PMID- 10205171
OWN - NLM
STAT- MEDLINE
DCOM- 19990611
LR  - 20181113
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 8
DP  - 1999 Apr 15
TI  - Maintenance of G2 arrest in the Xenopus oocyte: a role for 14-3-3-mediated
      inhibition of Cdc25 nuclear import.
PG  - 2174-83
AB  - Cdc2-cyclin B1 in the G2-arrested Xenopus oocyte is held inactive by
      phosphorylation of Cdc2 at two negative regulatory sites, Thr14 and Tyr15. Upon
      treatment with progesterone, these sites are dephosphorylated by the dual
      specificity phosphatase, Cdc25, leading to Cdc2-cyclin B1 activation. Whereas
      maintenance of the G2 arrest depends upon preventing Cdc25-induced Cdc2
      dephosphorylation, the mechanisms responsible for keeping Cdc25 in check in these
      cells have not yet been described. Here we report that Cdc25 in the G2-arrested
      oocyte is bound to 14-3-3 proteins and that progesterone treatment abrogates this
      binding. We demonstrate that Cdc25, apparently statically localized in the
      cytoplasm, is actually capable of shuttling in and out of the oocyte nucleus.
      Binding of 14-3-3 protein markedly reduces the nuclear import rate of Cdc25,
      allowing nuclear export mediated by a nuclear export sequence present in the
      N-terminus of Cdc25 to predominate. If 14-3-3 binding to Cdc25 is prevented while
      nuclear export is inhibited, the coordinate nuclear accumulation of Cdc25 and
      Cdc2-cyclin B1 facilitates their mutual activation, thereby promoting oocyte
      maturation.
FAU - Yang, J
AU  - Yang J
AD  - Department of Pharmacology and Cancer Biology, Duke University Medical Center,
      C366 LSRC, Research Drive, Box 3686, Durham, NC 27710, USA.
FAU - Winkler, K
AU  - Winkler K
FAU - Yoshida, M
AU  - Yoshida M
FAU - Kornbluth, S
AU  - Kornbluth S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (14-3-3 Proteins)
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Cyclin B)
RN  - 0 (DNA Primers)
RN  - 0 (Fatty Acids, Unsaturated)
RN  - 0 (Proteins)
RN  - EC 1.14.16.2 (Tyrosine 3-Monooxygenase)
RN  - EC 2.7.11.22 (CDC2 Protein Kinase)
RN  - EC 3.1.3.16 (Phosphoprotein Phosphatases)
RN  - EC 3.1.3.48 (cdc25 Phosphatases)
RN  - Y031I2N1EO (leptomycin B)
SB  - IM
MH  - 14-3-3 Proteins
MH  - Animals
MH  - Base Sequence
MH  - Biological Transport
MH  - CDC2 Protein Kinase/metabolism
MH  - Cell Cycle Proteins/*antagonists & inhibitors/genetics/metabolism
MH  - Cell Nucleus/*metabolism
MH  - Cyclin B/metabolism
MH  - DNA Primers
MH  - Fatty Acids, Unsaturated/pharmacology
MH  - *G2 Phase
MH  - Mutagenesis, Site-Directed
MH  - Oocytes/*cytology/drug effects
MH  - Phosphoprotein Phosphatases/*antagonists & inhibitors/genetics/metabolism
MH  - Protein Binding
MH  - Proteins/metabolism/*physiology
MH  - *Tyrosine 3-Monooxygenase
MH  - Xenopus laevis
MH  - cdc25 Phosphatases
PMC - PMC1171301
EDAT- 1999/04/16 00:00
MHDA- 1999/04/16 00:01
CRDT- 1999/04/16 00:00
PHST- 1999/04/16 00:00 [pubmed]
PHST- 1999/04/16 00:01 [medline]
PHST- 1999/04/16 00:00 [entrez]
AID - 10.1093/emboj/18.8.2174 [doi]
PST - ppublish
SO  - EMBO J. 1999 Apr 15;18(8):2174-83. doi: 10.1093/emboj/18.8.2174.