| Protein requirements for sister telomere association in human cells. | |
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MedLine Citation:
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PMID: 17962804 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Previous studies in human cells indicate that sister telomeres have distinct requirements for their separation at mitosis. In cells depleted for tankyrase 1, a telomeric poly(ADP-ribose) polymerase, sister chromatid arms and centromeres separate normally, but telomeres remain associated and cells arrest in mitosis. Here, we use biochemical and genetic approaches to identify proteins that might mediate the persistent association at sister telomeres. We use immunoprecipitation analysis to show that the telomeric proteins, TRF1 (an acceptor of PARsylation by tankyrase 1) and TIN2 (a TRF1 binding partner) each bind to the SA1 ortholog of the cohesin Scc3 subunit. Sucrose gradient sedimentation shows that TRF1 cosediments with the SA1-cohesin complex. Depletion of the SA1 cohesin subunit or the telomeric proteins (TRF1 and TIN2) restores the normal resolution of sister telomeres in mitosis in tankyrase 1-depleted cells. Moreover, depletion of TRF1 and TIN2 or SA1 abrogates the requirement for tankyrase 1 in mitotic progression. Our studies indicate that sister telomere association in human cells is mediated by a novel association between a cohesin subunit and components of telomeric chromatin. |
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Authors:
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Silvia Canudas; Benjamin R Houghtaling; Ju Youn Kim; Jasmin N Dynek; William G Chang; Susan Smith |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2007-10-25 |
Journal Detail:
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Title: The EMBO journal Volume: 26 ISSN: 1460-2075 ISO Abbreviation: EMBO J. Publication Date: 2007 Nov |
Date Detail:
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Created Date: 2007-11-28 Completed Date: 2007-12-13 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 8208664 Medline TA: EMBO J Country: England |
Other Details:
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Languages: eng Pagination: 4867-78 Citation Subset: IM |
Affiliation:
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Program in Molecular Pathogenesis and Department of Pathology, The Kimmel Center for Biology and Medicine of the Skirball Institute, New York University School of Medicine, New York, NY 10016, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Cell Cycle Proteins
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metabolism Centrifugation, Density Gradient Chromosomal Proteins, Non-Histone / metabolism Gene Expression Regulation, Neoplastic Hela Cells Humans Immunoprecipitation In Situ Hybridization, Fluorescence Mitosis Models, Biological Nuclear Proteins / metabolism Poly(ADP-ribose) Polymerases / metabolism Protein Binding Tankyrases / genetics, metabolism Telomere / ultrastructure* Telomere-Binding Proteins / metabolism Telomeric Repeat Binding Protein 1 / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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CA09161/CA/NCI NIH HHS; GM07238/GM/NIGMS NIH HHS; R01 CA116352/CA/NCI NIH HHS; R01 CA95099/CA/NCI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Cell Cycle Proteins; 0/Chromosomal Proteins, Non-Histone; 0/Nuclear Proteins; 0/TINF2 protein, human; 0/Telomere-Binding Proteins; 0/Telomeric Repeat Binding Protein 1; 0/cohesins; EC 2.4.2.30/Poly(ADP-ribose) Polymerases; EC 2.4.2.30/Tankyrases; EC 2.4.4.30/TNKS protein, human |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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