From <i>Drosophila</i> to Human: Biological Function of E3 Ligase Godzilla and Its Role in Disease
The ubiquitin–proteasome system is of fundamental importance in all fields of biology due to its impact on proteostasis and in regulating cellular processes. Ubiquitination, a type of protein post-translational modification, involves complex enzymatic machinery, such as E3 ubiquitin ligases. The E3...
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| Format: | Article |
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MDPI AG
2022-01-01
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| Series: | Cells |
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| Online Access: | https://www.mdpi.com/2073-4409/11/3/380 |
| _version_ | 1797488592275111936 |
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| author | Valérie C. Cabana Marc P. Lussier |
| author_facet | Valérie C. Cabana Marc P. Lussier |
| author_sort | Valérie C. Cabana |
| collection | DOAJ |
| description | The ubiquitin–proteasome system is of fundamental importance in all fields of biology due to its impact on proteostasis and in regulating cellular processes. Ubiquitination, a type of protein post-translational modification, involves complex enzymatic machinery, such as E3 ubiquitin ligases. The E3 ligases regulate the covalent attachment of ubiquitin to a target protein and are involved in various cellular mechanisms, including the cell cycle, cell division, endoplasmic reticulum stress, and neurotransmission. Because the E3 ligases regulate so many physiological events, they are also associated with pathologic conditions, such as cancer, neurological disorders, and immune-related diseases. This review focuses specifically on the protease-associated transmembrane-containing the Really Interesting New Gene (RING) subset of E3 ligases. We describe the structure, partners, and physiological functions of the <i>Drosophila</i> Godzilla E3 ligase and its human homologues, RNF13, RNF167, and ZNRF4. Also, we summarize the information that has emerged during the last decade regarding the association of these E3 ligases with pathophysiological conditions, such as cancer, asthma, and rare genetic disorders. We conclude by highlighting the limitations of the current knowledge and pinpointing the unresolved questions relevant to RNF13, RNF167, and ZNRF4 ubiquitin ligases. |
| first_indexed | 2024-03-10T00:04:29Z |
| format | Article |
| id | doaj.art-97ac01d6e3264293bd10cecafbb8f712 |
| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2024-03-10T00:04:29Z |
| publishDate | 2022-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cells |
| spelling | doaj.art-97ac01d6e3264293bd10cecafbb8f7122023-11-23T16:10:55ZengMDPI AGCells2073-44092022-01-0111338010.3390/cells11030380From <i>Drosophila</i> to Human: Biological Function of E3 Ligase Godzilla and Its Role in DiseaseValérie C. Cabana0Marc P. Lussier1Département de Chimie, Université du Québec à Montréal, Montréal, QC H2X 2J6, CanadaDépartement de Chimie, Université du Québec à Montréal, Montréal, QC H2X 2J6, CanadaThe ubiquitin–proteasome system is of fundamental importance in all fields of biology due to its impact on proteostasis and in regulating cellular processes. Ubiquitination, a type of protein post-translational modification, involves complex enzymatic machinery, such as E3 ubiquitin ligases. The E3 ligases regulate the covalent attachment of ubiquitin to a target protein and are involved in various cellular mechanisms, including the cell cycle, cell division, endoplasmic reticulum stress, and neurotransmission. Because the E3 ligases regulate so many physiological events, they are also associated with pathologic conditions, such as cancer, neurological disorders, and immune-related diseases. This review focuses specifically on the protease-associated transmembrane-containing the Really Interesting New Gene (RING) subset of E3 ligases. We describe the structure, partners, and physiological functions of the <i>Drosophila</i> Godzilla E3 ligase and its human homologues, RNF13, RNF167, and ZNRF4. Also, we summarize the information that has emerged during the last decade regarding the association of these E3 ligases with pathophysiological conditions, such as cancer, asthma, and rare genetic disorders. We conclude by highlighting the limitations of the current knowledge and pinpointing the unresolved questions relevant to RNF13, RNF167, and ZNRF4 ubiquitin ligases.https://www.mdpi.com/2073-4409/11/3/380ubiquitinGodzillaRNF13RNF167ZNRF4pathological dysfunction |
| spellingShingle | Valérie C. Cabana Marc P. Lussier From <i>Drosophila</i> to Human: Biological Function of E3 Ligase Godzilla and Its Role in Disease Cells ubiquitin Godzilla RNF13 RNF167 ZNRF4 pathological dysfunction |
| title | From <i>Drosophila</i> to Human: Biological Function of E3 Ligase Godzilla and Its Role in Disease |
| title_full | From <i>Drosophila</i> to Human: Biological Function of E3 Ligase Godzilla and Its Role in Disease |
| title_fullStr | From <i>Drosophila</i> to Human: Biological Function of E3 Ligase Godzilla and Its Role in Disease |
| title_full_unstemmed | From <i>Drosophila</i> to Human: Biological Function of E3 Ligase Godzilla and Its Role in Disease |
| title_short | From <i>Drosophila</i> to Human: Biological Function of E3 Ligase Godzilla and Its Role in Disease |
| title_sort | from i drosophila i to human biological function of e3 ligase godzilla and its role in disease |
| topic | ubiquitin Godzilla RNF13 RNF167 ZNRF4 pathological dysfunction |
| url | https://www.mdpi.com/2073-4409/11/3/380 |
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