Protein Sorting to the Storage Vacuoles of Plants: A Critical Appraisal
Protein Sorting to the Storage Vacuoles of Plants: A Critical Appraisal
复制标题
DOI：
10.1111/j.1600-0854.2005.00303.x
复制
发表时间：
2005-08
期刊：
影响因子：
4.5
通讯作者：
D. Robinson;Peter Oliviusson;G. Hinz
中科院分区：
文献类型：
--
作者：
D. Robinson;Peter Oliviusson;G. Hinz
植物细胞的液泡不再被认为是一个具有多功能特性的单室。现在有很多证据表明存在多个功能不同的空泡室，有些空泡室并排存在于同一个细胞中。因此，植物高尔基体面临着识别用于裂解和储存液泡的蛋白质并将它们从分泌蛋白流中分离出来的问题。酸水解酶是由植物细胞反式高尔基体上的BP - 80样受体分类的，与之相反，储存蛋白受体的鉴定在很多方面都类似于“寻找圣杯”。有几种候选的储存蛋白受体，但没有一个案例的证据是完全令人信服的。大部分问题在于对所研究的蛋白质排序序列缺乏共识。其他困难源于“脱离上下文”的异源表达研究。现在越来越多的证据表明，疏水序列参与了早期高尔基体中诱导蛋白质聚集体形成的过程，而经典的分选受体似乎并不需要。这篇综述严格审查了目前的情况，并对比了原位获得的数据和转基因获得的数据之间的差异。它强调了所谓的“密集囊泡”途径，并最终讨论了迄今为止被忽视的储存蛋白质加工酶的细胞内运输问题。
The vacuole of plant cells is no longer considered to be a single compartment with multifunctional properties. A lot of evidence now points to the presence of multiple functionally distinct vacuolar compartments, some existing side by side in the same cell. As a consequence, the plant Golgi apparatus is faced with the problem of recognizing proteins destined for lytic and storage vacuoles and segregating them individually from the flow of secretory proteins to the cell surface. In contrast to acid hydrolases, which are sorted by BP‐80‐like receptors at the trans‐Golgi of plant cells, the identification of receptors for storage proteins has in many ways resembled ‘the search for the Holy Grail’. There are several candidates for storage protein receptors, but in no single case is the evidence entirely convincing. Much of the problem lies in the lack of consensus, sorting sequences in the proteins investigated. Other difficulties stem from ‘out‐of‐context’ heterologous expression studies. Evidence is now accumulating for the participation of hydrophobic sequences in inducing the formation of protein aggregates in the early Golgi apparatus, for which classical sorting receptors do not appear to be necessary. This review critically examines the current situation and contrasts the differences between data obtained in situ and data obtained transgenically. It highlights the so‐called ‘dense‐vesicle’ pathway and culminates with a discussion on the hitherto neglected problem of the intracellular transport of storage protein processing enzymes.