by tumor necrosis factor alpha. In addition, FAT10 expression was found to be up-regulated in some Epstein-Barr virus-infected B-cell lines, in activated dendritic cells, and in several epithelial tumors. However, forced expression of FAT10 in cultured cells was also found to produce apoptotic cell death. Overall, these findings suggest that FAT10 may modulate cellular growth or cellular viability. Here we describe the steps to generate, by genetic targeting, a FAT10 gene knockout mouse model. The FAT10 knockout homozygous mice are viable and fertile. No gross lesions or obvious histological differences were found in these mutated mice. Examination of lymphocyte populations from spleen, thymus, and bone marrow did not reveal any abnormalities. However, flow cytometry analysis demonstrated that the lymphocytes of FAT10 knockout mice were, on average, more prone to spontaneous apoptotic death. Physiologically, these mice demonstrated a high level of sensitivity toward endotoxin challenge. These findings indicate that FAT10 may function as a survival factor.

7

Schregle, Richard, Stefanie Mueller, Daniel F. Legler, Jérémie Rossy, Wolfgang A. Krueger e Marcus Groettrup. "FAT10 localises in dendritic cell aggresome-like induced structures and contributes to their disassembly". Journal of Cell Science 133, n. 14 (16 giugno 2020): jcs240085. http://dx.doi.org/10.1242/jcs.240085.

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ABSTRACTDendritic cell (DC) aggresome-like induced structures (DALIS) are protein aggregates of polyubiquitylated proteins that form transiently during DC maturation. DALIS scatter randomly throughout the cytosol and serve as antigen storage sites synchronising DC maturation and antigen presentation. Maturation of DCs is accompanied by the induction of the ubiquitin-like modifier FAT10 (also known as UBD), which localises to aggresomes, structures that are similar to DALIS. FAT10 is conjugated to substrate proteins and serves as a signal for their rapid and irreversible degradation by the 26S proteasome similar to, yet independently of ubiquitin, thereby contributing to antigen presentation. Here, we have investigated whether FAT10 is involved in the formation and turnover of DALIS, and whether proteins accumulating in DALIS can be modified through conjunction to FAT10 (FAT10ylated). We found that FAT10 localises to DALIS in maturing DCs and that this localisation occurs independently of its conjugation to substrates. Additionally, we investigated the DALIS turnover in FAT10-deficient and -proficient DCs, and observed FAT10-mediated disassembly of DALIS. Thus, we report further evidence that FAT10 is involved in antigen processing, which may provide a functional rationale as to why FAT10 is selectively induced upon DC maturation.

8

Boehm, Annika N., Johanna Bialas, Nicola Catone, Almudena Sacristan-Reviriego, Jacqueline van der Spuy, Marcus Groettrup e Annette Aichem. "The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation". Journal of Biological Chemistry 295, n. 42 (14 agosto 2020): 14402–18. http://dx.doi.org/10.1074/jbc.ra120.013873.

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The retina-specific chaperone aryl hydrocarbon interacting protein-like 1 (AIPL1) is essential for the correct assembly of phosphodiesterase 6 (PDE6), which is a pivotal effector enzyme for phototransduction and vision because it hydrolyzes cGMP. AIPL1 interacts with the cytokine-inducible ubiquitin-like modifier FAT10, which gets covalently conjugated to hundreds of proteins and targets its conjugation substrates for proteasomal degradation, but whether FAT10 affects PDE6 function or turnover is unknown. Here, we show that FAT10 mRNA is expressed in human retina and identify rod PDE6 as a retina-specific substrate of FAT10 conjugation. We found that AIPL1 stabilizes the FAT10 monomer and the PDE6-FAT10 conjugate. Additionally, we elucidated the functional consequences of PDE6 FAT10ylation. On the one hand, we demonstrate that FAT10 targets PDE6 for proteasomal degradation by formation of a covalent isopeptide linkage. On the other hand, FAT10 inhibits PDE6 cGMP hydrolyzing activity by noncovalently interacting with the PDE6 GAFa and catalytic domains. Therefore, FAT10 may contribute to loss of PDE6 and, as a consequence, degeneration of retinal cells in eye diseases linked to inflammation and inherited blindness-causing mutations in AIPL1.

