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Published online 15 May 2006. doi:10.1083/jcb.200510161
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 173, Number 4, 615-626
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Article

 The clathrin adaptor complex 1 directly binds to a sorting signal in Ste13p to reduce the rate of its trafficking to the late endosome of yeast

Christopher Foote and Steven F. Nothwehr

Division of Biological Sciences, University of Missouri, Columbia, MO 65211

Correspondence to Steven F. Nothwehr: nothwehrs{at}missouri.edu

Yeast trans-Golgi network (TGN) membrane proteins maintain steady-state localization by constantly cycling to and from endosomes. In this study, we examined the trafficking itinerary and molecular requirements for delivery of a model TGN protein A(F->A)–alkaline phosphatase (ALP) to the prevacuolar/endosomal compartment (PVC). A(F->A)-ALP was found to reach the PVC via early endosomes (EEs) with a half-time of ~60 min. Delivery of A(F->A)-ALP to the PVC was not dependent on either the GGA or adaptor protein 1 (AP-1) type of clathrin adaptors, which are thought to function in TGN to PVC and TGN to EE transport, respectively. Surprisingly, in cells lacking the function of both GGA and AP-1 adaptors, A(F->A)-ALP transport to the PVC was dramatically accelerated. A 12-residue cytosolic domain motif of A(F->A)-ALP was found to mediate direct binding to AP-1 and was sufficient to slow TGN->EE->PVC trafficking. These results suggest a model in which this novel sorting signal targets A(F->A)-ALP into clathrin/AP-1 vesicles at the EE for retrieval back to the TGN.

Abbreviations used in this paper: ALP, alkaline phosphatase; AP-1, adaptor protein 1; EE, early endosome; MBP, maltose-binding protein; PVC, prevacuolar/endosomal compartment.


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