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TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres
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| Zeitschriftentitel: | Genes & Development |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Genes & Development, 17, 2003, 11, S. 1328-1333 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Cold Spring Harbor Laboratory
|
| Schlagwörter: |
| author_facet |
Chang, William Dynek, Jasmin N. Smith, Susan Chang, William Dynek, Jasmin N. Smith, Susan |
|---|---|
| author |
Chang, William Dynek, Jasmin N. Smith, Susan |
| spellingShingle |
Chang, William Dynek, Jasmin N. Smith, Susan Genes & Development TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres Developmental Biology Genetics |
| author_sort |
chang, william |
| spelling |
Chang, William Dynek, Jasmin N. Smith, Susan 0890-9369 1549-5477 Cold Spring Harbor Laboratory Developmental Biology Genetics http://dx.doi.org/10.1101/gad.1077103 <jats:p>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.</jats:p> TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres Genes & Development |
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Cold Spring Harbor Laboratory, 2003 |
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Cold Spring Harbor Laboratory, 2003 |
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Cold Spring Harbor Laboratory |
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Genes & Development |
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| title |
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres |
| title_unstemmed |
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres |
| title_full |
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres |
| title_fullStr |
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres |
| title_full_unstemmed |
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres |
| title_short |
TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres |
| title_sort |
trf1 is degraded by ubiquitin-mediated proteolysis after release from telomeres |
| topic |
Developmental Biology Genetics |
| url |
http://dx.doi.org/10.1101/gad.1077103 |
| publishDate |
2003 |
| physical |
1328-1333 |
| description |
<jats:p>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.</jats:p> |
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| author | Chang, William, Dynek, Jasmin N., Smith, Susan |
| author_facet | Chang, William, Dynek, Jasmin N., Smith, Susan, Chang, William, Dynek, Jasmin N., Smith, Susan |
| author_sort | chang, william |
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| description | <jats:p>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.</jats:p> |
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| imprint_str_mv | Cold Spring Harbor Laboratory, 2003 |
| institution | DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3 |
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| physical | 1328-1333 |
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| series | Genes & Development |
| source_id | 49 |
| spelling | Chang, William Dynek, Jasmin N. Smith, Susan 0890-9369 1549-5477 Cold Spring Harbor Laboratory Developmental Biology Genetics http://dx.doi.org/10.1101/gad.1077103 <jats:p>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.</jats:p> TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres Genes & Development |
| spellingShingle | Chang, William, Dynek, Jasmin N., Smith, Susan, Genes & Development, TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres, Developmental Biology, Genetics |
| title | TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres |
| title_full | TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres |
| title_fullStr | TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres |
| title_full_unstemmed | TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres |
| title_short | TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres |
| title_sort | trf1 is degraded by ubiquitin-mediated proteolysis after release from telomeres |
| title_unstemmed | TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres |
| topic | Developmental Biology, Genetics |
| url | http://dx.doi.org/10.1101/gad.1077103 |