PMID- 19696736
OWN - NLM
STAT- MEDLINE
DCOM- 20091007
LR  - 20211020
IS  - 1460-2075 (Electronic)
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 28
IP  - 18
DP  - 2009 Sep 16
TI  - Regulated activity of PP2A-B55 delta is crucial for controlling entry into and 
      exit from mitosis in Xenopus egg extracts.
PG  - 2777-85
LID - 10.1038/emboj.2009.238 [doi]
AB  - Entry into mitosis depends on the activity of cyclin-dependent kinases (CDKs). 
      Conversely, exit from mitosis occurs when mitotic cyclins are degraded, thereby 
      extinguishing CDK activity. Exit from mitosis must also require mitotic 
      phosphoproteins to revert to their interphase hypophosphorylated forms, but there 
      is a controversy about which phosphatase(s) is/are responsible for 
      dephosphorylating the CDK substrates. We find that PP2A associated with a B55 
      delta subunit is relatively specific for a model mitotic CDK substrate in Xenopus 
      egg extracts. The phosphatase activity measured by this substrate is regulated 
      during the cell cycle--high in interphase and suppressed during mitosis. 
      Depletion of PP2A-B55 delta (in interphase) from 'cycling' frog egg extracts 
      accelerated their entry into mitosis and kept them indefinitely in mitosis. When 
      PP2A-B55 delta was depleted from mitotic extracts, however, exit from mitosis was 
      hardly delayed, showing that other phosphatase(s) are also required for mitotic 
      exit. Increasing the concentration of PP2A-B55 delta in extracts by adding 
      recombinant enzyme inhibited the entry into mitosis. This form of PP2A seems to 
      be a key regulator of entry into and exit from mitosis.
FAU - Mochida, Satoru
AU  - Mochida S
AD  - Cancer Research UK, London Research Institute, Clare Hall Laboratories, South 
      Mimms, Herts, UK.
FAU - Ikeo, Satoshi
AU  - Ikeo S
FAU - Gannon, Julian
AU  - Gannon J
FAU - Hunt, Tim
AU  - Hunt T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20090820
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Peptides)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Xenopus Proteins)
RN  - EC 2.7.11.22 (Cyclin-Dependent Kinases)
RN  - EC 3.1.3.16 (Protein Phosphatase 2)
SB  - IM
MH  - Animals
MH  - Cell Cycle
MH  - Cyclin-Dependent Kinases/metabolism
MH  - Dose-Response Relationship, Drug
MH  - Escherichia coli/metabolism
MH  - *Gene Expression Regulation, Enzymologic
MH  - Inhibitory Concentration 50
MH  - *Mitosis
MH  - Ovum/metabolism
MH  - Peptides/chemistry
MH  - Phosphorylation
MH  - Protein Phosphatase 2/chemistry/*metabolism
MH  - Recombinant Proteins/chemistry
MH  - Xenopus Proteins/metabolism
MH  - Xenopus laevis
PMC - PMC2750019
EDAT- 2009/08/22 09:00
MHDA- 2009/10/08 06:00
PMCR- 2010/09/16
CRDT- 2009/08/22 09:00
PHST- 2009/01/26 00:00 [received]
PHST- 2009/07/15 00:00 [accepted]
PHST- 2009/08/22 09:00 [entrez]
PHST- 2009/08/22 09:00 [pubmed]
PHST- 2009/10/08 06:00 [medline]
PHST- 2010/09/16 00:00 [pmc-release]
AID - emboj2009238 [pii]
AID - 10.1038/emboj.2009.238 [doi]
PST - ppublish
SO  - EMBO J. 2009 Sep 16;28(18):2777-85. doi: 10.1038/emboj.2009.238. Epub 2009 Aug 
      20.