Cargando…
The CRL4(VPRBP(DCAF1)) E3 ubiquitin ligase directs constitutive RAG1 degradation in a non-lymphoid cell line
The development of B and T lymphocytes critically depends on RAG1/2 endonuclease activity to mediate antigen receptor gene assembly by V(D)J recombination. Although control of RAG1/2 activity through cell cycle- and ubiquitin-dependent degradation of RAG2 has been studied in detail, relatively littl...
Autores principales: | Schabla, N. Max, Swanson, Patrick C. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8516306/ https://www.ncbi.nlm.nih.gov/pubmed/34648572 http://dx.doi.org/10.1371/journal.pone.0258683 |
Ejemplares similares
-
DCAF1 (VprBP): emerging physiological roles for a unique dual-service E3 ubiquitin ligase substrate receptor
por: Schabla, N Max, et al.
Publicado: (2018) -
VprBP (DCAF1): a promiscuous substrate recognition subunit that incorporates into both RING-family CRL4 and HECT-family EDD/UBR5 E3 ubiquitin ligases
por: Nakagawa, Tadashi, et al.
Publicado: (2013) -
CRL4–DDB1–VPRBP ubiquitin ligase mediates the stress triggered proteolysis of Mcm10
por: Kaur, Manpreet, et al.
Publicado: (2012) -
Lentiviral Vpx Accessory Factor Targets VprBP/DCAF1 Substrate Adaptor for Cullin 4 E3 Ubiquitin Ligase to Enable Macrophage Infection
por: Srivastava, Smita, et al.
Publicado: (2008) -
The CRL4(DCAF1) cullin‐RING ubiquitin ligase is activated following a switch in oligomerization state
por: Mohamed, Weaam I, et al.
Publicado: (2021)