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Journal articles on the topic 'FAT10'

Author: Grafiati

Published: 15 June 2024

Last updated: 31 July 2025

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1

Cao, Jinjing, Annette Aichem, Michael Basler, Gerardo Omar Alvarez Salinas, and Gunter Schmidtke. "Phosphorylated FAT10 Is More Efficiently Conjugated to Substrates, Does Not Bind to NUB1L, and Does Not Alter Degradation by the Proteasome." Biomedicines 12, no. 12 (2024): 2795. https://doi.org/10.3390/biomedicines12122795.

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Background: FAT10 is a member of the ubiquitin-like modifier family. Similar to ubiquitin, FAT10 has a distinct enzyme cascade consisting of E1-activating, E2-conjugating, and possibly several E3-ligating enzymes, which will covalently link FAT10 to substrate proteins in order to target them directly for proteasomal degradation. FAT10 was reported to be phosphorylated by IKKβ during infection with influenza A virus. Methods: To assess the difference between the FAT10-dependent degradation of phosphorylated FAT10 and the non-phosphorylated FAT10 wild type (FAT10 WT), a mutated FAT10 that mimick

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2

Hipp, Mark Steffen, Birte Kalveram, Shahri Raasi, Marcus Groettrup, and Gunter Schmidtke. "FAT10, a Ubiquitin-Independent Signal for Proteasomal Degradation." Molecular and Cellular Biology 25, no. 9 (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

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3

Schnell, Leonie, Alina Zubrod, Nicola Catone, Johanna Bialas, and Annette Aichem. "Tumor necrosis factor mediates USE1-independent FAT10ylation under inflammatory conditions." Life Science Alliance 6, no. 11 (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 repor

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4

Jia, Yue, Ping Ji, and Samuel W. French. "The Role of FAT10 in Alcoholic Hepatitis Pathogenesis." Biomedicines 8, no. 7 (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 wh

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5

Mah, Mei Min, Nicola Roverato, and Marcus Groettrup. "Regulation of Interferon Induction by the Ubiquitin-Like Modifier FAT10." Biomolecules 10, no. 6 (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 differ

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6

Arshad, Maria, Nazefah Abdul Hamid, Mun Chiang Chan, et al. "NUB1 and FAT10 Proteins as Potential Novel Biomarkers in Cancer: A Translational Perspective." Cells 10, no. 9 (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

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7

Canaan, Allon, Xiaofeng Yu, Carmen J. Booth, et al. "FAT10/Diubiquitin-Like Protein-Deficient Mice Exhibit Minimal Phenotypic Differences." Molecular and Cellular Biology 26, no. 13 (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 pro

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8

Schregle, Richard, Stefanie Mueller, Daniel F. Legler, Jérémie Rossy, Wolfgang A. Krueger, and Marcus Groettrup. "FAT10 localises in dendritic cell aggresome-like induced structures and contributes to their disassembly." Journal of Cell Science 133, no. 14 (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

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9

Boehm, Annika N., Johanna Bialas, Nicola Catone, et al. "The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation." Journal of Biological Chemistry 295, no. 42 (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 ret

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10

Saxena, Kritika, Nicola Domenico Roverato, Melody Reithmann та ін. "FAT10 is phosphorylated by IKKβ to inhibit the antiviral type-I interferon response". Life Science Alliance 7, № 1 (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.

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11

Cao, Jinjing, Gerardo Omar Alvarez Salinas, Gunter Schmidtke, and Michael Basler. "The ubiquitin-like modifier FAT10 does not affect IL-12 expression and signaling." PLOS One 20, no. 5 (2025): e0323005. https://doi.org/10.1371/journal.pone.0323005.

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The ubiquitin-like modifier FAT10 is strongly expressed in dendritic cells (DCs) and upregulated during inflammation. Interleukin (IL)-12 plays a critical role in promoting CD4+ T cell differentiation into Th1 cells and in IFN-γ induction in T cells. Previously, it was shown that FAT10 is required for IFN-γ expression of activated T cells. In this study, we investigated whether FAT10 influences IL-12 expression or IL-12 induced signaling and thereby contributes to the reduced IFN-γ expression. Presence or absence of FAT10 did not alter IL-12 expression in DC2.4 cells and in bone marrow derived

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12

Saxena, Kritika, Katharina Inholz, Michael Basler, and Annette Aichem. "FAT10 inhibits TRIM21 to down-regulate antiviral type-I interferon secretion." Life Science Alliance 7, no. 9 (2024): e202402786. http://dx.doi.org/10.26508/lsa.202402786.