9

Saxena, Kritika, Nicola Domenico Roverato, Melody Reithmann, Mei Min Mah, Richard Schregle, Gunter Schmidtke, Ivan Silbern, Henning Urlaub e Annette Aichem. "FAT10 is phosphorylated by IKKβ to inhibit the antiviral type-I interferon response". Life Science Alliance 7, n. 1 (8 novembre 2023): e202101282. http://dx.doi.org/10.26508/lsa.202101282.

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IFN-I secretion provides a rapid host defense against infection with RNA viruses. Within the host cell, viral RNA triggers the activation of the RIG-I signaling pathway, leading to the production of IFN-I. Because an exaggerated IFN-I response causes severe tissue damage, RIG-I signaling is tightly regulated. One of the factors that control the IFN-I response is the ubiquitin-like modifier FAT10, which is induced by TNF and IFNγ and targets covalently FAT10-linked proteins for proteasomal degradation. However, the mechanism of how FAT10 modulates IFN-I secretion remains to be fully elucidated. Here, we provide strong evidence that FAT10 is phosphorylated by IκB kinase β (IKKβ) upon TNF stimulation and during influenza A virus infection on several serine and threonine residues. FAT10 phosphorylation increases the binding of FAT10 to the TRAF3-deubiquitylase OTUB1 and its FAT10-mediated activation. Consequently, FAT10 phosphorylation results in a low ubiquitylation state of TRAF3, which is unable to maintain interferon regulatory factor 3 phosphorylation and downstream induction of IFN-I. Taken together, we reveal a mechanism of how phosphorylation of FAT10 limits the production of tissue-destructive IFN-I in inflammation.

10

Yao, Yi, Weikun Jia, Xiaofei Zeng, Yali Wang, Qiuxia Hu, Shiran Yu, Dongsheng He e Ying Li. "FAT10 Combined with Miltefosine Inhibits Mitochondrial Apoptosis and Energy Metabolism in Hypoxia-Induced H9C2 Cells by Regulating the PI3K/AKT Signaling Pathway". Evidence-Based Complementary and Alternative Medicine 2022 (18 agosto 2022): 1–10. http://dx.doi.org/10.1155/2022/4388919.

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Hypoxia-induced cardiomyocyte apoptosis is the main contributor to heart diseases. Human leukocyte antigen F-associated transcript 10 (FAT10), the small ubiquitin-like protein family subtype involved in apoptosis, is expressed in the heart and exhibits cardioprotective functions. This study explored the impact of FAT10 on hypoxia-induced cardiomyocyte apoptosis and the involved mechanisms. The cardiomyocyte cell line H9C2 was cultivated in hypoxia-inducing conditions (94% N2, 5% CO2, and 1% O2) and the expression of FAT10 in hypoxia-stimulated H9C2 cells was identified. For this, FAT10 overexpression/interference vectors were exposed to transfection into H9C2 cells with/without the PI3K/AKT inhibitor, miltefosine. The results indicated that hypoxia exposure decreased the FAT10 expression, suppressed H9C2 cell growth, disrupted mitochondrial metabolism, and promoted H9C2 cell apoptosis and oxidative stress. However, these impacts were reversed by the FAT10 overexpression. In addition, the inhibition of PI3K/AKT in FAT10-overexpressing cells suppressed cell proliferation, impaired mitochondrial metabolism, and promoted apoptosis and oxidative stress response. The findings demonstrated that FAT10 inhibited mitochondrial apoptosis and energy metabolism in hypoxia-stimulated H9C2 cells through the PI3K/AKT pathway. This finding can be utilized for developing therapeutic targets for treating heart disorders associated with hypoxia-induced apoptosis.

11

Mueller, Stefanie, Johanna Bialas, Stella Ryu, Nicola Catone e Annette Aichem. "The ubiquitin-like modifier FAT10 covalently modifies HUWE1 and strengthens the interaction of AMBRA1 and HUWE1". PLOS ONE 18, n. 8 (14 agosto 2023): e0290002. http://dx.doi.org/10.1371/journal.pone.0290002.

