Abstract
Cdc25C phosphatase induces mitosis by dephosphorylating and activating Cdc2/cyclin B protein kinase. Phosphorylation of Xenopus Cdc25C at serine 287 creates a binding site for a 14-3-3 protein and restrains activation during interphase. Here, we show that dephosphorylation of S287 is catalysed by protein phosphatase-2A in Xenopus egg extracts. 14-3-3 protein binding to Cdc25C inhibits dephosphorylation of S287, providing a mechanism to maintain phosphorylation of that site during interphase. The rate of dephosphorylation of S287 is not increased in mitotic extracts, indicating that the phosphorylation status of the site is likely to be controlled through modulation of kinases or 14-3-3 binding activity.
| Original language | English |
|---|---|
| Pages (from-to) | 267-271 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 528 |
| Issue number | 1-3 |
| DOIs | |
| Publication status | Published - 25 Sep 2002 |
Fingerprint
Keywords
- 14-3-3 protein
- Cdc25
- Cell cycle checkpoint
- Chk1
- Protein phosphatase
Cite this
}
Dephosphorylation of the inhibitory phosphorylation site S287 in Xenopus Cdc25C by protein phosphatase-2A is inhibited by 14-3-3 binding. / Hutchins, James R.A.; Dikovskaya, Dina; Clarke, Paul R.
In: FEBS Letters, Vol. 528, No. 1-3, 25.09.2002, p. 267-271.Research output: Contribution to journal › Article
TY - JOUR
T1 - Dephosphorylation of the inhibitory phosphorylation site S287 in Xenopus Cdc25C by protein phosphatase-2A is inhibited by 14-3-3 binding
AU - Hutchins, James R.A.
AU - Dikovskaya, Dina
AU - Clarke, Paul R.
PY - 2002/9/25
Y1 - 2002/9/25
N2 - Cdc25C phosphatase induces mitosis by dephosphorylating and activating Cdc2/cyclin B protein kinase. Phosphorylation of Xenopus Cdc25C at serine 287 creates a binding site for a 14-3-3 protein and restrains activation during interphase. Here, we show that dephosphorylation of S287 is catalysed by protein phosphatase-2A in Xenopus egg extracts. 14-3-3 protein binding to Cdc25C inhibits dephosphorylation of S287, providing a mechanism to maintain phosphorylation of that site during interphase. The rate of dephosphorylation of S287 is not increased in mitotic extracts, indicating that the phosphorylation status of the site is likely to be controlled through modulation of kinases or 14-3-3 binding activity.
AB - Cdc25C phosphatase induces mitosis by dephosphorylating and activating Cdc2/cyclin B protein kinase. Phosphorylation of Xenopus Cdc25C at serine 287 creates a binding site for a 14-3-3 protein and restrains activation during interphase. Here, we show that dephosphorylation of S287 is catalysed by protein phosphatase-2A in Xenopus egg extracts. 14-3-3 protein binding to Cdc25C inhibits dephosphorylation of S287, providing a mechanism to maintain phosphorylation of that site during interphase. The rate of dephosphorylation of S287 is not increased in mitotic extracts, indicating that the phosphorylation status of the site is likely to be controlled through modulation of kinases or 14-3-3 binding activity.
KW - 14-3-3 protein
KW - Cdc25
KW - Cell cycle checkpoint
KW - Chk1
KW - Protein phosphatase
UR - http://www.scopus.com/inward/record.url?scp=0037174161&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(02)03327-6
DO - 10.1016/S0014-5793(02)03327-6
M3 - Article
C2 - 12297318
AN - SCOPUS:0037174161
VL - 528
SP - 267
EP - 271
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 1-3
ER -