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Vol. 9, Issue 12, 3383-3397, December 1998
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
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.
Corresponding author. E-mail address:
hp{at}mrc-lmb.cam.ac.uk.
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