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PP1-mediated dephosphorylation of phosphoproteins at mitotic exit is controlled by inhibitor-1 and PP1 phosphorylation.

Publication ,  Journal Article
Wu, JQ; Guo, JY; Tang, W; Yang, C-S; Freel, CD; Chen, C; Nairn, AC; Kornbluth, S
Published in: Nature cell biology
May 2009

Loss of cell division cycle 2 (Cdc2, also known as Cdk1) activity after cyclin B degradation is necessary, but not sufficient, for mitotic exit. Proteins phosphorylated by Cdc2 and downstream mitotic kinases must be dephosphorylated. We report here that protein phosphatase-1 (PP1) is the main catalyst of mitotic phosphoprotein dephosphorylation. Suppression of PP1 during early mitosis is maintained through dual inhibition by Cdc2 phosphorylation and the binding of inhibitor-1. Protein kinase A (PKA) phosphorylates inhibitor-1, mediating binding to PP1. As Cdc2 levels drop after cyclin B degradation, auto-dephosphorylation of PP1 at its Cdc2 phosphorylation site (Thr 320) allows partial PP1 activation. This promotes PP1-regulated dephosphorylation at the activating site of inhibitor-1 (Thr 35) followed by dissociation of the inhibitor-1-PP1 complex and then full PP1 activation to promote mitotic exit. Thus, Cdc2 both phosphorylates multiple mitotic substrates and inhibits their PP1-mediated dephosphorylation.

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Published In

Nature cell biology

DOI

EISSN

1476-4679

ISSN

1465-7392

Publication Date

May 2009

Volume

11

Issue

5

Start / End Page

644 / 651

Related Subject Headings

  • Xenopus laevis
  • Xenopus Proteins
  • Threonine
  • Roscovitine
  • Purines
  • Proteins
  • Protein Phosphatase 1
  • Protein Kinases
  • Protein Kinase Inhibitors
  • Protein Binding
 

Citation

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Wu, J. Q., Guo, J. Y., Tang, W., Yang, C.-S., Freel, C. D., Chen, C., … Kornbluth, S. (2009). PP1-mediated dephosphorylation of phosphoproteins at mitotic exit is controlled by inhibitor-1 and PP1 phosphorylation. Nature Cell Biology, 11(5), 644–651. https://doi.org/10.1038/ncb1871
Wu, Judy Qiju, Jessie Yanxiang Guo, Wanli Tang, Chih-Sheng Yang, Christopher D. Freel, Chen Chen, Angus C. Nairn, and Sally Kornbluth. “PP1-mediated dephosphorylation of phosphoproteins at mitotic exit is controlled by inhibitor-1 and PP1 phosphorylation.Nature Cell Biology 11, no. 5 (May 2009): 644–51. https://doi.org/10.1038/ncb1871.
Wu JQ, Guo JY, Tang W, Yang C-S, Freel CD, Chen C, et al. PP1-mediated dephosphorylation of phosphoproteins at mitotic exit is controlled by inhibitor-1 and PP1 phosphorylation. Nature cell biology. 2009 May;11(5):644–51.
Wu, Judy Qiju, et al. “PP1-mediated dephosphorylation of phosphoproteins at mitotic exit is controlled by inhibitor-1 and PP1 phosphorylation.Nature Cell Biology, vol. 11, no. 5, May 2009, pp. 644–51. Epmc, doi:10.1038/ncb1871.
Wu JQ, Guo JY, Tang W, Yang C-S, Freel CD, Chen C, Nairn AC, Kornbluth S. PP1-mediated dephosphorylation of phosphoproteins at mitotic exit is controlled by inhibitor-1 and PP1 phosphorylation. Nature cell biology. 2009 May;11(5):644–651.

Published In

Nature cell biology

DOI

EISSN

1476-4679

ISSN

1465-7392

Publication Date

May 2009

Volume

11

Issue

5

Start / End Page

644 / 651

Related Subject Headings

  • Xenopus laevis
  • Xenopus Proteins
  • Threonine
  • Roscovitine
  • Purines
  • Proteins
  • Protein Phosphatase 1
  • Protein Kinases
  • Protein Kinase Inhibitors
  • Protein Binding