Cargando…
Dephosphorylation of DBC1 by Protein Phosphatase 4 Is Important for p53-Mediated Cellular Functions
Deleted in breast cancer-1 (DBC1) contributes to the regulation of cell survival and apoptosis. Recent studies demonstrated that DBC is phosphorylated at Thr454 by ATM/ATR kinases in response to DNA damage, which is a critical event for p53 activation and apoptosis. However, how DBC1 phosphorylation...
Autores principales: | Lee, Jihye, Adelmant, Guillaume, Marto, Jarrod A., Lee, Dong-Hyun |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Korean Society for Molecular and Cellular Biology
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4546941/ https://www.ncbi.nlm.nih.gov/pubmed/26194823 http://dx.doi.org/10.14348/molcells.2015.0066 |
Ejemplares similares
-
Interaction of DBC1 with polyoma small T antigen promotes its degradation and negatively regulates tumorigenesis
por: Sarwar, Zarka, et al.
Publicado: (2021) -
DBC1 Functions as a Tumor Suppressor by Regulating p53 Stability
por: Qin, Bo, et al.
Publicado: (2015) -
Protein phosphatase 4 dephosphorylates phosphofructokinase-1 to regulate its enzymatic activity
por: Park, Jaehong, et al.
Publicado: (2023) -
DBC1 Regulates p53 Stability via Inhibition of CBP-Dependent p53 Polyubiquitination
por: Akande, Oluwatoyin E., et al.
Publicado: (2019) -
Dual-specificity phosphatase 23 mediates GCM1 dephosphorylation and activation
por: Lin, Fang-Yu, et al.
Publicado: (2011)