Skip to main content
Cellular and Molecular Life Sciences: CMLS logoLink to Cellular and Molecular Life Sciences: CMLS
. 2001 Jul;58(8):1067–1084. doi: 10.1007/PL00000922

Trans-Golgi network sorting

F Gu 1, CM Crump 1, G Thomas 1
PMCID: PMC1424219  NIHMSID: NIHMS8396  PMID: 11529500

Abstract:

The trans-Golgi network (TGN) is a major secretory pathway sorting station that directs newly synthesized proteins to different subcellular destinations. The TGN also receives extracellular materials and recycled molecules from endocytic compartments. In this review, we summarize recent progress on understanding TGN structure and the dynamics of trafficking to and from this compartment. Protein sorting into different transport vesicles requires specific interactions between sorting motifs on the cargo molecules and vesicle coat components that recognize these motifs. Current understanding of the various targeting signals and vesicle coat components that are involved in TGN sorting are discussed, as well as the molecules that participate in retrieval to this compartment in both yeast and mammalian cells. Besides proteins, lipids and lipid-modifying enzymes also participate actively in the formation of secretory vesicles. The possible mechanisms of action of these lipid hydrolases and lipid kinases are discussed. Finally, we summarize the fundamentally different apical and basolateral cell surface delivery mechanisms and the current facts and hypotheses on protein sorting from the TGN into the regulated secretory pathway in neuroendocrine cells.

Keywords: Key words: Trans-Golgi network; coat protein; sorting signal; lipid; lipid kinase; apical targeting; basolateral sorting; regulated secretion.

Footnotes

Received 2 November 2000; received after revision 19 February 2001; accepted 19 February 2001


Articles from Cellular and Molecular Life Sciences: CMLS are provided here courtesy of Springer

RESOURCES