Targeting of transmembrane proteins to different compartments of the endocytic and late (post-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 (e.g., 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...

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