Molecular bases for the recognition of tyrosine-based sorting signals.
Molecular bases for the recognition of tyrosine-based sorting signals.
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DOI：
10.1083/jcb.145.5.923
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发表时间：
1999-05-31
期刊：
影响因子：
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通讯作者：
Dell'Angelica EC
中科院分区：
文献类型：
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作者：
Bonifacino JS;Dell'Angelica EC
高尔基体)分泌途径在很大程度上依赖于蛋白质胞浆结构域中包含的信号的分选(见参考文献19，24)。信号被认为与特定的识别分子相互作用，这些识别分子是参与形成膜结合的运输中间体(例如，包被的囊泡；参考文献2)的机械组件。因此，信号与其识别分子的相互作用被认为是导致货物跨膜蛋白选择性地被招募到新生运输中间体的关键事件。过去30年的研究已经提供了广泛的证据，证明在细胞内的多个位置发生了这种基本的蛋白质分选机制。然而，信号识别事件的分子细节直到最近才开始解开。这篇简短的综述将集中于最近的进展，阐明分子基础的识别一个子集的分类信号，称为基于酪氨酸的信号，由一个家族的适配器蛋白(AP)1复合体。
Golgi) secretory pathways is largely dependent upon sorting signals contained within the cytosolic domains of the proteins (reviewed in reference 19, 24). The signals are thought to interact with specific recognition molecules, which are components of the machinery involved in the formation of membrane-bound transport intermediates (eg, coated vesicles; reference 2). The interaction of signals with their recognition molecules is thus considered to be the key event leading to selective recruitment of cargo transmembrane proteins into the nascent transport intermediates. Studies over the past 30 years have provided extensive evidence for the occurrence of this basic mechanism of protein sorting at multiple sites within the cell. However, the molecular details of the signal-recognition event have only recently begun to be unraveled. This mini-review will focus on recent progress in the elucidation of the molecular bases for the recognition of a subset of sorting signals, referred to as tyrosine-based signals, by a family of adaptor protein (AP) 1 complexes.