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Vol. 9, Issue 12, 3383-3397, December 1998

The Syntaxin Tlg1p Mediates Trafficking of Chitin Synthase III to Polarized Growth Sites in Yeast

Joost C. M. Holthuis,* Benjamin J. Nichols, and Hugh R. B. Pelhamdagger

Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom

Tlg1p and Tlg2p, members of the syntaxin family of SNAREs in yeast, have been implicated in both endocytosis and the retention of late Golgi markers. We have investigated the functions of these and the other endocytic syntaxins Pep12p and Vam3p. Remarkably, growth is possible in the absence of all four proteins. In the absence of the others, Pep12p and Tlg1p can each create endosomes accessible to the endocytic tracer dye FM4-64. However, although Pep12p is required for the ligand-induced internalization of the alpha  factor receptor and its passage via Pep12p-containing membranes to the vacuole, Tlg1p is not. In contrast, Tlg1p is required for the efficient localization of the catalytic subunit of chitin synthase III (Chs3p) to the bud neck, a process that involves endocytosis and polarized delivery of Chs3p. In wild-type cells, internalized Chs3p cofractionates with Tlg1p and Tlg2p, and in a strain lacking the other endocytic syntaxins, either Tlg1p or Tlg2p is sufficient for correct localization of the enzyme. Pep12p is neither necessary nor sufficient for this process. We conclude that there are two endocytic routes in yeast that can operate independently and that Tlg1p is located at the junction of one of these with the polarized exocytic pathway.


dagger    Corresponding author. E-mail address: hp{at}mrc-lmb.cam.ac.uk.
*   Present address: Department of Cell Biology and Histology, Academic Medical Center L3, University of Amsterdam, Meibergdreef 15, 1105 AZ Amsterdam, The Netherlands.


Molecular Biology of the Cell
Vol. 9, 3383-3397, December 1998
Copyright © 1998 by The American Society for Cell Biology



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