PMID- 10601234
OWN - NLM
STAT- MEDLINE
DCOM- 20000113
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 52
DP  - 1999 Dec 24
TI  - The xenopus Suc1/Cks protein promotes the phosphorylation of G(2)/M regulators.
PG  - 36839-42
AB  - The entry into mitosis is controlled by Cdc2/cyclin B, also known as maturation
      or M-phase promoting factor (MPF). In Xenopus egg extracts, the inhibitory
      phosphorylations of Cdc2 on Tyr-15 and Thr-14 are controlled by the phosphatase
      Cdc25 and the kinases Myt1 and Wee1. At mitosis, Cdc25 is activated and Myt1 and 
      Wee1 are inactivated through phosphorylation by multiple kinases, including Cdc2 
      itself. The Cdc2-associated Suc1/Cks1 protein (p9) is also essential for entry of
      egg extracts into mitosis, but the molecular basis of this requirement has been
      unknown. We find that p9 strongly stimulates the regulatory phosphorylations of
      Cdc25, Myt1, and Wee1 that are carried out by the Cdc2/cyclin B complex.
      Overexpression of the prolyl isomerase Pin1, which binds to the
      hyperphosphorylated forms of Cdc25, Myt1, and Wee1 found at M-phase, is known to 
      block the initiation of mitosis in egg extracts. We have observed that Pin1
      specifically antagonizes the stimulatory effect of p9 on phosphorylation of Cdc25
      by Cdc2/cyclin B. This observation could explain why overexpression of Pin1
      inhibits mitotic initiation. These findings suggest that p9 promotes the entry
      into mitosis by facilitating phosphorylation of the key upstream regulators of
      Cdc2.
FAU - Patra, D
AU  - Patra D
AD  - Division of Biology 216-76, Howard Hughes Medical Institute, California Institute
      of Technology, Pasadena, California 91125, USA.
FAU - Wang, S X
AU  - Wang SX
FAU - Kumagai, A
AU  - Kumagai A
FAU - Dunphy, W G
AU  - Dunphy WG
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (CKS1 protein, S cerevisiae)
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Cyclin B)
RN  - 0 (Fungal Proteins)
RN  - 0 (NIMA-Interacting Peptidylprolyl Isomerase)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Schizosaccharomyces pombe Proteins)
RN  - 0 (Suc1 protein, S pombe)
RN  - 0 (Xenopus Proteins)
RN  - EC 2.7.1.- (MYT1 kinase, Xenopus)
RN  - EC 2.7.1.- (WEE1 protein, Xenopus)
RN  - EC 2.7.1.- (wee1 protein, S pombe)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.22 (CDC2 Protein Kinase)
RN  - EC 3.1.3.48 (cdc25 Phosphatases)
RN  - EC 5.2.1.8 (ESS1 protein, S cerevisiae)
RN  - EC 5.2.1.8 (Peptidylprolyl Isomerase)
SB  - IM
MH  - Adaptor Proteins, Signal Transducing
MH  - Animals
MH  - CDC2 Protein Kinase/metabolism
MH  - *Cell Cycle Proteins
MH  - Cyclin B/metabolism
MH  - Female
MH  - Fungal Proteins/*physiology
MH  - G2 Phase
MH  - Mitosis
MH  - NIMA-Interacting Peptidylprolyl Isomerase
MH  - *Nuclear Proteins
MH  - Peptidylprolyl Isomerase/physiology
MH  - Phosphorylation
MH  - Protein-Serine-Threonine Kinases/*metabolism
MH  - Protein-Tyrosine Kinases/*metabolism
MH  - *Saccharomyces cerevisiae Proteins
MH  - *Schizosaccharomyces pombe Proteins
MH  - Xenopus
MH  - *Xenopus Proteins
MH  - cdc25 Phosphatases/*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 - 10.1074/jbc.274.52.36839 [doi]
AID - S0021-9258(19)53030-7 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Dec 24;274(52):36839-42. doi: 10.1074/jbc.274.52.36839.