The syntaxin homolog AtPEP12p resides on a late post-Golgi compartment in plants
The syntaxin homolog AtPEP12p resides on a late post-Golgi compartment in plants
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DOI：
10.1105/tpc.9.4.571
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发表时间：
1997-04-01
期刊：
影响因子：
11.6
通讯作者：
Raikhel, NV
中科院分区：
文献类型：
--
作者：
Conceicao, ADS;MartyMazars, D;Raikhel, NV
可溶性蛋白质通过膜结合囊泡通过分泌途径转运至植物液泡。将囊泡靶向适当的细胞器需要几种已在酵母和哺乳动物系统中表征的膜结合和可溶性因子。例如，酵母PEP12蛋白是一种突触蛋白同源物，参与蛋白质向酵母液泡的转运。此前，我们通过酵母pep12突变体的功能互补分离了PEP12的拟南芥同源物。针对 AtPEP12 细胞质部分的抗体已制备并用于该蛋白的细胞内定位。生化分析表明，AtPEP12 不定位于拟南芥植物的内质网、高尔基体、质膜或液泡膜；此外，根据生化和电子显微镜免疫金标记分析，AtPEP12 可能定位于液泡通路中的后高尔基体区室。
Soluble proteins are transported to the plant vacuole through the secretory pathway via membrane-bound vesicles. Targeting of vesicles to appropriate organelles requires several membrane-bound and soluble factors that have been characterized in yeast and mammalian systems. For example, the yeast PEP12 protein is a syntaxin homolog that is involved in protein transport to the yeast vacuole, Previously, we isolated an Arabidopsis thaliana homolog of PEP12 by functional complementation of the yeast pep12 mutant. Antibodies raised against the cytoplasmic portion of AtPEP12 have been prepared and used for intracellular localization of this protein. Biochemical analysis indicates that AtPEP12 does not localize to the endoplasmic reticulum, Golgi apparatus, plasma membrane, or tonoplast in Arabidopsis plants; furthermore, based on biochemical and electron microscopy immunogold labeling analyses, AtPEP12 is likely to be localized to a post-Golgi compartment in the vacuolar pathway.