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The ubiquitin-like modifier FAT10 is highly upregulated under inflammatory conditions and targets its conjugation substrates to the degradation by the 26S proteasome. This process termed FAT10ylation is mediated by an enzymatic cascade and includes the E1 activating enzyme ubiquitin-like modifier activating enzyme 6 (UBA6), the E2 conjugating enzyme UBA6-specific E2 enzyme 1 (USE1) and E3 ligases, such as Parkin. In this study, the function of the HECT-type ubiquitin E3 ligase HUWE1 was investigated as a putative E3 ligase and/or conjugation substrate of FAT10. Our data provide strong evidence that HUWE1 is FAT10ylated in a UBA6 and FAT10 diglycine-dependent manner in vitro and in cellulo and that the HUWE1-FAT10 conjugate is targeted to proteasomal degradation. Since the mutation of all relevant cysteine residues within the HUWE1 HECT domain did not abolish FAT10 conjugation, a role of HUWE1 as E3 ligase for FAT10ylation is rather unlikely. Moreover, we have identified the autophagy-related protein AMBRA1 as a new FAT10 interaction partner. We show that the HUWE1-FAT10 conjugate formation is diminished in presence of AMBRA1, while the interaction between AMBRA1 and HUWE1 is strengthened in presence of FAT10. This implies a putative interplay of all three proteins in cellular processes such as mitophagy.

12

Aichem, Annette, e Marcus Groettrup. "The ubiquitin-like modifier FAT10 – much more than a proteasome-targeting signal". Journal of Cell Science 133, n. 14 (15 luglio 2020): jcs246041. http://dx.doi.org/10.1242/jcs.246041.

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ABSTRACTHuman leukocyte antigen (HLA)-F adjacent transcript 10 (FAT10) also called ubiquitin D (UBD) is a member of the ubiquitin-like modifier (ULM) family. The FAT10 gene is localized in the MHC class I locus and FAT10 protein expression is mainly restricted to cells and organs of the immune system. In all other cell types and tissues, FAT10 expression is highly inducible by the pro-inflammatory cytokines interferon (IFN)-γ and tumor necrosis factor (TNF). Besides ubiquitin, FAT10 is the only ULM which directly targets its substrates for degradation by the 26S proteasome. This poses the question as to why two ULMs sharing the proteasome-targeting function have evolved and how they differ from each other. This Review summarizes the current knowledge of the special structure of FAT10 and highlights its differences from ubiquitin. We discuss how these differences might result in differential outcomes concerning proteasomal degradation mechanisms and non-covalent target interactions. Moreover, recent insights about the structural and functional impact of FAT10 interacting with specific non-covalent interaction partners are reviewed.

13

Xiang, Senfeng, Xuejing Shao, Ji Cao, Bo Yang, Qiaojun He e Meidan Ying. "FAT10: Function and Relationship with Cancer". Current Molecular Pharmacology 13, n. 3 (9 luglio 2020): 182–91. http://dx.doi.org/10.2174/1874467212666191113130312.

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Posttranslational protein modifications are known to be extensively involved in cancer, and a growing number of studies have revealed that the ubiquitin-like modifier FAT10 is directly involved in cancer development. FAT10 was found to be highly upregulated in various cancer types, such as glioma, hepatocellular carcinoma, breast cancer and gastrointestinal cancer. Protein FAT10ylation and interactions with FAT10 lead to the functional change of proteins, including proteasomal degradation, subcellular delocalization and stabilization, eventually having significant effects on cancer cell proliferation, invasion, metastasis and even tumorigenesis. In this review, we summarized the current knowledge on FAT10 and discussed its biological functions in cancer, as well as potential therapeutic strategies based on the FAT10 pathway.

14

Snyder, Alexandra, Zygimantas Alsauskas, Pengfei Gong, Paul E. Rosenstiel, Mary E. Klotman, Paul E. Klotman e Michael J. Ross. "FAT10: a Novel Mediator of Vpr-Induced Apoptosis in Human Immunodeficiency Virus-Associated Nephropathy". Journal of Virology 83, n. 22 (2 settembre 2009): 11983–88. http://dx.doi.org/10.1128/jvi.00034-09.

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ABSTRACT Human immunodeficiency virus (HIV)-associated nephropathy is a significant cause of morbidity and mortality in HIV-infected persons. Vpr-induced cell cycle dysregulation and apoptosis of renal tubular epithelial cells are important components of the pathogenesis of HIV-associated nephropathy (HIVAN). FAT10 is a ubiquitin-like protein that is upregulated in renal tubular epithelial cells in HIVAN. In these studies, we report that Vpr induces increased expression of FAT10 in tubular cells and that inhibition of FAT10 expression prevents Vpr-induced apoptosis in human and murine tubular cells. Moreover, we found that Vpr interacts with FAT10 and that these proteins colocalize at mitochondria. These studies establish FAT10 as a novel mediator of Vpr-induced cell death.

