K29/K48 分支泛素链触发警报，通过 CRL2 促进新底物的降解。
K29/K48-branched ubiquitin chains TRIP the alarm fueling neo-substrate degradation via the CRL2.
机构信息
The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Melbourne, VIC 3052, Australia; Department of Medical Biology, University of Melbourne, Parkville, VIC 3052, Australia.
The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Melbourne, VIC 3052, Australia; Department of Medical Biology, University of Melbourne, Parkville, VIC 3052, Australia.
出版信息
Mol Cell. 2021 Apr 1;81(7):1363-1365. doi: 10.1016/j.molcel.2021.02.030.
In this issue of Molecular Cell, Kaiho-Soma et al. (2021) demonstrate that the HECT-type E3 ubiquitin ligase TRIP12 cooperates with CRL complexes to promote PROTAC-induced degradation of neo-substrates by generating K29/K48-branched ubiquitin chains.
在本期《分子细胞》中，Kaiho-Soma 等人（2021 年）证明了 HECT 型 E3 泛素连接酶 TRIP12 通过生成 K29/K48 支链泛素链，与 CRL 复合物合作促进 PROTAC 诱导的新底物降解。
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