A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases
The E3 ligase TRIM21 targets a broad range of pathogenic proteins using a unique mechanism. Here, the authors combine structural, biochemical and cell biological approaches to elucidate how TRIM21 selectively recruits its canonical E2 partner enzyme Ube2N and catalyzes ubiquitination.
Guardado en:
Autores principales: | Leo Kiss, Jingwei Zeng, Claire F. Dickson, Donna L. Mallery, Ji-Chun Yang, Stephen H. McLaughlin, Andreas Boland, David Neuhaus, Leo C. James |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/470293ee22be4d32ba89b9430667e524 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members.
por: Jessica L Bell, et al.
Publicado: (2012) -
The ER membrane-anchored ubiquitin ligase Hrd1 is a positive regulator of T-cell immunity
por: Yuanming Xu, et al.
Publicado: (2016) -
The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3
por: Hui Song, et al.
Publicado: (2016) -
Antibody toolkit reveals N-terminally ubiquitinated substrates of UBE2W
por: Christopher W. Davies, et al.
Publicado: (2021) -
Structural Diversity of Ubiquitin E3 Ligase
por: Sachiko Toma-Fukai, et al.
Publicado: (2021)