| Zinc regulates the ability of Cdc25C to activate MPF/cdk1. | |
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MedLine Citation:
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PMID: 17443687 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Zn(2+) is an essential micronutrient for the growth and development of multicellular organisms, as Zn(2+) deficiencies lead to growth retardation and congenital malformations (Vallee, BL, Falchuk, KH. 1993. Physiol Rev., 73:79-118). At the cellular level Zn(2+) depravation results in proliferation defects in many cell types (Vallee, BL, Falchuk, KH. 1993. Physiol Rev., 73:79-118), however the molecular pathways involved remain poorly defined. Here we show that the transition metal chelator TPEN (N,N,N',N'-tetrakis(2-pyridylmethyl) ethylene diamine) blocks the G2/M transition of the meiotic cell cycle by inhibiting Cdc25C-cdk1 activation. ICP-MS analyses reveal that Cdc25C is a Zn(2+)-binding metalloprotein, and that TPEN effectively strips Zn(2+) away from the enzyme. Interestingly, although apo-Cdc25C (Zn(2+)-deficient) remains fully catalytically active, it is compromised in its ability to dephosphorylate and activate MPF/cdk1. Thus, Zn(2+) is an important regulator of Cdc25C function in vivo. Because of the conserved essential role of the Cdc25C-cdk1 module in the eukaryotic cell cycle, these studies provide fundamental insights into cell cycle regulation. |
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Authors:
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Lu Sun; Yingtao Chai; Robyn Hannigan; Venkata K Bhogaraju; Khaled Machaca |
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Publication Detail:
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Type: In Vitro; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of cellular physiology Volume: 213 ISSN: 0021-9541 ISO Abbreviation: J. Cell. Physiol. Publication Date: 2007 Oct |
Date Detail:
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Created Date: 2007-07-26 Completed Date: 2007-10-26 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 0050222 Medline TA: J Cell Physiol Country: United States |
Other Details:
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Languages: eng Pagination: 98-104 Citation Subset: IM |
Copyright Information:
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(c) 2007 Wiley-Liss, Inc. |
Affiliation:
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Department of Physiology and Biophysics, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals CDC2 Protein Kinase / metabolism* Cell Cycle Proteins / metabolism* Chelating Agents / pharmacology Enzyme Activation / drug effects Ethylenediamines / pharmacology Female Maturation-Promoting Factor / metabolism* Meiosis / drug effects Oocytes / cytology, drug effects, metabolism Phosphorylation Recombinant Fusion Proteins / metabolism Xenopus Xenopus Proteins / metabolism Zinc / metabolism* cdc25 Phosphatases / metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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GM-61829/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Cell Cycle Proteins; 0/Chelating Agents; 0/Ethylenediamines; 0/Recombinant Fusion Proteins; 0/Xenopus Proteins; 16858-02-9/N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine; 7440-66-6/Zinc; EC 2.7.11.22/CDC2 Protein Kinase; EC 2.7.11.22/Maturation-Promoting Factor; EC 3.1.3.48/cdc25 Phosphatases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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