| Constitutive phosphorylation mutation in Fas-associated death domain (FADD) results in early cell cycle defects. | |
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MedLine Citation:
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PMID: 17553783 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Fas-associated death domain (FADD) is an adaptor molecule for the death receptor subfamily of the tumor necrosis factor receptor superfamily, but it is also required for cell proliferation. Cell cycle-specific regulation of FADD phosphorylation plays an important role in FADD proliferative function since mice with a mutant form of FADD mimicking constitutive phosphorylation at serine 191 (FADD-D) exhibit defective T cell proliferation. Here we characterized these mice in detail and found that T cell development in 2-4-week-old mice is relatively normal, although mature FADD-D T cells manifest defective G(0) and G(1) to S transition with abnormalities in regulation of p130, p27 degradation, retinoblastoma protein phosphorylation, and CDK2 kinase activity. These downstream defects are further associated with the failure to up-regulate the forkhead box M1 cell cycle transcription factor, FoxM1. FADD-D protein is also mislocalized during cell cycle progression. Thus, regulation of FADD phosphorylation is crucial for proper cell cycle entry. |
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Authors:
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Stephanie L Osborn; Sue J Sohn; Astar Winoto |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2007-06-06 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 282 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2007 Aug |
Date Detail:
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Created Date: 2007-07-30 Completed Date: 2007-09-13 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 22786-92 Citation Subset: IM |
Affiliation:
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Cancer Research Laboratory and Department of Molecular and Cell Biology, University of California Berkeley, Berkeley, California 94720-3200, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Apoptosis Cell Cycle Cell Proliferation Fas-Associated Death Domain Protein / chemistry*, genetics* Flow Cytometry Gene Expression Regulation Immunoprecipitation Mice Mice, Transgenic Microscopy, Fluorescence Mutation* Phosphorylation Receptors, Death Domain / metabolism Retinoblastoma Protein / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Fas-Associated Death Domain Protein; 0/Receptors, Death Domain; 0/Retinoblastoma Protein |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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