15

Brockmann, Florian, Nicola Catone, Christine Wünsch, Fabian Offensperger, Martin Scheffner, Gunter Schmidtke e Annette Aichem. "FAT10 and NUB1L cooperate to activate the 26S proteasome". Life Science Alliance 6, n. 8 (15 maggio 2023): e202201463. http://dx.doi.org/10.26508/lsa.202201463.

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The interaction of the 19S regulatory particle of the 26S proteasome with ubiquitylated proteins leads to gate opening of the 20S core particle and increases its proteolytic activity by binding of the ubiquitin chain to the inhibitory deubiquitylation enzyme USP14 on the 19S regulatory subunit RPN1. Covalent modification of proteins with the cytokine inducible ubiquitin-like modifier FAT10 is an alternative signal for proteasomal degradation. Here, we report that FAT10 and its interaction partner NUB1L facilitate the gate opening of the 20S proteasome in an ubiquitin- and USP14-independent manner. We also show that FAT10 is capable to activate all peptidolytic activities of the 26S proteasome, however only together with NUB1L, by binding to the UBA domains of NUB1L and thereby interfering with NUB1L dimerization. The binding of FAT10 to NUB1L leads to an increased affinity of NUB1L for the subunit RPN1. In conclusion, the herein described cooperation of FAT10 and NUB1L is a substrate-induced mechanism to activate the 26S proteasome.

16

Wang, Fengting, e Bo Zhao. "UBA6 and Its Bispecific Pathways for Ubiquitin and FAT10". International Journal of Molecular Sciences 20, n. 9 (7 maggio 2019): 2250. http://dx.doi.org/10.3390/ijms20092250.

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Questions have been raised since the discovery of UBA6 and its significant coexistence with UBE1 in the ubiquitin–proteasome system (UPS). The facts that UBA6 has the dedicated E2 enzyme USE1 and the E1–E2 cascade can activate and transfer both ubiquitin and ubiquitin-like protein FAT10 have attracted a great deal of attention to the regulational mechanisms of the UBA6–USE1 cascade and to how FAT10 and ubiquitin differentiate with each other. This review recapitulates the latest advances in UBA6 and its bispecific UBA6–USE1 pathways for both ubiquitin and FAT10. The intricate networks of UBA6 and its interplays with ubiquitin and FAT10 are briefly reviewed, as are their individual and collective functions in diverse physiological conditions.

17

Buchsbaum, Samuel, Beatrice Bercovich e Aaron Ciechanover. "FAT10 is a proteasomal degradation signal that is itself regulated by ubiquitination". Molecular Biology of the Cell 23, n. 1 (gennaio 2012): 225–32. http://dx.doi.org/10.1091/mbc.e11-07-0609.

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FAT10 is a ubiquitin-like protein modifier that is induced in vertebrates following certain inflammatory stimuli. Its functions and the repertoire of its target substrates have remained elusive. In contrast to ubiquitin, its cellular abundance is tightly controlled by both transcriptional and posttranslational regulation, and it was reported to be rapidly degraded by the proteasome. Here we provide data to indicate that the degradation of FAT10 requires ubiquitination: degradation was inhibited in cells expressing a ubiquitin mutant that cannot be polymerized and in a mutant cell harboring a thermolabile ubiquitin-activating enzyme, E1. Of importance, FAT10 can serve as a degradation signal for otherwise stable proteins, and in this case, too, the targeting to the proteasome requires ubiquitination. Degradation of FAT10 is accelerated after induction of apoptosis, suggesting that it plays a role in prosurvival pathways.

18

Oliveri, Franziska, Steffen Johannes Keller, Heike Goebel, Gerardo Omar Alvarez Salinas e Michael Basler. "The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro but not in cellulo". Life Science Alliance 6, n. 6 (3 aprile 2023): e202201760. http://dx.doi.org/10.26508/lsa.202201760.

