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DNA-dependent protein kinase-mediated phosphorylation of protein kinase B requires a specific recognition sequence in the C-terminal hydrophobic motif.

Artikel i vetenskaplig tidskrift
Författare Jongsun Park
Jianhua Feng
Yuwen Li
Ola Hammarsten
Derek P Brazil
Brian A Hemmings
Publicerad i The Journal of biological chemistry
Volym 284
Nummer/häfte 10
Sidor 6169-74
ISSN 0021-9258
Publiceringsår 2009
Publicerad vid Institutionen för biomedicin, avdelningen för klinisk kemi och transfusionsmedicin
Sidor 6169-74
Språk en
Länkar dx.doi.org/10.1074/jbc.C800210200
Ämnesord Animals, Cell Line, Tumor, DNA Breaks, Double-Stranded, DNA Repair, physiology, DNA-Activated Protein Kinase, genetics, metabolism, DNA-Binding Proteins, genetics, metabolism, Humans, Mice, Mice, Knockout, Nuclear Proteins, genetics, metabolism, Peptides, genetics, metabolism, Phosphorylation, physiology, Proto-Oncogene Proteins c-akt, genetics, metabolism, Signal Transduction, physiology, Somatic Hypermutation, Immunoglobulin, physiology, Substrate Specificity, physiology, Tumor Suppressor Protein p53, genetics, metabolism
Ämneskategorier Biofarmaci

Sammanfattning

DNA-dependent protein kinase (DNA-PK) has been implicated in a variety of nuclear processes including DNA double strand break repair, V(D)J recombination, and transcription. A recent study showed that DNA-PK is responsible for Ser-473 phosphorylation in the hydrophobic motif of protein kinase B (PKB/Akt) in genotoxic-stressed cells, suggesting a novel role for DNA-PK in cell signaling. Here, we report that DNA-PK activity toward PKB peptides is impaired in DNA-PK knock-out mouse embryonic fibroblast cells when compared with wild type. In addition, human glioblastoma cells expressing a mutant form of DNA-PK (M059J) displayed a lower DNA-PK activity when compared with glioblastoma cells expressing wild-type DNA-PK (M059K) when PKB peptide substrates were tested. DNA-PK preferentially phosphorylated PKB on Ser-473 when compared with its known in vitro substrate, p53. A consensus hydrophobic amino acid surrounding the Ser-473 phospho-acceptor site in PKB containing amino acids Phe at position +1 and +4 and Tyr at position -1 are critical for DNA-PK activity. Thus, these data define the specificity of DNA-PK action as a Ser-473 kinase for PKB in DNA repair signaling.

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