Department of Genetics, 425-G Henry Mall, University of Wisconsin-Madison, Madison, WI 53706, USA.
Trends Plant Sci. 2012 Sep;17(9):526-37. doi: 10.1016/j.tplants.2012.05.006. Epub 2012 Jun 11.
Plants have evolved sophisticated mechanisms to recycle intracellular constituents. One gaining in appreciation is autophagy, which involves specialized vesicles engulfing and delivering unwanted cytoplasmic material to the vacuole for breakdown. Central to this process is the ubiquitin-fold protein autophagy (ATG)-8, which becomes tethered to the developing autophagic membranes by lipidation. Here, we review data showing that the ATG8 moiety provides a docking site not only for proteins that help shape the enclosing vesicles and promote their fusion with the tonoplast, but also for a host of receptors that recruit appropriate autophagic cargo. The identity of these receptors has dramatically altered the view of autophagy as being a relatively nonspecific mechanism to one that may selectively sequester aggregated proteins, protein complexes, organelles, and even invading pathogens.
植物已经进化出了复杂的机制来回收细胞内的成分。其中，自噬作用越来越受到重视，它涉及到专门的囊泡吞噬并将不需要的细胞质物质输送到液泡中进行分解。这个过程的核心是泛素样蛋白自噬（ATG）-8，它通过脂化与正在形成的自噬膜结合。在这里，我们回顾了一些数据，这些数据表明 ATG8 部分不仅为帮助形成封闭囊泡并促进其与液泡融合的蛋白质提供了一个 docking 位点，而且还为许多招募适当自噬货物的受体提供了一个 docking 位点。这些受体的身份极大地改变了人们对自噬作用的看法，使其从一种相对非特异性的机制转变为一种可能选择性地隔离聚集蛋白、蛋白复合物、细胞器甚至入侵病原体的机制。
