The BCR-ABL oncoprotein potentially interacts with the xeroderma pigmentosum group B protein
AUTOR(ES)
Takeda, Norifumi
FONTE
The National Academy of Sciences
RESUMO
The previously uncharacterized CDC24 homology domain of BCR, which is missing in the P185 BCR-ABL oncogene of Philadelphia chromosome (Ph1)-positive acute lymphocytic leukemia but is retained in P210 BCR-ABL of chronic myelogeneous leukemia, was found to bind to the xeroderma pigmentosum group B protein (XPB). The binding appeared to be required for XPB to be tyrosine-phosphorylated by BCR-ABL. The interaction not only reduced both the ATPase and the helicase activities of XPB purified in the baculovirus system but also impaired XPB-mediated cross-complementation of the repair deficiency in rodent UV-sensitive mutants of group 3. The persistent dysfunction of XPB may in part underlie genomic instability in blastic crisis.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=15117Documentos Relacionados
- Protein Tyrosine Phosphatase 1B Antagonizes Signalling by Oncoprotein Tyrosine Kinase p210 bcr-abl In Vivo
- A temperature sensitive p210 BCR-ABL mutant defines the primary consequences of BCR-ABL tyrosine kinase expression in growth factor dependent cells.
- Relação entre o oncogene BCR-ABL e os receptores de tipo TOLL (TLR).
- An actin-binding function contributes to transformation by the Bcr-Abl oncoprotein of Philadelphia chromosome-positive human leukemias.
- The BCR-ABL oncogene transforms Rat-1 cells and cooperates with v-myc.