| Characterization of cell cycle specific protein interaction networks of the yeast 26S proteasome complex by the QTAX strategy. | |
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MedLine Citation:
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PMID: 20170199 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Ubiquitin-proteasome dependent protein degradation plays a fundamental role in the regulation of the eukaryotic cell cycle. Cell cycle transitions between different phases are tightly regulated to prevent uncontrolled cell proliferation, which is characteristic of cancer cells. To understand cell cycle phase specific regulation of the 26S proteasome and reveal the molecular mechanisms underlying the ubiquitin-proteasome degradation pathway during cell cycle progression, we have carried out comprehensive characterization of cell cycle phase specific proteasome interacting proteins (PIPs) by QTAX analysis of synchronized yeast cells. Our efforts have generated specific proteasome interaction networks for the G1, S, and M phases of the cell cycle and identified a total of 677 PIPs, 266 of which were not previously identified from unsynchronized cells. On the basis of the dynamic changes of their SILAC ratios across the three cell cycle phases, we have employed a profile vector-based clustering approach and identified 20 functionally significant groups of PIPs, 3 of which are enriched with cell cycle related functions. This work presents the first step toward understanding how dynamic proteasome interactions are involved in various cellular pathways during the cell cycle. |
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Authors:
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Robyn M Kaake; Tijana Milenković; Natasa Przulj; Peter Kaiser; Lan Huang |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: Journal of proteome research Volume: 9 ISSN: 1535-3907 ISO Abbreviation: J. Proteome Res. Publication Date: 2010 Apr |
Date Detail:
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Created Date: 2010-04-05 Completed Date: 2010-07-02 Revised Date: 2011-09-26 |
Medline Journal Info:
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Nlm Unique ID: 101128775 Medline TA: J Proteome Res Country: United States |
Other Details:
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Languages: eng Pagination: 2016-29 Citation Subset: IM |
Affiliation:
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Departments of Physiology & Biophysics and Developmental & Cell Biology, University of California, Irvine, California 92697-4560, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Cell Cycle Proteins
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chemistry*,
classification,
metabolism Flow Cytometry Formaldehyde Fungal Proteins / chemistry*, classification, metabolism Immunoprecipitation Isotope Labeling Proteasome Endopeptidase Complex / chemistry*, classification, metabolism Protein Interaction Mapping / methods* Reproducibility of Results Tandem Mass Spectrometry / methods* Yeasts / metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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GM-66164/GM/NIGMS NIH HHS; GM-74830/GM/NIGMS NIH HHS; R01 GM066164-08/GM/NIGMS NIH HHS; R01 GM074830-05/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Cell Cycle Proteins; 0/Fungal Proteins; 50-00-0/Formaldehyde; EC 3.4.25.1/Proteasome Endopeptidase Complex; EC 3.4.99.-/ATP dependent 26S protease |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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