Cargando…
SAMHD1 Phosphorylation at T592 Regulates Cellular Localization and S-phase Progression
SAMHD1 activity is regulated by a network of mechanisms including phosphorylation, oxidation, oligomerization, and others. Significant questions remain about the effects of phosphorylation on SAMHD1 function and activity. We investigated the effects of a SAMHD1 T592E phosphorylation mimic on its cel...
Autores principales: | Batalis, Stephanie, Rogers, LeAnn C., Hemphill, Wayne O., Mauney, Christopher H., Ornelles, David A., Hollis, Thomas |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8426622/ https://www.ncbi.nlm.nih.gov/pubmed/34513928 http://dx.doi.org/10.3389/fmolb.2021.724870 |
Ejemplares similares
-
Protein oxidation increases SAMHD1 binding ssDNA via its regulatory site
por: Simermeyer, Theresa L, et al.
Publicado: (2023) -
The dNTP triphosphohydrolase activity of SAMHD1 persists during S-phase when the enzyme is phosphorylated at T592
por: Tramentozzi, Elisa, et al.
Publicado: (2018) -
A Novel Identified Long Non-coding RNA, lncRNA MEF2C-AS1, Inhibits Cervical Cancer via Regulation of miR-592/RSPO1
por: Wang, Xiaoping, et al.
Publicado: (2021) -
Phosphorylation of SAMHD1 Thr592 increases C-terminal domain dynamics, tetramer dissociation and ssDNA binding kinetics
por: Orris, Benjamin, et al.
Publicado: (2022) -
Phosphorylation Regulates CIRBP Arginine Methylation, Transportin-1 Binding and Liquid-Liquid Phase Separation
por: Lenard, Aneta J., et al.
Publicado: (2021)