PIAS1-mediated sumoylation promotes STUbL-dependent proteasomal degradation of the human telomeric protein TRF2.
FEBS Lett
; 589(21): 3277-86, 2015 Oct 24.
Article
em En
| MEDLINE
| ID: mdl-26450775
The human telomeric protein TRF2 protects chromosome ends by facilitating their organization into the protective capping structure. Here we show that the stability of TRF2 is regulated via modification by the small ubiquitin-like modifiers (SUMO). TRF2 specifically interacts with and is sumoylated by PIAS1 in mammalian cells. The proteasome inhibitor stabilizes SUMO-conjugated TRF2 without affecting the level of unmodified TRF2, suggesting that SUMO conjugation is required for proteasomal degradation of TRF2. We also show that RNF4, a mammalian SUMO-targeted ubiquitin ligase, interacts with TRF2 in a SUMO-dependent manner and preferentially targets SUMO-conjugated TRF2 for ubiquitination. Collectively, our data demonstrate that the PIAS1-mediated sumoylation status of TRF2 serves as a molecular switch that controls the level of TRF2 at telomeres.
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MEDLINE
Assunto principal:
Fatores de Transcrição
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Proteínas Nucleares
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Proteínas Modificadoras Pequenas Relacionadas à Ubiquitina
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Proteína 2 de Ligação a Repetições Teloméricas
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Complexo de Endopeptidases do Proteassoma
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Proteínas Inibidoras de STAT Ativados
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article