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Identification of a CK2 phosphorylation site in mdm2.
Open accessAbstract
Mdm2 is a cellular oncoprotein the most obvious function of which is the down‐regulation of the growth suppressor protein p53. It represents a highly phosphorylated protein but only little is yet known about the sites phosphorylated in vivo, the kinases that are responsible for the phosphorylation or the functional relevance of the phosphorylation status. Recently, we have shown that mdm2 is a good substrate for protein kinase CK2 at least in vitro. Computer analysis of the primary amino acid sequence of mdm2 revealed 19 putative CK2 phosphorylation sites. By using deletion mutants of mdm2 and a peptide library we identified the serine residue at position 269 which lies within a canonical CK2 consensus sequence (EGQEL S DEDDE) as the most important CK2 phosphorylation site. Moreover, by using the mdm2 S269A mutant for in vitro phosphorylation assays this site was shown to be phosphorylated by CK2. Binding studies revealed that phosphorylation of mdm2 at S269 does not have any influence on the binding of p53 to mdm2.
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References 56 · Cited by 39
Metadata
- Authors
- Götz, C., Kartarius, S., Scholtes, P., Nastainczyk, W., & Montenarh, M.
- Affiliations
- Saarland University (DE)
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1999-12
- Volume
- 266
- Issue
- 2
- Pages
- 493-501
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W2039556757
- Cited by
- 39
- References
- 56
- Citations by year
- 2022: 1 · 2021: 1 · 2020: 2 · 2019: 1 · 2018: 1 · 2013: 3
- FWCI
- 1.10
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- European Journal of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- MDM2, casein kinase 2, p53, protein phosphorylation, peptide library screening
- MeSH terms
- Amino Acid Sequence, Animals, Binding Sites, Cell Line, Codon, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Humans, Insecta, Molecular Sequence Data, Mutation, Nuclear Proteins, Peptides, Phosphorylation, Plasmids, Protein Binding, Proto-Oncogene Proteins, Recombinant Proteins, Blotting, Western, Tumor Suppressor Protein p53, Protein Serine-Threonine Kinases, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Casein Kinase II, Proto-Oncogene Proteins c-mdm2
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