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and
*Institut Jacques Monod, Centre National de la Recherche
Scientifique-UMRC7592, Université Paris 7-Denis Diderot,
Paris Cedex 05, France;
The ORF YOL018c (TLG2) of Saccharomyces
cerevisiae encodes a protein that belongs to the syntaxin
protein family. The proteins of this family, t-SNAREs, are
present on target organelles and are thought to participate in the
specific interaction between vesicles and acceptor membranes in
intracellular membrane trafficking. TLG2 is not an
essential gene, and its deletion does not cause defects in the
secretory pathway. However, its deletion in cells lacking the vacuolar
ATPase subunit Vma2p leads to loss of viability, suggesting that Tlg2p
is involved in endocytosis. In tlg2VTT Biotechnology and Food
Research, FIN-02044 VTT, Finland;
Biozentrum, University
of Basel, CH-4056 Basel, Switzerland; and
§Department of
Molecular Genetics and Cell Biology, The University of Chicago,
Chicago, Illinois 60637
cells, internalization was normal for two endocytic markers, the pheromone 
-factor and the plasma membrane uracil permease. In contrast, degradation of -factor and uracil permease was delayed in
tlg2 cells. Internalization of positively charged
Nanogold shows that the endocytic pathway is perturbed in the mutant,
which accumulates Nanogold in primary endocytic vesicles and shows a
greatly reduced complement of early endosomes. These results strongly
suggest that Tlg2p is a t-SNARE involved in early endosome biogenesis.
Corresponding author. E-mail
address: haguenauer{at}ijm.jussieu.fr.
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