Cargando…
Phosphorylated (pT371)TRF1 is recruited to sites of DNA damage to facilitate homologous recombination and checkpoint activation
TRF1, a duplex telomeric DNA-binding protein, plays an important role in telomere metabolism. We have previously reported that a fraction of endogenous TRF1 can stably exist free of telomere chromatin when it is phosphorylated at T371 by Cdk1; however, the role of this telomere-free (pT371)TRF1 has...
Autores principales: | McKerlie, Megan, Walker, John R., Mitchell, Taylor R. H., Wilson, Florence R., Zhu, Xu-Dong |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3905873/ https://www.ncbi.nlm.nih.gov/pubmed/23997120 http://dx.doi.org/10.1093/nar/gkt775 |
Ejemplares similares
-
ATM regulates proteasome-dependent subnuclear localization of TRF1, which is important for telomere maintenance
por: McKerlie, Megan, et al.
Publicado: (2012) -
TRF2-mediated ORC recruitment underlies telomere stability upon DNA replication stress
por: Higa, Mitsunori, et al.
Publicado: (2021) -
CDK-mediated RNF4 phosphorylation regulates homologous recombination in S-phase
por: Luo, Kuntian, et al.
Publicado: (2015) -
A phosphorylation-and-ubiquitylation circuitry driving ATR activation and homologous recombination
por: Dubois, Jean-Christophe, et al.
Publicado: (2017) -
Phosphorylation of TRF2 promotes its interaction with TIN2 and regulates DNA damage response at telomeres
por: Storchova, Radka, et al.
Publicado: (2023)