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Vol. 13, Issue 10, 3672-3682, October 2002

ARF1·GTP, Tyrosine-based Signals, and Phosphatidylinositol 4,5-Bisphosphate Constitute a Minimal Machinery to Recruit the AP-1 Clathrin Adaptor to Membranes

Pascal Crottet,^* Daniel M. Meyer,^* Jack Rohrer, and Martin Spiess^*

 ^*Biozentrum, University of Basel, CH-4056 Basel, Switzerland; and  Institute of Physiology, University of Zürich, CH-8057 Zürich, Switzerland

At the trans-Golgi network, clathrin coats containing AP-1 adaptor complexes are formed in an ARF1-dependent manner, generating vesicles transporting cargo proteins to endosomes. The mechanism of site-specific targeting of AP-1 and the role of cargo are poorly understood. We have developed an in vitro assay to study the recruitment of purified AP-1 adaptors to chemically defined liposomes presenting peptides corresponding to tyrosine-based sorting motifs. AP-1 recruitment was found to be dependent on myristoylated ARF1, GTP or nonhydrolyzable GTP-analogs, tyrosine signals, and small amounts of phosphoinositides, most prominently phosphatidylinositol 4,5-bisphosphate, in the absence of any additional cytosolic or membrane bound proteins. AP-1 from cytosol could be recruited to a tyrosine signal independently of the lipid composition, but the rate of recruitment was increased by phosphatidylinositol 4,5-bisphosphate. The results thus indicate that cargo proteins are involved in coat recruitment and that the local lipid composition contributes to specifying the site of vesicle formation.

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Corresponding author. E-mail address: Martin.Spiess{at}unibas.ch.

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Molecular Biology of the Cell
Vol. 13, 3672-3682, October 2002
Copyright © 2002 by The American Society for Cell Biology

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