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doi: 10.1242/10.1242/jcs.00270
Commentary |
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,
-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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