PMID- 10644693
OWN - NLM
STAT- MEDLINE
DCOM- 20000229
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 4
DP  - 2000 Jan 28
TI  - The human Cdc14 phosphatases interact with and dephosphorylate the tumor
      suppressor protein p53.
PG  - 2410-4
AB  - The yeast Cdc14 phosphatase has been shown to play an important role in cell
      cycle regulation by dephosphorylating proteins phosphorylated by the
      cyclin-dependent kinase Cdc28/clb. We recently cloned two human orthologs of the 
      yeast CDC14, termed hCDC14A and -B, the gene products of which share
      approximately 80% amino acid sequence identity within their N termini and
      phosphatase domains. Here we report that the hCdc14A and hCdc14B proteins
      interact with the tumor suppressor protein p53 both in vitro and in vivo. This
      interaction is dependent on the N termini of the hCdc14 proteins and the C
      terminus of p53. Furthermore, the hCdc14 phosphatases were found to
      dephosphorylate p53 specifically at the p34(Cdc2)/clb phosphorylation site
      (p53-phosphor-Ser(315)). Our findings that hCdc14 is a cyclin-dependent kinase
      substrate phosphatase suggest that it may play a role in cell cycle control in
      human cells. Furthermore, the identification of p53 as a substrate for hCdc14
      indicates that hCdc14 may regulate the function of p53.
FAU - Li, L
AU  - Li L
AD  - Department of Medicine, Wake Forest University School of Medicine, Winston-Salem,
      North Carolina 27157, USA. lwli@wfubmc.edu
FAU - Ljungman, M
AU  - Ljungman M
FAU - Dixon, J E
AU  - Dixon JE
LA  - eng
GR  - CA09676/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (CDC14 protein, S cerevisiae)
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Fungal Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Tumor Suppressor Protein p53)
RN  - 452VLY9402 (Serine)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
SB  - IM
MH  - Cell Cycle Proteins/*metabolism
MH  - Fungal Proteins/*metabolism
MH  - Humans
MH  - Phosphorylation
MH  - Protein Binding
MH  - *Protein Tyrosine Phosphatases
MH  - Saccharomyces cerevisiae/metabolism
MH  - *Saccharomyces cerevisiae Proteins
MH  - Serine/metabolism
MH  - Tumor Suppressor Protein p53/chemistry/*metabolism
EDAT- 2000/01/25 09:00
MHDA- 2000/03/04 09:00
CRDT- 2000/01/25 09:00
PHST- 2000/01/25 09:00 [pubmed]
PHST- 2000/03/04 09:00 [medline]
PHST- 2000/01/25 09:00 [entrez]
AID - 10.1074/jbc.275.4.2410 [doi]
PST - ppublish
SO  - J Biol Chem. 2000 Jan 28;275(4):2410-4. doi: 10.1074/jbc.275.4.2410.