Myb DNA binding inhibited by phosphorylation at a site deleted during oncogenic activation
- 1 April 1990
- journal article
- Published by Springer Nature in Nature
- Vol. 344 (6266), 517-522
- https://doi.org/10.1038/344517a0
Abstract
The c-Myb nuclear oncoprotein is phosphorylated in vitro and in vivo at an N-terminal site near its DNA-binding domain by casein kinase II (CK-II) or a CK-II-like activity. This in vitro phosphorylation reversibly inhibits the sequence-specific binding of c-Myb to DNA. The site of this phosphorylation is deleted in nearly all oncogenically activated Myb proteins, resulting in DNA-binding that is independent of CK-II. Because CK-II activity is modulated by growth factors, loss of the site could uncouple c-Myb from its normal physiological regulator.Keywords
This publication has 56 references indexed in Scilit:
- Autophosphorylation of the PDGF receptor in the kinase insert region regulates interactions with cell proteinsCell, 1989
- MyoD is a sequence-specific DNA binding protein requiring a region of myc homology to bind to the muscle creatine kinase enhancerCell, 1989
- DNA-binding activity of the adenovirus-induced E4F transcription factor is regulated by phosphorylation.Genes & Development, 1989
- Structural changes in glycogen phosphorylase induced by phosphorylationNature, 1988
- Viral myb oncogene encodes a sequence-specific DNA-binding activityNature, 1988
- Phosphorylation-induced binding and transcriptional efficacy of nuclear factor CREBNature, 1988
- PROTEIN SERINE/THREONINE KINASESAnnual Review of Biochemistry, 1987
- A new method for the selective isolation of phosphoserine‐containing peptidesFEBS Letters, 1987
- Sequence analysis of phosphoserine‐containing peptidesFEBS Letters, 1986
- Activation of the c- myb Locus by Viral Insertional Mutagenesis in Plasmacytoid LymphosarcomasScience, 1984