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doi: 10.1242/10.1242/jcs.00270


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Journal of Cell Science 116, 763-771 (2003)
doi: 10.1242/jcs.00270


Commentary

Changing directions: clathrin-mediated transport between the Golgi and endosomes

Ina Hinners and Sharon A. Tooze*

Secretory Pathways Laboratory, Cancer Research UK London Research Institute, 44 Lincoln's Inn Fields, London WC2A 3PX, UK

* Author for correspondence (e-mail: sharon.tooze{at}cancer.org.uk)

Clathrin-coated vesicles mediate transport between the trans-Golgi network (TGN) and endosomes. In recent years there has been tremendous progress in identifying factors involved in anterograde and retrograde transport steps. The well-characterised heterotetrameric clathrin adaptor complex AP-1 has long been thought to mediate anterograde transport from the TGN to endosomes. However, recent studies of AP-1-knockout mice implicate AP-1 in retrograde as well as anterograde transport. The recently identified Golgi-associated, {gamma}-ear-containg, ARF-binding (GGA) proteins share functional similarities with tetrameric adaptor complexes and are essential for anterograde transport of mannose-6-phosphate receptors, the sorting receptors for soluble lysosomal enzymes. To date, it is not clear whether GGAs and AP-1 mediate transport in different directions, act in parallel pathways, or cooperate in the same transport steps. Recent data have shed light on the locations, functions and interactions of AP-1 and GGA proteins. These data provide support for the role of both in anterograde transport from the Golgi complex.

Key words: AP-1, GGA protein, Golgi, Endosome, TGN


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