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Ubiquitin-independent protein degradation via the 20S proteasome without the 19S regulatory particle has gained increasing attention over the last years. The degradation of the ubiquitin-like modifier FAT10 by the 20S proteasome was investigated in this study. We found that FAT10 was rapidly degraded by purified 20S proteasomes in vitro, which was attributed to the weak folding of FAT10 and the N-terminally disordered tail. To confirm our results in cellulo, we established an inducible RNA interference system in which the AAA-ATPase Rpt2 of the 19S regulatory particle is knocked down to impair the function of the 26S proteasome. Using this system, degradation of FAT10 in cellulo was strongly dependent on functional 26S proteasome. Our data indicate that in vitro degradation studies with purified proteins do not necessarily reflect biological degradation mechanisms occurring in cells and, therefore, cautious data interpretation is required when 20S proteasome function is studied in vitro.

19

Peng, Xiaogang, Jianghua Shao, Yang Shen, Yunguo Zhou, Qing Cao, Jinzhu Hu, Wenfeng He et al. "FAT10 protects cardiac myocytes against apoptosis". Journal of Molecular and Cellular Cardiology 59 (giugno 2013): 1–10. http://dx.doi.org/10.1016/j.yjmcc.2013.01.018.

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20

Ma, Chengbin, Zhiyu Zhang, Yan Cui, Hongmou Yuan e Feng Wang. "Silencing FAT10 inhibits metastasis of osteosarcoma". International Journal of Oncology 49, n. 2 (1 giugno 2016): 666–74. http://dx.doi.org/10.3892/ijo.2016.3549.

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21

Chiu, Yu-Hsin, Qinmiao Sun e Zhijian J. Chen. "E1-L2 Activates Both Ubiquitin and FAT10". Molecular Cell 27, n. 6 (settembre 2007): 1014–23. http://dx.doi.org/10.1016/j.molcel.2007.08.020.

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Kubo, Yoshinao, Kiyoshi Yasui, Mai Izumida, Hideki Hayashi e Toshifumi Matsuyama. "IDO1, FAT10, IFI6, and GILT Are Involved in the Antiretroviral Activity of γ-Interferon and IDO1 Restricts Retrovirus Infection by Autophagy Enhancement". Cells 11, n. 14 (19 luglio 2022): 2240. http://dx.doi.org/10.3390/cells11142240.

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Gamma-interferon (γ-IFN) significantly inhibits infection by replication-defective viral vectors derived from the human immunodeficiency virus type 1 (HIV-1) or murine leukemia virus (MLV) but the underlying mechanism remains unclear. Previously we reported that knockdown of γ-IFN-inducible lysosomal thiolreductase (GILT) abrogates the antiviral activity of γ-IFN in TE671 cells but not in HeLa cells, suggesting that other γ-IFN-inducible host factors are involved in its antiviral activity in HeLa cells. We identified cellular factors, the expression of which are induced by γ-IFN in HeLa cells, using a microarray, and analyzed the effects of 11 γ-IFN-induced factors on retroviral vector infection. Our results showed that the exogenous expression of FAT10, IFI6, or IDO1 significantly inhibits both HIV-1- and MLV-based vector infections. The antiviral activity of γ-IFN was decreased in HeLa cells, in which the function of IDO1, IFI6, FAT10, and GILT were simultaneously inhibited. IDO1 is an enzyme that metabolizes an essential amino acid, tryptophan. However, IDO1 did not restrict retroviral vector infection in Atg3-silencing HeLa cells, in which autophagy did not occur. This study found that IDO1, IFI6, FAT10, and GILT are involved in the antiviral activity of γ-IFN, and IDO1 inhibits retroviral infection by inducing autophagy.

23

Jia, Yue, e Sameul W. French. "The Role of FAT10 in Alcoholic Hepatitis Pathogenesis". FASEB Journal 34, S1 (aprile 2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.04810.

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24

Theng, Steven Setiawan, Wei Wang, Way-Champ Mah, Cheryl Chan, Jingli Zhuo, Yun Gao, Haina Qin et al. "Disruption of FAT10–MAD2 binding inhibits tumor progression". Proceedings of the National Academy of Sciences 111, n. 49 (24 novembre 2014): E5282—E5291. http://dx.doi.org/10.1073/pnas.1403383111.

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25

Aichem, Annette, e Marcus Groettrup. "The ubiquitin-like modifier FAT10 in cancer development". International Journal of Biochemistry & Cell Biology 79 (ottobre 2016): 451–61. http://dx.doi.org/10.1016/j.biocel.2016.07.001.

