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- W363945232 endingPage "e0123581" @default.
- W363945232 startingPage "e0123581" @default.
- W363945232 abstract "The ubiquitin-proteasome system for protein degradation plays a major role in regulating cell function and many signaling proteins are tightly controlled by this mechanism. Among these, Regulator of G Protein Signaling 2 (RGS2) is a target for rapid proteasomal degradation, however, the specific enzymes involved are not known. Using a genomic siRNA screening approach, we identified a novel E3 ligase complex containing cullin 4B (CUL4B), DNA damage binding protein 1 (DDB1) and F-box protein 44 (FBXO44) that mediates RGS2 protein degradation. While the more typical F-box partners CUL1 and Skp1 can bind FBXO44, that E3 ligase complex does not bind RGS2 and is not involved in RGS2 degradation. These observations define an unexpected DDB1/CUL4B-containing FBXO44 E3 ligase complex. Pharmacological targeting of this mechanism provides a novel therapeutic approach to hypertension, anxiety, and other diseases associated with RGS2 dysregulation." @default.
- W363945232 created "2016-06-24" @default.
- W363945232 creator A5016819654 @default.
- W363945232 creator A5033090689 @default.
- W363945232 creator A5080590812 @default.
- W363945232 date "2015-05-13" @default.
- W363945232 modified "2023-09-27" @default.
- W363945232 title "FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends on a Cullin 4B/DDB1 Complex" @default.
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- W363945232 doi "https://doi.org/10.1371/journal.pone.0123581" @default.
- W363945232 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4430315" @default.
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