UNC-11, a Caenorhabditis elegans AP180 homologue, regulates the size and protein composition of synaptic vesicles
UNC-11, a Caenorhabditis elegans AP180 homologue, regulates the size and protein composition of synaptic vesicles
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DOI：
10.1091/mbc.10.7.2343
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发表时间：
1999-07-01
影响因子：
3.3
通讯作者：
Alfonso, A
中科院分区：
文献类型：
--
作者：
Nonet, ML;Holgado, AM;Alfonso, A
秀丽隐杆线虫的unc-11基因编码与哺乳动物脑特异性网格蛋白接头蛋白AP 180同源的蛋白质的多种同种型。该蛋白在神经系统中以高水平表达，在其他组织中以较低水平表达。在神经元中，β-11在突触前末梢富集，但也存在于细胞体中。UNC-11突变体在突触囊泡生物发生的两个方面有缺陷。首先，SNARE蛋白小突触泡蛋白被错误定位，不再只定位于突触囊泡。突触囊泡中小突触泡蛋白的减少可能是这些突变体中神经递质释放减少的原因。第二，unc-11突变体在突触处积累大的囊泡。我们建议，在突触囊泡生物发生过程中，ESTA-11蛋白介导的两个功能：它招募突触泡蛋白突触囊泡膜和它调节出芽囊泡的大小在网格蛋白外套组装。
The unc-11 gene of Caenorhabditis elegans encodes multiple isoforms of a protein homologous to the mammalian brain-specific clathrin-adaptor protein AP180. The UNC-11 protein is expressed at high levels in the nervous system and at lower levels in other tissues. Ln neurons, UNC-11 is enriched at presynaptic terminals but is also present in cell bodies. unc-11 mutants are defective in two aspects of synaptic vesicle biogenesis. First, the SNARE protein synaptobrevin is mislocalized, no longer being exclusively localized to synaptic vesicles. The reduction of synaptobrevin at synaptic vesicles is the probable cause of the reduced neurotransmitter release observed in these mutants. Second, unc-11 mutants accumulate large vesicles at synapses. We propose that the UNC-11 protein mediates two functions during synaptic vesicle biogenesis: it recruits synaptobrevin to synaptic vesicle membranes and it regulates the size of the budded vesicle during clathrin coat assembly.