The xenopus Suc1/Cks protein promotes the phosphorylation of G(2)/M regulators
- PMID: 10601234
- DOI: 10.1074/jbc.274.52.36839
The xenopus Suc1/Cks protein promotes the phosphorylation of G(2)/M regulators
Abstract
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.
Similar articles
-
Constant regulation of both the MPF amplification loop and the Greatwall-PP2A pathway is required for metaphase II arrest and correct entry into the first embryonic cell cycle.J Cell Sci. 2010 Jul 1;123(Pt 13):2281-91. doi: 10.1242/jcs.064527. J Cell Sci. 2010. PMID: 20554897
-
Xe-p9, a Xenopus Suc1/Cks protein, is essential for the Cdc2-dependent phosphorylation of the anaphase- promoting complex at mitosis.Genes Dev. 1998 Aug 15;12(16):2549-59. doi: 10.1101/gad.12.16.2549. Genes Dev. 1998. PMID: 9716407 Free PMC article.
-
Mitotic progression becomes irreversible in prometaphase and collapses when Wee1 and Cdc25 are inhibited.Mol Biol Cell. 2011 Apr 15;22(8):1191-206. doi: 10.1091/mbc.E10-07-0599. Epub 2011 Feb 16. Mol Biol Cell. 2011. PMID: 21325631 Free PMC article.
-
Myt1: a Wee1-type kinase that phosphorylates Cdc2 on residue Thr14.Prog Cell Cycle Res. 1997;3:233-40. doi: 10.1007/978-1-4615-5371-7_18. Prog Cell Cycle Res. 1997. PMID: 9552418 Review.
-
Many fingers on the mitotic trigger: post-translational regulation of the Cdc25C phosphatase.Cell Cycle. 2004 Jan;3(1):41-5. Cell Cycle. 2004. PMID: 14657664 Review.
Cited by
-
Functional modules in the Arabidopsis core cell cycle binary protein-protein interaction network.Plant Cell. 2010 Apr;22(4):1264-80. doi: 10.1105/tpc.109.073635. Epub 2010 Apr 20. Plant Cell. 2010. PMID: 20407024 Free PMC article.
-
Structural insights into the functional diversity of the CDK-cyclin family.Open Biol. 2018 Sep;8(9):180112. doi: 10.1098/rsob.180112. Open Biol. 2018. PMID: 30185601 Free PMC article. Review.
-
Cks overexpression enhances chemotherapeutic efficacy by overriding DNA damage checkpoints.Oncogene. 2015 Apr 9;34(15):1961-7. doi: 10.1038/onc.2014.137. Epub 2014 May 26. Oncogene. 2015. PMID: 24858038 Free PMC article.
-
CKS Proteins Promote Checkpoint Recovery by Stimulating Phosphorylation of Treslin.Mol Cell Biol. 2017 Sep 26;37(20):e00344-17. doi: 10.1128/MCB.00344-17. Print 2017 Oct 15. Mol Cell Biol. 2017. PMID: 28739856 Free PMC article.
-
Molecular and biochemical characterization of the parvulin-type PPIases in Lotus japonicus.Plant Physiol. 2009 Jul;150(3):1160-73. doi: 10.1104/pp.108.132415. Epub 2009 Apr 29. Plant Physiol. 2009. PMID: 19403733 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous
