Tlg2p, a yeast syntaxin homolog that resides on the Golgi and endocytic structures.

Intracellular membrane fusion events in eukaryotic cells are thought to be mediated by protein-protein interactions between soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex proteins. We have identified and analyzed a new yeast syntaxin homolog, Tlg2p. Tlg2p is unique among known syntaxin family proteins in possessing a sizeable hydrophilic domain ...
of 63 amino acids that is C-terminal to the membrane spanning region and nonessential for Tlg2p function. Tlg2p resides on the endosome and late Golgi by co-localization with an endocytic intermediate and co-fractionation with markers for both endosomes and late Golgi. Cells depleted for Tlg2p missort a portion of carboxypeptidase Y and are defective in endocytosis. In addition, we report that Tlg2p forms a SEC18-dependent SNARE complex with Snc2p, a vesicle SNARE known to function in Golgi to plasma membrane trafficking. Based on these findings we propose that Tlg2p is a t-SNARE that functions in transport from the endosome to the late Golgi and on the endocytic pathway.
Mesh Terms:
Adenosine Triphosphatases, Amino Acid Sequence, Carboxypeptidases, Cathepsin A, Cell Compartmentation, Endocytosis, Fungal Proteins, Golgi Apparatus, Macromolecular Substances, Membrane Fusion, Membrane Proteins, Membrane Transport Proteins, Molecular Sequence Data, Mutagenesis, Insertional, Qa-SNARE Proteins, R-SNARE Proteins, Receptors, Cytoplasmic and Nuclear, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Vesicular Transport Proteins
J. Biol. Chem.
Date: May. 08, 1998
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