FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends on a Cullin 4B/DDB1 Complex.
FBXO44-Mediated Degradation of RGS2 Protein Uniquely Depends on a Cullin 4B/DDB1 Complex.
复制标题
RGS2蛋白的FBXO44介导的降解独特地取决于Cullin 4b/ddb1复合物。
DOI：
10.1371/journal.pone.0123581
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发表时间：
2015
期刊：
影响因子：
3.7
通讯作者：
Neubig RR
中科院分区：
文献类型：
--
作者：
Sjögren B;Swaney S;Neubig RR
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.
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影响因子：
8.8
作者：
通讯作者：
--
影响因子：
15.9
作者：
Heximer, SP;Knutsen, RH;Blumer, KJ
通讯作者：
Blumer, KJ
影响因子：
4.8
作者：
Davydov, IV;Varshavsky, A
通讯作者：
Varshavsky, A
DOI：
10.1016/s0167-4781(01)00342-6
发表时间：
2001-12-03
期刊：
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION
影响因子：
--
作者：
Doupnik, CA;Xu, T;Shinaman, JM
通讯作者：
Shinaman, JM
影响因子：
3.4
作者：
Gold, SJ;Han, MH;Nestler, EJ
通讯作者：
Nestler, EJ