Abstract:
:Mammalian telomeres are coated by the sequence-specific, DNA-binding protein, TRF1, a negative regulator of telomere length. Previous results showed that ADP-ribosylation of TRF1 by tankyrase 1 released TRF1 from telomeres and promoted telomere elongation. We now show that loss of TRF1 from telomeres results in ubiquitination and degradation of TRF1 by the proteasome and that degradation is required to keep TRF1 off telomeres. Ubiquitination of TRF1 is regulated by its telomere-binding status; only the telomere-unbound form of TRF1 is ubiquitinated. Our findings suggest a novel mechanism of sequential post translational modification of TRF1 (ADP-ribosylation and ubiquitination) for regulating access of telomerase to telomeres.
journal_name
Genes Devjournal_title
Genes & developmentauthors
Chang W,Dynek JN,Smith Sdoi
10.1101/gad.1077103subject
Has Abstractpub_date
2003-06-01 00:00:00pages
1328-33issue
11eissn
0890-9369issn
1549-5477pii
17/11/1328journal_volume
17pub_type
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journal_title:Genes & development
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pub_type: 杂志文章
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journal_title:Genes & development
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journal_title:Genes & development
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journal_title:Genes & development
pub_type: 杂志文章
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更新日期:2004-10-15 00:00:00
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journal_title:Genes & development
pub_type: 杂志文章
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journal_title:Genes & development
pub_type: 杂志文章
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journal_title:Genes & development
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journal_title:Genes & development
pub_type: 杂志文章,评审
doi:10.1101/gad.993902
更新日期:2002-08-15 00:00:00
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journal_title:Genes & development
pub_type: 杂志文章
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更新日期:2009-05-01 00:00:00
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journal_title:Genes & development
pub_type: 杂志文章
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journal_title:Genes & development
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journal_title:Genes & development
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journal_title:Genes & development
pub_type: 杂志文章
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journal_title:Genes & development
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journal_title:Genes & development
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journal_title:Genes & development
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journal_title:Genes & development
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