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The ubiquitin-like modifier FAT10 is upregulated under pro-inflammatory conditions, targets its substrates for proteasomal degradation and functions as a negative regulator of the type-I IFN response. Influenza A virus infection upregulates the production of type-I IFN and the expression of the E3 ligase TRIM21, which regulates type-I IFN production in a positive feedback manner. In this study, we show that FAT10 becomes covalently conjugated to TRIM21 and that this targets TRIM21 for proteasomal degradation. We further show that the coiled-coil and PRYSPRY domains of TRIM21 and the C-terminal

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13

Yao, Yi, Weikun Jia, Xiaofei Zeng, et al. "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 (August 18, 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 overexp

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14

Mueller, Stefanie, Johanna Bialas, Stella Ryu, Nicola Catone, and Annette Aichem. "The ubiquitin-like modifier FAT10 covalently modifies HUWE1 and strengthens the interaction of AMBRA1 and HUWE1." PLOS ONE 18, no. 8 (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

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15

Aichem, Annette, and Marcus Groettrup. "The ubiquitin-like modifier FAT10 – much more than a proteasome-targeting signal." Journal of Cell Science 133, no. 14 (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 ques

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16

Xiang, Senfeng, Xuejing Shao, Ji Cao, Bo Yang, Qiaojun He, and Meidan Ying. "FAT10: Function and Relationship with Cancer." Current Molecular Pharmacology 13, no. 3 (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 prolif

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17

Snyder, Alexandra, Zygimantas Alsauskas, Pengfei Gong, et al. "FAT10: a Novel Mediator of Vpr-Induced Apoptosis in Human Immunodeficiency Virus-Associated Nephropathy." Journal of Virology 83, no. 22 (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

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18

Liang, Yusi, Ngar Woon Kam, Zhuoyou YU, and Ho Fun LEE. "Abstract 6724: The role of human leukocyte antigen F adjacent transcript 10 in the tumorigenesis of nasopharyngeal carcinoma." Cancer Research 85, no. 8_Supplement_1 (2025): 6724. https://doi.org/10.1158/1538-7445.am2025-6724.

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Abstract Nasopharyngeal carcinoma (NPC) is a highly aggressive malignancy prevalent in Southern China and Southeast Asia related to Epstein-Barr virus (EBV) infection and genetic variations at the Human Leukocyte Antigen (HLA) locus. Human leukocyte antigen (HLA)-F adjacent transcript 10 (FAT10) is a ubiquitin-like protein modifier that can modulate its substrates by (1) mediating degradation via the 26S proteasome or (2) altering function through Fat10ylation. Previously studies have found FAT10 overexpression in various cancers, including gliomas and hepatocellular carcinoma, promoting tumor

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19

Brockmann, Florian, Nicola Catone, Christine Wünsch, et al. "FAT10 and NUB1L cooperate to activate the 26S proteasome." Life Science Alliance 6, no. 8 (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 man

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20

Wang, Fengting, and Bo Zhao. "UBA6 and Its Bispecific Pathways for Ubiquitin and FAT10." International Journal of Molecular Sciences 20, no. 9 (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

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Buchsbaum, Samuel, Beatrice Bercovich, and Aaron Ciechanover. "FAT10 is a proteasomal degradation signal that is itself regulated by ubiquitination." Molecular Biology of the Cell 23, no. 1 (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 t

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22

Oliveri, Franziska, Steffen Johannes Keller, Heike Goebel, Gerardo Omar Alvarez Salinas, and Michael Basler. "The ubiquitin-like modifier FAT10 is degraded by the 20S proteasome in vitro but not in cellulo." Life Science Alliance 6, no. 6 (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

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23

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

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24

Ma, Chengbin, Zhiyu Zhang, Yan Cui, Hongmou Yuan, and Feng Wang. "Silencing FAT10 inhibits metastasis of osteosarcoma." International Journal of Oncology 49, no. 2 (2016): 666–74. http://dx.doi.org/10.3892/ijo.2016.3549.

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25

Kubo, Yoshinao, Kiyoshi Yasui, Mai Izumida, Hideki Hayashi та 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, № 14 (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,

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Chiu, Yu-Hsin, Qinmiao Sun, and Zhijian J. Chen. "E1-L2 Activates Both Ubiquitin and FAT10." Molecular Cell 27, no. 6 (2007): 1014–23. http://dx.doi.org/10.1016/j.molcel.2007.08.020.

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

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Theng, Steven Setiawan, Wei Wang, Way-Champ Mah, et al. "Disruption of FAT10–MAD2 binding inhibits tumor progression." Proceedings of the National Academy of Sciences 111, no. 49 (2014): E5282—E5291. http://dx.doi.org/10.1073/pnas.1403383111.

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

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30

Li, Tianwei, Rasa Santockyte, Shiqin Yu, et al. "FAT10 modifies p53 and upregulates its transcriptional activity." Archives of Biochemistry and Biophysics 509, no. 2 (2011): 164–69. http://dx.doi.org/10.1016/j.abb.2011.02.017.

