Maintaining the integrity and function of the presynaptic neurotransmitter release apparatus is a demanding process for a post-mitotic neuron; the mechanisms behind it are still unclear. BSN (bassoon), an active zone scaffolding protein, has been implicated in the control of presynaptic macroautophagy/autophagy, a process we recently showed depends on poly-ubiquitination of synaptic proteins. Moreover, loss of BSN was found to lead to smaller synaptic vesicle (SV) pools and younger pools of the SV protein SV2. Of note, the E3 ligase PRKN/parkin appears to be involved in BSN deficiency-related changes in autophagy levels, as shRNA-mediated knockdown of PRKN counteracts BSN-deficiency and rescues decreased SV protein levels as well as impaired SV recycling in primary cultured neurons. These data imply that BSN and PRKN act in concert to control presynaptic autophagy and maintain presynaptic proteostasis and SV turnover at the physiologically required levels.

保持突触前神经递质释放装置的完整性和功能对有丝分裂后神经元来说是一个要求很高的过程；其背后的机制尚不清楚。BSN（巴松管）是一种活性区支架蛋白，与突触前巨自噬/自噬的控制有关，我们最近展示的这一过程依赖于突触蛋白的多泛素化。此外，发现 BSN 的丢失导致更小的突触小泡 (SV) 池和更年轻的 SV 蛋白 SV2 池。值得注意的是，E3 连接酶 PRKN/parkin 似乎参与了 BSN 缺陷相关的自噬水平变化，因为 shRNA 介导的 PRKN 敲低抵消了 BSN 缺陷并挽救了 SV 蛋白水平降低以及原代培养神经元中 SV 循环受损.