作者: Zoltán Lipinszki , Margit Pál , Olga Nagy , Péter Deák , Eva Hunyadi-Gulyas
DOI: 10.1111/J.1742-4658.2011.08383.X
关键词:
摘要: Polyubiquitin receptors execute the targeting of polyubiquitylated proteins to 26S proteasome. In vitro studies indicate that disturbance physiological balance among different receptor impairs proteasomal degradation proteins. To study consequences shifting in vivo equilibrium between p54/Rpn10 and Dsk2/dUbqln extraproteasomal polyubiquitin receptors, transgenic Drosophila lines were constructed which overexpression or RNA interference-mediated silencing these can be induced. Flies overexpressing Flag-p54 viable fertile, without any detectable morphological abnormalities, although accumulation demonstrated a certain level proteolytic disturbance. was assembled into proteasome could fully complement lethal phenotype p54 null mutant line. The Dsk2 caused severe abnormalities late pupal stages, leading pharate adult lethality, accompanied by huge highly rescued double line coexpressing Flag-Dsk2 Flag-p54. Although it did not restore defects; even more Significant differences found Dsk2-26S interaction melanogaster as compared with Saccharomyces cerevisiae. yeast, interact only ΔRpn10 proteasomes wild-type one. Drosophila, does Δp54 proteasomes, but restored complementing deletion