| Phosphorylation on Thr-55 by TAF1 mediates degradation of p53: a role for TAF1 in cell G1 progression. | |
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MedLine Citation:
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PMID: 15053879 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The largest subunit of TFIID, TAF1, possesses an intrinsic protein kinase activity and is important for cell G1 progression and apoptosis. Since p53 functions by inducing cell G1 arrest and apoptosis, we investigated the link between TAF1 and p53. We found that TAF1 induces G1 progression in a p53-dependent manner. TAF1 interacts with and phosphorylates p53 at Thr-55 in vivo. Substitution of Thr-55 with an alanine residue (T55A) stabilizes p53 and impairs the ability of TAF1 to induce G1 progression. Furthermore, both RNAi-mediated TAF1 ablation and apigenin-mediated inhibition of the kinase activity of TAF1 markedly reduced Thr-55 phosphorylation. Thus, phosphorylation and the resultant degradation of p53 provide a mechanism for regulation of the cell cycle by TAF1. Significantly, the Thr-55 phosphorylation was reduced following DNA damage, suggesting that this phosphorylation contributes to the stabilization of p53 in response to DNA damage. |
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Authors:
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Heng-Hong Li; Andrew G Li; Hilary M Sheppard; Xuan Liu |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Molecular cell Volume: 13 ISSN: 1097-2765 ISO Abbreviation: Mol. Cell Publication Date: 2004 Mar |
Date Detail:
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Created Date: 2004-03-31 Completed Date: 2004-05-25 Revised Date: 2013-04-29 |
Medline Journal Info:
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Nlm Unique ID: 9802571 Medline TA: Mol Cell Country: United States |
Other Details:
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Languages: eng Pagination: 867-78 Citation Subset: IM |
Affiliation:
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Department of Biochemistry, University of California, Riverside, CA 92521, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Alanine
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metabolism Amino Acid Substitution Antineoplastic Agents / pharmacology Apigenin Bone Neoplasms / genetics, pathology Cell Cycle / physiology* Cell Line, Tumor DNA Damage Drug Stability Flavonoids / pharmacology G1 Phase Humans Nuclear Proteins* Phosphorylation Protein Kinases / drug effects, metabolism* Proto-Oncogene Proteins / metabolism Proto-Oncogene Proteins c-mdm2 RNA, Small Interfering / metabolism TATA-Binding Protein Associated Factors / metabolism* Threonine / metabolism* Transcription Factor TFIID / metabolism* Transfection Tumor Suppressor Protein p53 / metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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CA75180/CA/NCI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Antineoplastic Agents; 0/Flavonoids; 0/Nuclear Proteins; 0/Proto-Oncogene Proteins; 0/RNA, Small Interfering; 0/TATA-Binding Protein Associated Factors; 0/Transcription Factor TFIID; 0/Tumor Suppressor Protein p53; 520-36-5/Apigenin; 56-41-7/Alanine; 72-19-5/Threonine; EC 2.7.-/Protein Kinases; EC 2.7.11.1/TATA-binding protein associated factor 250 kDa; EC 6.3.2.19/MDM2 protein, human; EC 6.3.2.19/Proto-Oncogene Proteins c-mdm2 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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