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A role for Cdc2- and PP2A-mediated regulation of Emi2 in the maintenance of CSF arrest.

Publication ,  Journal Article
Wu, Q; Guo, Y; Yamada, A; Perry, JA; Wang, MZ; Araki, M; Freel, CD; Tung, JJ; Tang, W; Margolis, SS; Jackson, PK; Yamano, H; Asano, M; Kornbluth, S
Published in: Current biology : CB
February 2007

Vertebrate oocytes are arrested in metaphase II of meiosis prior to fertilization by cytostatic factor (CSF). CSF enforces a cell-cycle arrest by inhibiting the anaphase-promoting complex (APC), an E3 ubiquitin ligase that targets Cyclin B for degradation. Although Cyclin B synthesis is ongoing during CSF arrest, constant Cyclin B levels are maintained. To achieve this, oocytes allow continuous slow Cyclin B degradation, without eliminating the bulk of Cyclin B, which would induce release from CSF arrest. However, the mechanism that controls this continuous degradation is not understood.We report here the molecular details of a negative feedback loop wherein Cyclin B promotes its own destruction through Cdc2/Cyclin B-mediated phosphorylation and inhibition of the APC inhibitor Emi2. Emi2 bound to the core APC, and this binding was disrupted by Cdc2/Cyclin B, without affecting Emi2 protein stability. Cdc2-mediated phosphorylation of Emi2 was antagonized by PP2A, which could bind to Emi2 and promote Emi2-APC interactions.Constant Cyclin B levels are maintained during a CSF arrest through the regulation of Emi2 activity. A balance between Cdc2 and PP2A controls Emi2 phosphorylation, which in turn controls the ability of Emi2 to bind to and inhibit the APC. This balance allows proper maintenance of Cyclin B levels and Cdc2 kinase activity during CSF arrest.

Duke Scholars

Published In

Current biology : CB

DOI

EISSN

1879-0445

ISSN

0960-9822

Publication Date

February 2007

Volume

17

Issue

3

Start / End Page

213 / 224

Related Subject Headings

  • Xenopus Proteins
  • Xenopus
  • Ubiquitin-Protein Ligase Complexes
  • Recombinant Fusion Proteins
  • Proto-Oncogene Proteins c-mos
  • Protein Binding
  • Phosphorylation
  • Phosphoprotein Phosphatases
  • Oocytes
  • Okadaic Acid
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Wu, Q., Guo, Y., Yamada, A., Perry, J. A., Wang, M. Z., Araki, M., … Kornbluth, S. (2007). A role for Cdc2- and PP2A-mediated regulation of Emi2 in the maintenance of CSF arrest. Current Biology : CB, 17(3), 213–224. https://doi.org/10.1016/j.cub.2006.12.045
Wu, Qiju, Yanxiang Guo, Ayumi Yamada, Jennifer A. Perry, Michael Z. Wang, Marito Araki, Christopher D. Freel, et al. “A role for Cdc2- and PP2A-mediated regulation of Emi2 in the maintenance of CSF arrest.Current Biology : CB 17, no. 3 (February 2007): 213–24. https://doi.org/10.1016/j.cub.2006.12.045.
Wu Q, Guo Y, Yamada A, Perry JA, Wang MZ, Araki M, et al. A role for Cdc2- and PP2A-mediated regulation of Emi2 in the maintenance of CSF arrest. Current biology : CB. 2007 Feb;17(3):213–24.
Wu, Qiju, et al. “A role for Cdc2- and PP2A-mediated regulation of Emi2 in the maintenance of CSF arrest.Current Biology : CB, vol. 17, no. 3, Feb. 2007, pp. 213–24. Epmc, doi:10.1016/j.cub.2006.12.045.
Wu Q, Guo Y, Yamada A, Perry JA, Wang MZ, Araki M, Freel CD, Tung JJ, Tang W, Margolis SS, Jackson PK, Yamano H, Asano M, Kornbluth S. A role for Cdc2- and PP2A-mediated regulation of Emi2 in the maintenance of CSF arrest. Current biology : CB. 2007 Feb;17(3):213–224.
Journal cover image

Published In

Current biology : CB

DOI

EISSN

1879-0445

ISSN

0960-9822

Publication Date

February 2007

Volume

17

Issue

3

Start / End Page

213 / 224

Related Subject Headings

  • Xenopus Proteins
  • Xenopus
  • Ubiquitin-Protein Ligase Complexes
  • Recombinant Fusion Proteins
  • Proto-Oncogene Proteins c-mos
  • Protein Binding
  • Phosphorylation
  • Phosphoprotein Phosphatases
  • Oocytes
  • Okadaic Acid