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Li, Tianwei, Rasa Santockyte, Shiqin Yu, Rong-Fong Shen, Ephrem Tekle, Caroline G. L. Lee, David C. H. Yang e P. Boon Chock. "FAT10 modifies p53 and upregulates its transcriptional activity". Archives of Biochemistry and Biophysics 509, n. 2 (maggio 2011): 164–69. http://dx.doi.org/10.1016/j.abb.2011.02.017.

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Chen, Chen, Xiaoqing Li, Tao Zhou, Yuhao Su, Bodong Yu, Jiejing Jin, Jinyan Xie, Yang Shen, Rong Wan e Kui Hong. "Ubiquitin like protein FAT10 repressed cardiac fibrosis after myocardial ischemic via mediating degradation of Smad3 dependent on FAT10-proteasome system". International Journal of Biological Sciences 19, n. 3 (2023): 881–96. http://dx.doi.org/10.7150/ijbs.77677.

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Liu, Shuaichen, Yu Jin, Dongwei Zhang, Jingbo Wang, Guangyi Wang e Caroline G. L. Lee. "Investigating the Promoter of FAT10 Gene in HCC Patients". Genes 9, n. 7 (26 giugno 2018): 319. http://dx.doi.org/10.3390/genes9070319.

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29

Gong, Pengfei, Allon Canaan, Bin Wang, Jeremy Leventhal, Alexandra Snyder, Viji Nair, Clemens D. Cohen et al. "The Ubiquitin-Like Protein FAT10 Mediates NF-κB Activation". Journal of the American Society of Nephrology 21, n. 2 (3 dicembre 2009): 316–26. http://dx.doi.org/10.1681/asn.2009050479.

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Hong, K., Y. Shen, J. H. Shao, X. G. P. Peng, Q. Cao, W. F. He, X. Yu, X. X. Liu e A. J. Marian. "Ubiquitin-like protein fat10 protects cardiac myocytes against apoptosis". European Heart Journal 34, suppl 1 (2 agosto 2013): P3279. http://dx.doi.org/10.1093/eurheartj/eht309.p3279.

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31

Wimalarathne, Madushika M., Luis D. Mercado, Quiana C. Wilkerson Vidal, James Wolfsberger, Victoria J. McConnell, Bernhard Vogler e Sharifa Tahirah Love-Rutledge. "Young Adult LEW.1WR1 Rats, a Model of Liver FAT10 Overexpression, Develop Insulin Resistance and Fatty Liver With Age". Journal of the Endocrine Society 5, Supplement_1 (1 maggio 2021): A514. http://dx.doi.org/10.1210/jendso/bvab048.1051.

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Abstract (sommario):

Abstract As human lifespan increases, comorbid conditions that impact quality of life have become a serious problem. FAT10 has been identified as a gene that when knocked out, improves age associated metabolic dysfunctions and increased longevity in mice (1). There is increased Fat10 expression in the liver in obesity (2,5). Providing evidence that fat10 expression may be important for triggering the transition to metabolic dysfunction in aging. Adult LEW.1WR1(1WR1) rats have increased body mass without excess abdominal fat mass compared to control rats (3). Yet, it was unclear where the excess mass was stored. We hypothesized that the 1WR1 rat would develop increased liver fat mass as a product of increased insulin resistance in response to increased liver fat10 expression over time. To test this hypothesis, we did insulin tolerance tests(7 weeks & 15 weeks), triglyceride assays, and histological analysis of the liver(23 weeks), in 1WR1 rats(n=7) and Wistar Furth (WF) rats(n=7) on control diets. We analyzed images using histological scoring for nonalcoholic fatty liver disease from the literature (4). We also assessed the slides for Mallory Denk bodies (MBs). The body mass of 1WR1 rats were increased compared to WF rat groups starting from the age of 7 weeks (391.4∓8.572g vs. 271.8∓11.62g; p <0.0006). 1WR1 rats became more insulin resistant with age, the 1WR1 rat group has increased AUC of 7 and 15 week Insulin Tolerance Tests (401.5∓23.54 vs. 245.3∓10.20 7w ITT1; p= 0.0728, 15w ITT2 328.2∓14.86 vs. 217.8∓9.; p <0.0003) compared to WF rats. 1WR1 rats have increased liver mass (11.85g∓0.7699g vs. 7.235g∓0.3864g; p=0.0006) liver triglyceride levels compared to WF rats (192.8∓21.8 mg/mL vs. 130.1∓13.075 mg/mL; p=0.0728). 1WR1 rats have increased steatosis scores(1.857∓0.2608 vs. 1.143∓0.1429;p= 0.0862) yet significantly reduced inflammatory foci level (2∓0.8165 vs. 3∓0;p= 0.007), most 1WR1 hepatocytes are enlarged (ballooned) and contained MBs compared to WF rats suggesting 1WR1 rats have already passed the early inflammation stage. Adult 1WR1 rats developed reduced insulin sensitivity and lipid accumulation in the liver. These data support our hypothesis that 1WR1 rats would develop increased liver fat and impaired insulin resistance in response to aging and show that this process may be inflammation driven. (1) Canaan et al.,PNAS. April 2014; 111 (14): 5313-5318.(2)Vidal et al., FASEB.2020, 34: 1-1,(3) Collins et al., J Endocr Soc. 2019;3(1),(4).Kleiner et al., Hepatology, 2005; 41 (6): 1313–1321,(5).Dali-Youcef et al., Hepatol Commun. 2019;3(9):1205-1220.