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Chen, Chen, Xiaoqing Li, Tao Zhou, et al. "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, no. 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, and Caroline G. L. Lee. "Investigating the Promoter of FAT10 Gene in HCC Patients." Genes 9, no. 7 (2018): 319. http://dx.doi.org/10.3390/genes9070319.

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Gong, Pengfei, Allon Canaan, Bin Wang та ін. "The Ubiquitin-Like Protein FAT10 Mediates NF-κB Activation". Journal of the American Society of Nephrology 21, № 2 (2009): 316–26. http://dx.doi.org/10.1681/asn.2009050479.

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Hong, K., Y. Shen, J. H. Shao, et al. "Ubiquitin-like protein fat10 protects cardiac myocytes against apoptosis." European Heart Journal 34, suppl 1 (2013): P3279. http://dx.doi.org/10.1093/eurheartj/eht309.p3279.

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Wimalarathne, Madushika M., Luis D. Mercado, Quiana C. Wilkerson Vidal, et al. "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 (2021): A514. http://dx.doi.org/10.1210/jendso/bvab048.1051.

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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 exces

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Ren, Jianwei, Alison Kan, Siew Hong Leong, et al. "FAT10 Plays a Role in the Regulation of Chromosomal Stability." Journal of Biological Chemistry 281, no. 16 (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, and C. G. L. Lee. "FAT10 mediates the effect of TNF- in inducing chromosomal instability." Journal of Cell Science 124, no. 21 (2011): 3665–75. http://dx.doi.org/10.1242/jcs.087403.

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

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Nagashima, Yu, Hisatomo Kowa, Shoji Tsuji, and Atsushi Iwata. "FAT10 Protein Binds to Polyglutamine Proteins and Modulates Their Solubility." Journal of Biological Chemistry 286, no. 34 (2011): 29594–600. http://dx.doi.org/10.1074/jbc.m111.261032.

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Spinnenhirn, Valentina, Annegret Bitzer, Annette Aichem, and Marcus Groettrup. "Newly translated proteins are substrates for ubiquitin, ISG15, and FAT10." FEBS Letters 591, no. 1 (2016): 186–95. http://dx.doi.org/10.1002/1873-3468.12512.

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Um, Hyojin, Hoim Jeong, Beomgu Lee, et al. "FAT10 Induces cancer cell migration by stabilizing phosphorylated ABI3/NESH." Animal Cells and Systems 27, no. 1 (2023): 53–60. http://dx.doi.org/10.1080/19768354.2023.2186486.

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Dong, Dingxiang, Weifan Jiang, Jun Lei, et al. "Ubiquitin-like protein FAT10 promotes bladder cancer progression by stabilizing survivin." Oncotarget 7, no. 49 (2016): 81463–73. http://dx.doi.org/10.18632/oncotarget.12976.

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43

Lukasiak, S., C. Schiller, P. Oehlschlaeger, et al. "Proinflammatory cytokines cause FAT10 upregulation in cancers of liver and colon." Oncogene 27, no. 46 (2008): 6068–74. http://dx.doi.org/10.1038/onc.2008.201.

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Basler, Michael, Stefanie Buerger, and Marcus Groettrup. "The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense." Molecular Immunology 68, no. 2 (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 та ін. "IFNγ potentiates TNFα/TNFR1 signaling to induce FAT10 expression in macrophages". Molecular Immunology 117 (січень 2020): 101–9. http://dx.doi.org/10.1016/j.molimm.2019.11.004.

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Canaan, A., J. DeFuria, E. Perelman, et al. "Extended lifespan and reduced adiposity in mice lacking the FAT10 gene." Proceedings of the National Academy of Sciences 111, no. 14 (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, and Nir London. "Phenotypic Screen Identifies JAK2 as a Major Regulator of FAT10 Expression." ACS Chemical Biology 14, no. 12 (2019): 2538–45. http://dx.doi.org/10.1021/acschembio.9b00667.

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Bett, John S., Naheed Kanuga, Emma Richet, et al. "The Inherited Blindness Protein AIPL1 Regulates the Ubiquitin-Like FAT10 Pathway." PLoS ONE 7, no. 2 (2012): e30866. http://dx.doi.org/10.1371/journal.pone.0030866.

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Raasi, Shahri, Gunter Schmidtke, and Marcus Groettrup. "The Ubiquitin-like Protein FAT10 Forms Covalent Conjugates and Induces Apoptosis." Journal of Biological Chemistry 276, no. 38 (2001): 35334–43. http://dx.doi.org/10.1074/jbc.m105139200.

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Ross, Michael J., Matthew S. Wosnitzer, Michael D. Ross, et al. "Role of Ubiquitin-Like Protein FAT10 in Epithelial Apoptosis in Renal Disease." Journal of the American Society of Nephrology 17, no. 4 (2006): 996–1004. http://dx.doi.org/10.1681/asn.2005070692.

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