A putative vacuolar cargo receptor partially colocalizes with AtPEP12p on a prevacuolar compartment in Arabidopsis roots.
A putative vacuolar cargo receptor partially colocalizes with AtPEP12p on a prevacuolar compartment in Arabidopsis roots.
复制标题
假定的液泡货物受体与拟南芥根部液泡前区室中的 AtPEP12p 部分共定位。
DOI：
10.1073/pnas.95.17.9920
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发表时间：
1998
影响因子：
11.1
通讯作者：
Raikhel,NV
中科院分区：
文献类型：
--
作者：
Sanderfoot,AA;Ahmed,SU;Marty-Mazars,D;Rapoport,I;Kirchhausen,T;Marty,F;Raikhel,NV
将蛋白质货物靶向到液泡/溶酶体是一个多步骤过程，其似乎在哺乳动物、酵母和植物细胞之间具有保守特征。在每种情况下，一些可溶性空泡/溶酶体蛋白被认为是由跨膜货物受体在反式高尔基体网络（TGN），重新定向这些蛋白到网格蛋白包被的囊泡。然后，这些囊泡似乎被运输到前液泡/内体的运输机械，需要在其他囊泡靶向步骤中确定的成分，如N-乙基马来酰亚胺敏感因子（NSF），可溶性NSF附着蛋白（SNAP），SNAP受体（SNARE），rab型GTP酶和Sec 1 p同源物。这种运输机制的两个可能成员已经从拟南芥中鉴定出来：AtPEP 12 p，一种位于我们现在所说的前液泡区室的t-SNARE，以及AtELP，一种与哺乳动物和酵母跨膜货物受体共享许多共同特征的蛋白质。在这里，我们进一步研究了AtELP的细胞内分布。我们发现AtELP位于拟南芥根细胞的trans-Golgi，其C端可以优先与哺乳动物TGN特异的AP-1网格蛋白-适配体复合物在体外相互作用，这表明AtELP可能在TGN的网格蛋白包被的囊泡定向运输中发挥作用。此外，一致的作用，在贩运的液泡货物，我们发现，AtELP部分共定位与AtPEP 12 p的prevacuolar室。
Targeting of protein cargo to the vacuole/lysosome is a multistep process that appears to have conserved features between mammalian, yeast, and plant cells. In each case, some soluble vacuolar/lysosomal proteins are believed to be bound by transmembrane cargo receptors in the trans-Golgi network (TGN) that redirect these proteins into clathrin-coated vesicles. These vesicles then appear to be transported to the prevacuole/endosome by a trafficking machinery that requires components identified in other vesicle-targeting steps such asN-ethylmaleimide-sensitive factor (NSF), soluble NSF attachment protein (SNAP), SNAP receptors (SNAREs), rab-type GTPases, and Sec1p homologs. Two likely members of this trafficking machinery have been characterized fromArabidopsis thaliana: AtPEP12p, a t-SNARE that resides on a what we now call a prevacuolar compartment, and AtELP, a protein that shares many common features with mammalian and yeast transmembrane cargo receptors. Here, we have further investigated the intracellular distribution of AtELP. We have found that AtELP is located at the trans-Golgi ofArabidopsisroot cells, and that its C terminus can preferentially interactin vitrowith the mammalian TGN-specific AP-1 clathrin–adapter complex, suggesting a likely role in clathrin-coated, vesicle-directed trafficking at the TGN. Further, consistent with a role in trafficking of vacuolar cargo, we have found that AtELP partially colocalizes with AtPEP12p on a prevacuolar compartment.