Cargando…
Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4
The small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and stress response. The SUMO-targeted ubiquitin ligase RNF4 engages with SUMO chains on linked substrates and catalyses their ubiquitination, which...
Autores principales: | Xu, Yingqi, Plechanovová, Anna, Simpson, Peter, Marchant, Jan, Leidecker, Orsolya, Kraatz, Sebastian, Hay, Ronald T., Matthews, Steve J. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Pub. Group
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4083429/ https://www.ncbi.nlm.nih.gov/pubmed/24969970 http://dx.doi.org/10.1038/ncomms5217 |
Ejemplares similares
-
SUMO Chain-Induced Dimerization Activates RNF4
por: Rojas-Fernandez, Alejandro, et al.
Publicado: (2014) -
Arkadia/RNF111 is a SUMO-targeted ubiquitin ligase with preference for substrates marked with SUMO1-capped SUMO2/3 chain
por: Sriramachandran, Annie M., et al.
Publicado: (2019) -
Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer
por: Murphy, Paul, et al.
Publicado: (2020) -
Antagonistic roles of ubiquitin ligase HEI10 and SUMO ligase RNF212 regulate meiotic recombination
por: Qiao, Huanyu, et al.
Publicado: (2014) -
RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response
por: Poulsen, Sara L., et al.
Publicado: (2013)