BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling
The K63-linkage specific deubiquitinase BRCC36 forms the core of two multi-subunit deubiquitination complexes: BRCA1-A and BRISC. BRCA1-A is recruited to DNA repair <i>foci</i>, edits ubiquitin signals on chromatin, and sequesters BRCA1 away from the site of damage, suppressing homologou...
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| Formato: | Artigo |
| Idioma: | English |
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MDPI AG
2020-10-01
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| Colecção: | Biomolecules |
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| Acesso em linha: | https://www.mdpi.com/2218-273X/10/11/1503 |
| _version_ | 1827703074064433152 |
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| author | Julius Rabl |
| author_facet | Julius Rabl |
| author_sort | Julius Rabl |
| collection | DOAJ |
| description | The K63-linkage specific deubiquitinase BRCC36 forms the core of two multi-subunit deubiquitination complexes: BRCA1-A and BRISC. BRCA1-A is recruited to DNA repair <i>foci</i>, edits ubiquitin signals on chromatin, and sequesters BRCA1 away from the site of damage, suppressing homologous recombination by limiting resection. BRISC forms a complex with metabolic enzyme SHMT2 and regulates the immune response, mitosis, and hematopoiesis. Almost two decades of research have revealed how BRCA1-A and BRISC use the same core of subunits to perform very distinct biological tasks. |
| first_indexed | 2024-03-10T15:11:19Z |
| format | Article |
| id | doaj.art-cca7747870ab4c5dbf372af1978c6158 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T15:11:19Z |
| publishDate | 2020-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-cca7747870ab4c5dbf372af1978c61582023-11-20T19:22:07ZengMDPI AGBiomolecules2218-273X2020-10-011011150310.3390/biom10111503BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin SignalingJulius Rabl0Cryo-EM Knowledge Hub, ETH Zürich, Otto-Stern-Weg 3, HPM C51, 8093 Zürich, SwitzerlandThe K63-linkage specific deubiquitinase BRCC36 forms the core of two multi-subunit deubiquitination complexes: BRCA1-A and BRISC. BRCA1-A is recruited to DNA repair <i>foci</i>, edits ubiquitin signals on chromatin, and sequesters BRCA1 away from the site of damage, suppressing homologous recombination by limiting resection. BRISC forms a complex with metabolic enzyme SHMT2 and regulates the immune response, mitosis, and hematopoiesis. Almost two decades of research have revealed how BRCA1-A and BRISC use the same core of subunits to perform very distinct biological tasks.https://www.mdpi.com/2218-273X/10/11/1503deubiquitinationBRCA1DNA repairimmune regulationBRCC36SHMT2 |
| spellingShingle | Julius Rabl BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling Biomolecules deubiquitination BRCA1 DNA repair immune regulation BRCC36 SHMT2 |
| title | BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling |
| title_full | BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling |
| title_fullStr | BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling |
| title_full_unstemmed | BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling |
| title_short | BRCA1-A and BRISC: Multifunctional Molecular Machines for Ubiquitin Signaling |
| title_sort | brca1 a and brisc multifunctional molecular machines for ubiquitin signaling |
| topic | deubiquitination BRCA1 DNA repair immune regulation BRCC36 SHMT2 |
| url | https://www.mdpi.com/2218-273X/10/11/1503 |
| work_keys_str_mv | AT juliusrabl brca1aandbriscmultifunctionalmolecularmachinesforubiquitinsignaling |