USP48 restrains resection by site-specific cleavage of the BRCA1 ubiquitin mark from H2A
BRCA1 ligase activity is tightly regulated to maintain genome stability and confer DNA double strand repair. Here the authors identify USP48 as a H2A deubiquitinating enzyme that acts as a BRCA1 E3 ligase antagonist and characterize its role during DNA repair.
Guardado en:
Autores principales: | Michael Uckelmann, Ruth M. Densham, Roy Baas, Herrie H. K. Winterwerp, Alexander Fish, Titia K. Sixma, Joanna R. Morris |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/1e3a338b35724ff5b4dbc88530cac69f |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Structural basis of specific H2A K13/K15 ubiquitination by RNF168
por: Velten Horn, et al.
Publicado: (2019) -
Identification of recurrent USP48 and BRAF mutations in Cushing’s disease
por: Jianhua Chen, et al.
Publicado: (2018) -
Kinetic analysis of multistep USP7 mechanism shows critical role for target protein in activity
por: Robbert Q. Kim, et al.
Publicado: (2019) -
The molecular determinants for distinguishing between ubiquitin and NEDD8 by USP2
por: Yung-Cheng Shin, et al.
Publicado: (2017) -
Map of synthetic rescue interactions for the Fanconi anemia DNA repair pathway identifies USP48
por: Georgia Velimezi, et al.
Publicado: (2018)