Cofilin-mediated sorting and export of specific cargo from the Golgi apparatus in yeast.
Cofilin-mediated sorting and export of specific cargo from the Golgi apparatus in yeast.
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DOI：
10.1091/mbc.e11-09-0826
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发表时间：
2012-06
影响因子：
3.3
通讯作者：
Malhotra V
中科院分区：
文献类型：
--
作者：
Curwin AJ;von Blume J;Malhotra V
从高尔基体的分泌货物的排序仍然是一个难以捉摸的过程。以前的作用被确定为cofilin和Ca 2 + ATP酶SPCA 1在分选分泌货物从哺乳动物细胞的高尔基体。现在，它表明，酵母直向同源物cofilin和Pmr 1也需要在酵母中的高尔基体的选择性分泌货物的分选。在trans-Golgi网络（TGN）的货物分选分泌的机制知之甚少。我们先前报道了肌动蛋白切割蛋白cofilin和Ca 2 + ATP酶分泌途径钙ATP酶1（SPCA 1）在哺乳动物细胞TGN可溶性分泌货物的分选参与。现在，我们报告说，cofilin在酵母是需要出口的选择性分泌货物在高尔基体膜晚期。在cofilin突变体（cof 1 -8）的细胞，细胞壁蛋白Bgl 2的分泌速度降低，并保留在后期的高尔基体室，而质膜H+ ATP酶Pma 1，这是在同一类载体中运输，到达细胞表面。此外，羧肽酶Y（CPY）的液泡的分选延迟，CPY分泌的cof 1 -8细胞。SPCA 1（Pmr 1）的酵母直向同源物的损失表现出类似的分选缺陷，并显示与cof 1 -8的合成病。此外，PMR 1的过表达恢复了cof 1 -8细胞中Bgl 2的分泌。这些发现突出了cofilin和SPCA 1/Pmr 1在真核生物中TGN/晚期高尔基体膜上可溶性分泌蛋白的分选中的保守作用。
Sorting of secretory cargo from the Golgi remains an elusive process. Previously a role was identified for cofilin and the Ca2+ATPase SPCA1 in sorting of secretory cargo from the Golgi of mammalian cells. Now it is shown that the yeast orthologues cofilin and Pmr1 are also required for sorting of selective secretory cargo at the Golgi in yeast. The mechanism of cargo sorting at the trans-Golgi network (TGN) for secretion is poorly understood. We previously reported the involvement of the actin-severing protein cofilin and the Ca2+ ATPase secretory pathway calcium ATPase 1 (SPCA1) in the sorting of soluble secretory cargo at the TGN in mammalian cells. Now we report that cofilin in yeast is required for export of selective secretory cargo at the late Golgi membranes. In cofilin mutant (cof1-8) cells, the cell wall protein Bgl2 was secreted at a reduced rate and retained in a late Golgi compartment, whereas the plasma membrane H+ ATPase Pma1, which is transported in the same class of carriers, reached the cell surface. In addition, sorting of carboxypeptidase Y (CPY) to the vacuole was delayed, and CPY was secreted from cof1-8 cells. Loss of the yeast orthologue of SPCA1 (Pmr1) exhibited similar sorting defects and displayed synthetic sickness with cof1-8. In addition, overexpression of PMR1 restored Bgl2 secretion in cof1-8 cells. These findings highlight the conserved role of cofilin and SPCA1/Pmr1 in sorting of the soluble secretory proteins at the TGN/late Golgi membranes in eukaryotes.