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Control of Emi2 activity and stability through Mos-mediated recruitment of PP2A.

Publication ,  Journal Article
Wu, JQ; Hansen, DV; Guo, Y; Wang, MZ; Tang, W; Freel, CD; Tung, JJ; Jackson, PK; Kornbluth, S
Published in: Proceedings of the National Academy of Sciences of the United States of America
October 2007

Before fertilization, vertebrate eggs are arrested in meiosis II by cytostatic factor (CSF), which holds the anaphase-promoting complex (APC) in an inactive state. It was recently reported that Mos, an integral component of CSF, acts in part by promoting the Rsk-mediated phosphorylation of the APC inhibitor Emi2/Erp1. We report here that Rsk phosphorylation of Emi2 promotes its interaction with the protein phosphatase PP2A. Emi2 residues adjacent to the Rsk phosphorylation site were important for PP2A binding. An Emi2 mutant that retained Rsk phosphorylation but lacked PP2A binding could not be modulated by Mos. PP2A bound to Emi2 acted on two distinct clusters of sites phosphorylated by Cdc2, one responsible for modulating its stability during CSF arrest and one that controls binding to the APC. These findings provide a molecular mechanism for Mos action in promoting CSF arrest and also define an unusual mechanism, whereby protein phosphorylation recruits a phosphatase for dephosphorylation of distinct sites phosphorylated by another kinase.

Duke Scholars

Published In

Proceedings of the National Academy of Sciences of the United States of America

DOI

EISSN

1091-6490

ISSN

0027-8424

Publication Date

October 2007

Volume

104

Issue

42

Start / End Page

16564 / 16569

Related Subject Headings

  • Xenopus Proteins
  • Xenopus
  • Signal Transduction
  • Ribosomal Protein S6 Kinases
  • Proto-Oncogene Proteins c-mos
  • Phosphorylation
  • Phosphorylase Phosphatase
  • Ovum
  • Molecular Sequence Data
  • Meiosis
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Wu, J. Q., Hansen, D. V., Guo, Y., Wang, M. Z., Tang, W., Freel, C. D., … Kornbluth, S. (2007). Control of Emi2 activity and stability through Mos-mediated recruitment of PP2A. Proceedings of the National Academy of Sciences of the United States of America, 104(42), 16564–16569. https://doi.org/10.1073/pnas.0707537104
Wu, Judy Qiju, David V. Hansen, Yanxiang Guo, Michael Zhuo Wang, Wanli Tang, Christopher D. Freel, Jeffrey J. Tung, Peter K. Jackson, and Sally Kornbluth. “Control of Emi2 activity and stability through Mos-mediated recruitment of PP2A.Proceedings of the National Academy of Sciences of the United States of America 104, no. 42 (October 2007): 16564–69. https://doi.org/10.1073/pnas.0707537104.
Wu JQ, Hansen DV, Guo Y, Wang MZ, Tang W, Freel CD, et al. Control of Emi2 activity and stability through Mos-mediated recruitment of PP2A. Proceedings of the National Academy of Sciences of the United States of America. 2007 Oct;104(42):16564–9.
Wu, Judy Qiju, et al. “Control of Emi2 activity and stability through Mos-mediated recruitment of PP2A.Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 42, Oct. 2007, pp. 16564–69. Epmc, doi:10.1073/pnas.0707537104.
Wu JQ, Hansen DV, Guo Y, Wang MZ, Tang W, Freel CD, Tung JJ, Jackson PK, Kornbluth S. Control of Emi2 activity and stability through Mos-mediated recruitment of PP2A. Proceedings of the National Academy of Sciences of the United States of America. 2007 Oct;104(42):16564–16569.
Journal cover image

Published In

Proceedings of the National Academy of Sciences of the United States of America

DOI

EISSN

1091-6490

ISSN

0027-8424

Publication Date

October 2007

Volume

104

Issue

42

Start / End Page

16564 / 16569

Related Subject Headings

  • Xenopus Proteins
  • Xenopus
  • Signal Transduction
  • Ribosomal Protein S6 Kinases
  • Proto-Oncogene Proteins c-mos
  • Phosphorylation
  • Phosphorylase Phosphatase
  • Ovum
  • Molecular Sequence Data
  • Meiosis