Dreier Lars, Burbea Michelle, Kaplan Joshua M
Department of Molecular Biology, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts 02114, USA.
Neuron. 2005 Apr 7;46(1):51-64. doi: 10.1016/j.neuron.2004.12.058.
Ubiquitin-mediated protein degradation has been proposed to play an important role in regulating synaptic transmission. Here we show that LIN-23, the substrate binding subunit of a Skp1/Cullin/F Box (SCF) ubiquitin ligase, regulates the abundance of the glutamate receptor GLR-1 in the ventral nerve cord of C. elegans. Mutants lacking lin-23 had an increased abundance of GLR-1 in the ventral cord. The increase of GLR-1 was not caused by changes in the ubiquitination of GLR-1. Instead, SCF(LIN-23) regulates GLR-1 through the beta-catenin homolog BAR-1 and the TCF/Lef transcription factor homolog POP-1. We hypothesize that LIN-23-mediated degradation of BAR-1 beta-catenin regulates the transcription of Wnt target genes, which in turn alter postsynaptic properties.
泛素介导的蛋白质降解被认为在调节突触传递中起重要作用。在这里，我们表明，Skp1/Cullin/F盒（SCF）泛素连接酶的底物结合亚基LIN-23调节秀丽隐杆线虫腹侧神经索中谷氨酸受体GLR-1的丰度。缺乏lin-23的突变体腹侧索中GLR-1的丰度增加。GLR-1的增加不是由GLR-1泛素化的变化引起的。相反，SCF（LIN-23）通过β-连环蛋白同源物BAR-1和TCF/Lef转录因子同源物POP-1调节GLR-1。我们假设LIN-23介导的BAR-1β-连环蛋白降解调节Wnt靶基因的转录，进而改变突触后特性。
