Open AccessA screen for E3 ubiquitination ligases that genetically interact with the adaptor protein Cindr during Drosophila eye patterning
Author(s) -
Kwami F. Ketosugbo,
Henry L. Bushnell,
Ruth I. Johnson
Publication year - 2017
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0187571
Subject(s) - ubiquitin , microbiology and biotechnology , ubiquitin protein ligases , biology , phenotype , signal transducing adaptor protein , ubiquitin ligase , genetic screen , f box protein , skp1 , signal transduction , genetics , gene
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 cindr RNAi transgenes during Drosophila eye development. In total, we identified 36 E3 ligases, as well as 4 Cullins, that modified the mild cindr RNA 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.