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PIAS1‐mediated sumoylation promotes STUbL‐dependent proteasomal degradation of the human telomeric protein TRF2
Author(s) -
Her Joonyoung,
Jeong Yu Young,
Chung In Kwon
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.09.030
Subject(s) - sumo protein , degradation (telecommunications) , microbiology and biotechnology , chemistry , ubiquitin , protein degradation , telomere , biology , biochemistry , computer science , dna , gene , telecommunications
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.