scholarly journals Phosphorylation of linker histones by DNA-dependent protein kinase is required for DNA ligase IV-dependent ligation in the presence of histone H1

2005 ◽  
Vol 102 (6) ◽  
pp. 1877-1882 ◽  
Author(s):  
B. Kysela ◽  
M. Chovanec ◽  
P. A. Jeggo
Keyword(s):  
Protein Kinase ◽  
Histone H1 ◽  
Dna Ligase ◽  
Dependent Protein Kinase ◽  
Linker Histones ◽  
Dna Ligase Iv ◽  
Ligase Iv ◽  
Dependent Protein

scholarly journals Phosphorylation and Regulation of DNA Ligase IV Stability by DNA-dependent Protein Kinase

2004 ◽  
Vol 279 (36) ◽  
pp. 37282-37290 ◽  
Author(s):  
Yu-Gang Wang ◽  
Chinonye Nnakwe ◽  
William S. Lane ◽  
Mauro Modesti ◽  
Karen M. Frank
Keyword(s):  
Protein Kinase ◽  
Dna Ligase ◽  
Dependent Protein Kinase ◽  
Dna Ligase Iv ◽  
Ligase Iv ◽  
Dependent Protein

scholarly journals DNA-dependent Protein Kinase and XRCC4-DNA Ligase IV Mobilization in the Cell in Response to DNA Double Strand Breaks

2004 ◽  
Vol 280 (8) ◽  
pp. 7060-7069 ◽  
Author(s):  
Jérôme Drouet ◽  
Christine Delteil ◽  
Jacques Lefrançois ◽  
Patrick Concannon ◽  
Bernard Salles ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Double Strand Breaks ◽  
Dna Ligase ◽  
Dna Double Strand Breaks ◽  
Dependent Protein Kinase ◽  
Strand Breaks ◽  
Dna Ligase Iv ◽  
Ligase Iv ◽  
Dependent Protein

scholarly journals Interactions of the DNA Ligase IV-XRCC4 Complex with DNA Ends and the DNA-dependent Protein Kinase

2000 ◽  
Vol 275 (34) ◽  
pp. 26196-26205 ◽  
Author(s):  
Ling Chen ◽  
Kelly Trujillo ◽  
Patrick Sung ◽  
Alan E. Tomkinson
Keyword(s):  
Protein Kinase ◽  
Dna Ligase ◽  
Dependent Protein Kinase ◽  
Dna Ligase Iv ◽  
Ligase Iv ◽  
Dependent Protein ◽  
Dna Ends

Coordinated Assembly of Ku and p460 Subunits of the DNA-dependent Protein Kinase on DNA Ends is Necessary for XRCC4–ligase IV Recruitment

2003 ◽  
Vol 326 (1) ◽  
pp. 93-103 ◽  
Author(s):  
Patrick Calsou ◽  
Christine Delteil ◽  
Philippe Frit ◽  
Jérôme Drouet ◽  
Bernard Salles
Keyword(s):  
Protein Kinase ◽  
Dependent Protein Kinase ◽  
Ligase Iv ◽  
Dependent Protein ◽  
Dna Ends

scholarly journals DNA-Ligase IV and DNA-Protein Kinase Play a Critical Role in Deficient Caspases Activation in Apoptosis-resistant Cancer Cells by Using Doxorubicin

2008 ◽  
Vol 19 (8) ◽  
pp. 3283-3289 ◽  
Author(s):  
Claudia Friesen ◽  
Miriam Uhl ◽  
Ulrich Pannicke ◽  
Klaus Schwarz ◽  
Erich Miltner ◽  
...  
Keyword(s):  
Dna Damage ◽  
Protein Kinase ◽  
Cancer Cells ◽  
Critical Role ◽  
Dna Ligase ◽  
Apoptosis Resistance ◽  
Dsb Repair ◽  
Doxorubicin Treatment ◽  
Dna Ligase Iv ◽  
Ligase Iv

Resistance toward cytotoxic drugs is one of the primary causes for therapeutic failure in cancer therapy. DNA repair mechanisms as well as deficient caspases activation play a critical role in apoptosis resistance of tumor cells toward anticancer drug treatment. Here, we discovered that deficient caspases activation in apoptosis-resistant cancer cells depends on DNA-ligase IV and DNA-protein kinase (DNA-PK), playing crucial roles in the nonhomologous end joining (NHEJ) pathway, which is the predominant pathway for DNA double-strand break repair (DNA-DSB-repair) in mammalian cells. DNA-PK(+/+) as well as DNA-ligase IV (+/+) cancer cells were apoptosis resistant and deficient in activation of caspase-3, caspase-9, and caspase-8 and in cleavage of poly(ADP-ribose) polymerase after doxorubicin treatment. Inhibition of NHEJ by knocking out DNA-PK or DNA-ligase IV restored caspases activation and apoptosis sensitivity after doxorubicin treatment. In addition, inhibition of caspases activation prevented doxorubicin-induced apoptosis but could not prevent doxorubicin-induced DNA damage, indicating that induction of DNA damage is independent of caspases activation. However, caspases activation depends on induction of DNA damage left unrepaired by NHEJ-DNA-DSB-repair. We conclude that DNA damage left unrepaired by DNA-ligase IV or DNA-PK might be the initiator for caspases activation by doxorubicin in cancer cells. Failure in caspases activation using doxorubicin depends on loss of DNA damage and is due to higher rates of NHEJ-DNA-DBS-repair.

scholarly journals Properties of a microtubule-associated cofactor-independent protein kinase from pig brain

1989 ◽  
Vol 263 (1) ◽  
pp. 207-214 ◽  
Author(s):  
C W Scott ◽  
C B Caputo ◽  
A I Salama
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Histone H1 ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Protein Kinase Activity ◽  
Dependent Protein Kinase ◽  
Pig Brain ◽  
Dependent Protein ◽  
Independent Protein

A protein kinase activity was identified in pig brain that co-purified with microtubules through repeated cycles of temperature-dependent assembly and disassembly. The microtubule-associated protein kinase (MTAK) phosphorylated histone H1; this activity was not stimulated by cyclic nucleotides. Ca2+ plus calmodulin, phospholipids or polyamines. MTAK did not phosphorylate synthetic peptides which are substrates for cyclic AMP-dependent protein kinase, cyclic GMP-dependent protein kinase. Ca2+/calmodulin-dependent protein kinase II, protein kinase C or casein kinase II. MTAK activity was inhibited by trifluoperazine [IC50 (median inhibitory concn.) = 600 microM] in a Ca2+-independent fashion. Ca2+ alone was inhibitory [IC50 = 4 mM). MTAK was not inhibited by heparin, a potent inhibitor of casein kinase II, nor a synthetic peptide inhibitor of cyclic AMP-dependent protein kinase. MTAK demonstrated a broad pH maximum (7.5-8.5) and an apparent Km for ATP of 45 microM. Mg2+ was required for enzyme activity and could not be replaced by Mn2+. MTAK phosphorylated serine and threonine residues on histone H1. MTAK is a unique cofactor-independent protein kinase that binds to microtubule structures.

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