scholarly journals The p38 Mitogen-activated Protein Kinase Augments Nucleotide Excision Repair by Mediating DDB2 Degradation and Chromatin Relaxation

2008 ◽  
Vol 283 (47) ◽  
pp. 32553-32561 ◽  
Author(s):  
Qun Zhao ◽  
Bassant M. Barakat ◽  
Song Qin ◽  
Alo Ray ◽  
Mohamed A. El-Mahdy ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Nucleotide Excision Repair ◽  
Excision Repair ◽  
Mitogen Activated Protein Kinase ◽  
Nucleotide Excision ◽  
Mitogen Activated Protein ◽  
Chromatin Relaxation

scholarly journals Atypical protein kinase C stimulates nucleotide excision repair activity

FEBS Letters ◽  
2004 ◽  
Vol 574 (1-3) ◽  
pp. 121-125 ◽  
Author(s):  
Thierry Louat ◽  
Yvan Canitrot ◽  
Sandra Jousseaume ◽  
Caroline Baudouin ◽  
Pierre Canal ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Nucleotide Excision Repair ◽  
Excision Repair ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Kinase C ◽  
Nucleotide Excision ◽  
Repair Activity

scholarly journals MEKK1-dependent activation of the CRL4 complex is important for DNA damage-induced degradation of p21 and DDB2 and cell survival

2021 ◽  
Author(s):  
Susanne Bacher ◽  
Hilda Stekman ◽  
Carla M. Farah ◽  
Annika Karger ◽  
Michael Kracht ◽  
...  
Keyword(s):  
Dna Damage ◽  
Cell Survival ◽  
Genome Stability ◽  
Excision Repair ◽  
Mitogen Activated Protein Kinase ◽  
Protein Assemblies ◽  
Cell Recovery ◽  
Nucleotide Excision ◽  
Mitogen Activated Protein ◽  
Cycle Regulation

Cullin-4 ubiquitin ligase (CRL4) complexes are differentially composed and highly dynamic protein assemblies that control many biological processes including the global genome nucleotide excision repair (GG-NER) pathway. Here we identified the kinase mitogen-activated protein kinase kinase kinase 1 (MEKK1) as a novel constitutive interactor of a cytosolic CRL4 complex that disassembles after DNA damage due to the Caspase-mediated cleavage of MEKK1. The kinase activity of MEKK1 was important to trigger auto-ubiquitination of the CRL4 complex by K48- and K63-linked ubiquitin chains. MEKK1 knockdown prohibited DNA damage-induced degradation of the CRL4 component DNA-damage binding protein 2 (DDB2) and the CRL4 substrate p21 and also cell recovery and survival. A ubiquitin replacement strategy revealed a contribution of K63-branched ubiquitin chains for DNA damage-induced DDB2/p21 decay, cell cycle regulation and cell survival. These data might have also implications for cancer, as frequently occurring mutations of MEKK1 might have an impact on genome stability and the therapeutic efficacy of CRL4-dependent immunomodulatory drugs such as thalidomide-derivatives.

scholarly journals UV sensitivity and impaired nucleotide excision repair in DNA-dependent protein kinase mutant cells

1998 ◽  
Vol 26 (6) ◽  
pp. 1382-1389 ◽  
Author(s):  
C. Muller ◽  
P. Calsou ◽  
P. Frit ◽  
B. Salles ◽  
C. Cayrol ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Nucleotide Excision Repair ◽  
Excision Repair ◽  
Dependent Protein Kinase ◽  
Uv Sensitivity ◽  
Nucleotide Excision ◽  
Dependent Protein ◽  
Mutant Cells
Sign in / Sign up

Export Citation Format

Share Document