Transport of ricin and 2S albumin precursors to the storage vacuoles of Ricinus communis endosperm involves the Golgi and VSR-like receptors
Transport of ricin and 2S albumin precursors to the storage vacuoles of Ricinus communis endosperm involves the Golgi and VSR-like receptors
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DOI：
10.1111/j.1365-313x.2004.02167.x
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发表时间：
2004-09-01
期刊：
影响因子：
7.2
通讯作者：
Frigerio, L
中科院分区：
文献类型：
--
作者：
Jolliffe, NA;Brown, JC;Frigerio, L
我们研究了Proricin和pro 2S白蛋白向发育中的蓖麻子（Ricinus communis L.）胚乳免疫电子显微镜和细胞分级显示，这两种蛋白质旅行通过高尔基体和共定位在其整个路线的存储液泡。在到达PSV的过程中，蛋白质共定位于大的（>200 nm）囊泡中，这可能代表发育中的储存液泡。我们进一步表明，序列特异性空泡分选信号的proricin和pro2 SA结合在体外的蛋白质，具有较高的序列相似性的VSR/AtELP/BP-80空泡分选受体家族的成员，通常与网格蛋白介导的交通裂解空泡。这些研究结果的影响，在目前的模型蛋白质分选储存液泡进行了讨论。
We have studied the transport of proricin and pro2S albumin to the protein storage vacuoles of developing castor bean (Ricinus communis L.) endosperm. Immunoelectron microscopy and cell fractionation reveal that both proteins travel through the Golgi apparatus and co-localize throughout their route to the storage vacuole. En route to the PSV, the proteins co-localize in large (>200 nm) vesicles, which are likely to represent developing storage vacuoles. We further show that the sequence-specific vacuolar sorting signals of both proricin and pro2SA bind in vitro to proteins that have high sequence similarity to members of the VSR/AtELP/BP-80 vacuolar sorting receptor family, generally associated with clathrin-mediated traffic to the lytic vacuole. The implications of these findings in relation to the current model for protein sorting to storage vacuoles are discussed.