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Originally published as MBC in Press, 10.1091/mbc.E02-10-0686 on December 25, 2002
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Vol. 14, Issue 4, 1319-1333, April 2003

The Synaptojanin-like Protein Inp53/Sjl3 Functions with Clathrin in a Yeast TGN-to-Endosome Pathway Distinct from the GGA Protein-dependent Pathway

Seon-Ah Ha,* Javad Torabinejad,dagger Daryll B. DeWald,dagger Markus R. Wenk,Dagger Louise Lucast,Dagger Pietro De Camilli,Dagger Richard A. Newitt,§ Ruedi Aebersold,§ and Steven F. Nothwehr*

 *Division of Biological Sciences, University of Missouri, Columbia, Missouri 65211;  dagger Department of Biology, Utah State University, Logan, Utah 84322;  Dagger Department of Cell Biology and Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510; and  §Institute for Systems Biology, Seattle, Washington 98103

Yeast TGN resident proteins that frequently cycle between the TGN and endosomes are much more slowly transported to the prevacuolar/late endosomal compartment (PVC) than other proteins. However, TGN protein transport to the PVC is accelerated in mutants lacking function of Inp53p. Inp53p contains a SacI polyphosphoinositide phosphatase domain, a 5-phosphatase domain, and a proline-rich domain. Here we show that all three domains are required to mediate "slow delivery" of TGN proteins into the PVC. Although deletion of the proline-rich domain did not affect general membrane association, it caused localization to become less specific. The proline-rich domain was shown to bind to two proteins, including clathrin heavy chain, Chc1p. Unlike chc1 mutants, inp53 mutants do not mislocalize TGN proteins to the cell surface, consistent with the idea that Chc1p and Inp53p act at a common vesicular trafficking step but that Chc1p is used at other steps also. Like mutations in the AP-1 adaptor complex, mutations in INP53 exhibit synthetic growth and transport defects when combined with mutations in the GGA proteins. Taken together with other recent studies, our results suggest that Inp53p and AP-1/clathrin act together in a TGN-to-early endosome pathway distinct from the direct TGN-to-PVC pathway mediated by GGA/clathrin.

Corresponding author and present address: Département de Biologie Cellulaire, Sciences III, Quai Ernest-Ansermet 30, CH-1211 Genève 4, Switzerland. E-mail address: nothwehrs{at}missouri.edu.

Molecular Biology of the Cell
Vol. 14, 1319-1333, April 2003
Copyright © 2003 by The American Society for Cell Biology


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