PMID- 10606744
OWN - NLM
STAT- MEDLINE
DCOM- 20000119
LR  - 20190621
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 463
IP  - 3
DP  - 1999 Dec 17
TI  - Protein kinase CK1 is a p53-threonine 18 kinase which requires prior
      phosphorylation of serine 15.
PG  - 312-6
AB  - p53 is a potent transcription factor which is regulated by sequential multisite
      phosphorylation and acetylation. In this paper, we identify threonine 18 of p53, 
      a key site in regulating the interaction between p53 and its regulatory partner
      MDM2, as a novel site phosphorylated in vitro by purified recombinant casein
      kinase 1 (CK1) delta. Strikingly, phosphorylation of threonine 18 is dependent
      upon prior phosphorylation of serine 15. These data highlight an additional and
      physiologically important target residue for CK1 in p53 and suggest a potential
      mechanism by which sequential modification of a pivotal N-terminal residue in p53
      may occur following stress-activated modification of serine 15.
FAU - Dumaz, N
AU  - Dumaz N
AD  - Biomedical Research Centre, Ninewells Hospital and Medical School, Dundee, UK.
FAU - Milne, D M
AU  - Milne DM
FAU - Meek, D W
AU  - Meek DW
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Isoenzymes)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Tumor Suppressor Protein p53)
RN  - 2ZD004190S (Threonine)
RN  - 452VLY9402 (Serine)
RN  - EC 2.5.1.18 (Glutathione Transferase)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.11.1 (Casein Kinases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Casein Kinases
MH  - DNA Damage
MH  - Glutathione Transferase/chemistry
MH  - Humans
MH  - Isoenzymes/metabolism
MH  - Molecular Sequence Data
MH  - Phosphorylation
MH  - Protein Kinases/*metabolism
MH  - Recombinant Fusion Proteins/biosynthesis/chemistry
MH  - Sequence Alignment
MH  - Serine/chemistry
MH  - Substrate Specificity
MH  - Threonine/chemistry
MH  - Tumor Suppressor Protein p53/chemistry/genetics/*metabolism
EDAT- 1999/12/22 00:00
MHDA- 1999/12/22 00:01
CRDT- 1999/12/22 00:00
PHST- 1999/12/22 00:00 [pubmed]
PHST- 1999/12/22 00:01 [medline]
PHST- 1999/12/22 00:00 [entrez]
AID - S0014-5793(99)01647-6 [pii]
AID - 10.1016/s0014-5793(99)01647-6 [doi]
PST - ppublish
SO  - FEBS Lett. 1999 Dec 17;463(3):312-6. doi: 10.1016/s0014-5793(99)01647-6.