A screen for E3 ubiquitination ligases that genetically interact with the adaptor protein Cindr during Drosophila eye patterning.
A screen for E3 ubiquitination ligases that genetically interact with the adaptor protein Cindr during Drosophila eye patterning.
复制标题
DOI：
10.1371/journal.pone.0187571
复制
发表时间：
2017
期刊：
影响因子：
3.7
通讯作者：
Johnson RI
中科院分区：
文献类型：
--
作者：
Ketosugbo KF;Bushnell HL;Johnson RI
泛素化是一种重要的翻译后修饰，可以针对蛋白质进行降解。E3泛素连接酶负责识别泛素化的底物蛋白，从而为蛋白质降解过程提供特异性。在这里，我们描述了一个基因修饰剂筛选，鉴定了E3连接酶，这些连接酶修饰了果蝇眼睛发育过程中由cindrRNAi转基因表达产生的粗糙眼表型。总共，我们鉴定了36个E3连接酶，以及4个Cullins，它们修饰了轻微的cindrRNA错误模式表型。这表明这些E3s/Cullins可能在需要Cindr功能的过程中发挥作用，包括细胞骨架调节、细胞粘附、细胞信号传导和细胞存活。在我们的筛选中发现的三个E3连接酶先前与调节JNK信号传导有关。
Ubiquitination is a crucial post-translational modification that can target proteins for degradation. The E3 ubiquitin ligases are responsible for recognizing substrate proteins for ubiquitination, hence providing specificity to the process of protein degradation. Here, we describe a genetic modifier screen that identified E3 ligases that modified the rough-eye phenotype generated by expression of cindrRNAi transgenes during Drosophila eye development. In total, we identified 36 E3 ligases, as well as 4 Cullins, that modified the mild cindrRNA mis-patterning phenotype. This indicates possible roles for these E3s/Cullins in processes that require Cindr function, including cytoskeletal regulation, cell adhesion, cell signaling and cell survival. Three E3 ligases identified in our screen had previously been linked to regulating JNK signaling.
登录
查看更多内容
DOI：
10.1523/jneurosci.3190-10.2011
发表时间：
2011-04-13
期刊：
The Journal of neuroscience : the official journal of the Society for Neuroscience
影响因子：
--
作者：
Akalal DB;Yu D;Davis RL
通讯作者：
Davis RL
影响因子：
4
作者：
Carthew, Richard W.
通讯作者：
Carthew, Richard W.
DOI：
10.1073/pnas.0500346102
发表时间：
2005-07-19
影响因子：
11.1
作者：
Cha, GH;Kim, S;Cho, KS
通讯作者：
Cho, KS
影响因子：
2.6
作者：
Cooper, Sarah E.
通讯作者：
Cooper, Sarah E.
影响因子：
4.6
作者：
Barry, Kevin C.;Abed, Mona;Parkhurst, Susan M.
通讯作者：
Parkhurst, Susan M.