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首页> 外文期刊>Neuron >Identification of E2/E3 ubiquitinating enzymes and caspase activity regulating Drosophila sensory neuron dendrite pruning.
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Identification of E2/E3 ubiquitinating enzymes and caspase activity regulating Drosophila sensory neuron dendrite pruning.

机译：鉴定E2 / E3泛素化酶和调节果蝇感觉神经元树突修剪的半胱天冬酶活性。

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摘要

Ubiquitin-proteasome system (UPS) is a multistep protein degradation machinery implicated in many diseases. In the nervous system, UPS regulates remodeling and degradation of neuronal processes and is linked to Wallerian axonal degeneration, though the ubiquitin ligases that confer substrate specificity remain unknown. Having shown previously that class IV dendritic arborization (C4da) sensory neurons in Drosophila undergo UPS-mediated dendritic pruning during metamorphosis, we conducted an E2/E3 ubiquitinating enzyme mutant screen, revealing that mutation in ubcD1, an E2 ubiquitin-conjugating enzyme, resulted in retention of C4da neuron dendrites during metamorphosis. Further, we found that UPS activation likely leads to UbcD1-mediated degradation of DIAP1, a caspase-antagonizing E3 ligase. This allows for local activation of the Dronc caspase, thereby preserving C4da neurons while severing their dendrites. Thus, in addition to uncovering E2/E3 ubiquitinating enzymes for dendrite pruning, this study provides a mechanistic link between UPS and the apoptotic machinery in regulating neuronal process remodeling.
机译：泛素-蛋白酶体系统（UPS）是涉及许多疾病的多步蛋白质降解机制。在神经系统中，UPS调节神经元过程的重塑和降解，并且与Wallerian轴突变性有关，尽管赋予底物特异性的泛素连接酶尚不清楚。先前已经证明果蝇中的IV类树突状树突（C4da）感觉神经元在变态过程中经历了UPS介导的树突修剪，我们进行了E2 / E3泛素化酶突变体筛选，揭示了ubcD1（E2泛素缀合酶）中的突变导致在变态过程中保留C4da神经元树突。此外，我们发现UPS激活可能导致UbcD1介导的DIAP1降解，一种Caspase拮抗E3连接酶。这允许Dronc caspase的局部激活，从而在切断C4da神经元的树突的同时保留它们。因此，除了发现用于树突修剪的E2 / E3泛素化酶外，本研究还提供了UPS与凋亡机制之间的机制联系，以调节神经元过程重塑。

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