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Ren, Jianwei, Alison Kan, Siew Hong Leong, London L. P. J. Ooi, Kuan-Teh Jeang, Samuel S. Chong, Oi Lian Kon e Caroline G. L. Lee. "FAT10 Plays a Role in the Regulation of Chromosomal Stability". Journal of Biological Chemistry 281, n. 16 (22 febbraio 2006): 11413–21. http://dx.doi.org/10.1074/jbc.m507218200.

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Ren, J., Y. Wang, Y. Gao, S. B. K. Mehta e C. G. L. Lee. "FAT10 mediates the effect of TNF- in inducing chromosomal instability". Journal of Cell Science 124, n. 21 (24 ottobre 2011): 3665–75. http://dx.doi.org/10.1242/jcs.087403.

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Zhou, Qiongqiong, Xiaogang Peng, Xiao Liu, Leifeng Chen, Qinmei Xiong, Yang Shen, Jinyan Xie et al. "FAT10 attenuates hypoxia-induced cardiomyocyte apoptosis by stabilizing caveolin-3". Journal of Molecular and Cellular Cardiology 116 (marzo 2018): 115–24. http://dx.doi.org/10.1016/j.yjmcc.2018.02.008.

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35

Nagashima, Yu, Hisatomo Kowa, Shoji Tsuji e Atsushi Iwata. "FAT10 Protein Binds to Polyglutamine Proteins and Modulates Their Solubility". Journal of Biological Chemistry 286, n. 34 (8 luglio 2011): 29594–600. http://dx.doi.org/10.1074/jbc.m111.261032.

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Spinnenhirn, Valentina, Annegret Bitzer, Annette Aichem e Marcus Groettrup. "Newly translated proteins are substrates for ubiquitin, ISG15, and FAT10". FEBS Letters 591, n. 1 (20 dicembre 2016): 186–95. http://dx.doi.org/10.1002/1873-3468.12512.

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Um, Hyojin, Hoim Jeong, Beomgu Lee, Yerin Kim, Jihyeon Lee, Jong Seong Roh, Seung-Geun Lee, Hae Ryoun Park, William H. Robinson e Dong Hyun Sohn. "FAT10 Induces cancer cell migration by stabilizing phosphorylated ABI3/NESH". Animal Cells and Systems 27, n. 1 (11 marzo 2023): 53–60. http://dx.doi.org/10.1080/19768354.2023.2186486.

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Dong, Dingxiang, Weifan Jiang, Jun Lei, Leifeng Chen, Xiuxia Liu, Jin Ge, Ben Che, Xiaoqing Xi e Jianghua Shao. "Ubiquitin-like protein FAT10 promotes bladder cancer progression by stabilizing survivin". Oncotarget 7, n. 49 (28 ottobre 2016): 81463–73. http://dx.doi.org/10.18632/oncotarget.12976.

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Lukasiak, S., C. Schiller, P. Oehlschlaeger, G. Schmidtke, P. Krause, D. F. Legler, F. Autschbach, P. Schirmacher, K. Breuhahn e M. Groettrup. "Proinflammatory cytokines cause FAT10 upregulation in cancers of liver and colon". Oncogene 27, n. 46 (23 giugno 2008): 6068–74. http://dx.doi.org/10.1038/onc.2008.201.

