Cargando…
Chk1 KA1 domain auto-phosphorylation stimulates biological activity and is linked to rapid proteasomal degradation
The DNA damage-activated protein kinase Chk1 is known to undergo auto-phosphorylation, however the sites and functional significance of this modification remain poorly understood. We have identified two novel Chk1 auto-phosphorylation sites, threonines 378 and 382 (T378/382), located in a highly con...
Autores principales: | Gong, Eun-Yeung, Hernández, Beatriz, Nielsen, Jessica Hernández, Smits, Veronique A. J., Freire, Raimundo, Gillespie, David A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6277497/ https://www.ncbi.nlm.nih.gov/pubmed/30510197 http://dx.doi.org/10.1038/s41598-018-35616-9 |
Ejemplares similares
-
KA1-targeted regulatory domain mutations activate Chk1 in the absence of DNA damage
por: Gong, Eun-Yeung, et al.
Publicado: (2015) -
Chk1 C-terminal regulatory phosphorylation mediates checkpoint activation via derepression of Chk1 catalytic activity
por: Walker, M, et al.
Publicado: (2009) -
PRP4KA phosphorylates SERRATE for degradation via 20S proteasome to fine-tune miRNA production in Arabidopsis
por: Wang, Lin, et al.
Publicado: (2022) -
USP1 deubiquitinase maintains phosphorylated CHK1 by limiting its DDB1-dependent degradation
por: Guervilly, Jean-Hugues, et al.
Publicado: (2011) -
Hornerin mediates phosphorylation of the polo-box domain in Plk1 by Chk1 to induce death in mitosis
por: Song, Haiyu, et al.
Publicado: (2023)