School of Life Sciences, Oxford Brookes University, Headington Campus, Gipsy Lane, Oxford OX30BP, UK.
Mol Plant. 2011 Mar;4(2):220-8. doi: 10.1093/mp/ssq082. Epub 2011 Feb 9.
In all eukaryotes, the Golgi apparatus is the main site of protein glycosylation. It is widely accepted that the glycosidases and glycosyltransferases involved in N-glycan processing are found concentrated within the Golgi stack where they provide their function. This means that enzymes catalyzing early steps in the processing pathway are located mainly at the cis-side, whereas late-acting enzymes mostly locate to the trans-side of the stacks, creating a non-uniform distribution along the cis-trans axis of the Golgi. There is compelling evidence that the information for their sorting to specific Golgi cisternae depends on signals encoded in the proteins themselves as well as on the trafficking machinery that recognizes these signals and it is believed that cisternal sub-compartmentalization is achieved and maintained by a combination of retention and retrieval mechanisms. Yet, the signals, mechanism(s), and molecular factors involved are still unknown. Here, we address recent findings and summarize the current understanding of this fundamental process in plant cell biology.
在所有真核生物中，高尔基体是蛋白质糖基化的主要场所。人们普遍认为，参与 N-聚糖加工的糖苷酶和糖基转移酶集中在高尔基体堆叠中，在那里发挥其功能。这意味着催化加工途径早期步骤的酶主要位于顺面，而晚期作用的酶主要位于堆叠的反面，从而在高尔基体顺面-反面轴上形成不均匀的分布。有确凿的证据表明，将它们分拣到特定的高尔基体潴泡取决于蛋白质本身编码的信息以及识别这些信号的运输机制，人们相信潴泡的亚区室化是通过保留和检索机制的组合来实现和维持的。然而，相关的信号、机制和分子因素仍不清楚。在这里，我们将介绍最近的发现，并总结目前对植物细胞生物学中这一基本过程的理解。