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Basler, Michael, Stefanie Buerger e Marcus Groettrup. "The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense". Molecular Immunology 68, n. 2 (dicembre 2015): 129–32. http://dx.doi.org/10.1016/j.molimm.2015.04.012.

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Kandel-Kfir, Michal, Rolando Garcia-Milan, Itai Gueta, Irit Lubitz, Ilan Ben-Zvi, Aviv Shaish, Lidar Shir et al. "IFNγ potentiates TNFα/TNFR1 signaling to induce FAT10 expression in macrophages". Molecular Immunology 117 (gennaio 2020): 101–9. http://dx.doi.org/10.1016/j.molimm.2019.11.004.

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Canaan, A., J. DeFuria, E. Perelman, V. Schultz, M. Seay, D. Tuck, R. A. Flavell, M. P. Snyder, M. S. Obin e S. M. Weissman. "Extended lifespan and reduced adiposity in mice lacking the FAT10 gene". Proceedings of the National Academy of Sciences 111, n. 14 (24 marzo 2014): 5313–18. http://dx.doi.org/10.1073/pnas.1323426111.

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Reznik, Nava, Noga Kozer, Avital Eisenberg-Lerner, Haim Barr, Yifat Merbl e Nir London. "Phenotypic Screen Identifies JAK2 as a Major Regulator of FAT10 Expression". ACS Chemical Biology 14, n. 12 (3 dicembre 2019): 2538–45. http://dx.doi.org/10.1021/acschembio.9b00667.

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44

Bett, John S., Naheed Kanuga, Emma Richet, Gunter Schmidtke, Marcus Groettrup, Michael E. Cheetham e Jacqueline van der Spuy. "The Inherited Blindness Protein AIPL1 Regulates the Ubiquitin-Like FAT10 Pathway". PLoS ONE 7, n. 2 (7 febbraio 2012): e30866. http://dx.doi.org/10.1371/journal.pone.0030866.

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Raasi, Shahri, Gunter Schmidtke e Marcus Groettrup. "The Ubiquitin-like Protein FAT10 Forms Covalent Conjugates and Induces Apoptosis". Journal of Biological Chemistry 276, n. 38 (9 luglio 2001): 35334–43. http://dx.doi.org/10.1074/jbc.m105139200.

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Ross, Michael J., Matthew S. Wosnitzer, Michael D. Ross, Benedetta Granelli, G. Luca Gusella, Mohammad Husain, Lewis Kaufman et al. "Role of Ubiquitin-Like Protein FAT10 in Epithelial Apoptosis in Renal Disease". Journal of the American Society of Nephrology 17, n. 4 (22 febbraio 2006): 996–1004. http://dx.doi.org/10.1681/asn.2005070692.

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Bialas, Johanna, Annika N. Boehm, Nicola Catone, Annette Aichem e Marcus Groettrup. "The ubiquitin-like modifier FAT10 stimulates the activity of deubiquitylating enzyme OTUB1". Journal of Biological Chemistry 294, n. 12 (4 febbraio 2019): 4315–30. http://dx.doi.org/10.1074/jbc.ra118.005406.

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Zhou, Qiongqiong, e Kui Hong. "GW29-e0267 FAT10 attenuates hypoxia-induced cardiomyocyte apoptosis by stabilizing caveolin-3". Journal of the American College of Cardiology 72, n. 16 (ottobre 2018): C9. http://dx.doi.org/10.1016/j.jacc.2018.08.039.

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Sun, Guo-Hui, Ying-Di Liu, Guo Yu, Nan Li, Xiao Sun e Jing Yang. "Increased FAT10 expression is related to poor prognosis in pancreatic ductal adenocarcinoma". Tumor Biology 35, n. 6 (4 febbraio 2014): 5167–71. http://dx.doi.org/10.1007/s13277-014-1670-1.

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Qing, Xin, Babara A. French, Joan Oliva e Samuel W. French. "Increased expression of FAT10 in colon benign, premalignant and malignant epithelial neoplasms". Experimental and Molecular Pathology 90, n. 1 (febbraio 2011): 51–54. http://dx.doi.org/10.1016/j.yexmp.2010.09.005.

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