Dephosphorylation of the inhibitory phosphorylation site S287 in Xenopus Cdc25C by protein phosphatase-2A is inhibited by 14-3-3 binding

James R.A. Hutchins, Dina Dikovskaya, Paul R. Clarke

Research output: Contribution to journalArticle

21 Citations (Scopus)

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 languageEnglish
Pages (from-to)267-271
Number of pages5
JournalFEBS Letters
Volume528
Issue number1-3
DOIs
Publication statusPublished - 25 Sep 2002

Fingerprint

cdc25 Phosphatases
Xenopus Proteins
Protein Phosphatase 2
Phosphorylation
14-3-3 Proteins
Interphase
Xenopus
Cyclin B
Mitosis
Protein Binding
Protein Kinases
Serine
Ovum
Phosphotransferases
Chemical activation
Binding Sites
Modulation

Keywords

  • 14-3-3 protein
  • Cdc25
  • Cell cycle checkpoint
  • Chk1
  • Protein phosphatase

Cite this

@article{16ae9d125c0a4c0489e5df72de7509f2,
title = "Dephosphorylation of the inhibitory phosphorylation site S287 in Xenopus Cdc25C by protein phosphatase-2A is inhibited by 14-3-3 binding",
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.",
keywords = "14-3-3 protein, Cdc25, Cell cycle checkpoint, Chk1, Protein phosphatase",
author = "Hutchins, {James R.A.} and Dina Dikovskaya and Clarke, {Paul R.}",
year = "2002",
month = "9",
day = "25",
doi = "10.1016/S0014-5793(02)03327-6",
language = "English",
volume = "528",
pages = "267--271",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Wiley",
number = "1-3",

}

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 journalArticle

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 -