H. Abeliovich et al., TLG2P, A YEAST SYNTAXIN HOMOLOG THAT RESIDES ON THE GOLGI AND ENDOCYTIC STRUCTURES, The Journal of biological chemistry, 273(19), 1998, pp. 11719-11727
Intracellular membrane fusion events in eukaryotic cells are thought t
o be mediated by protein-protein interactions between soluble N-ethylm
aleimide-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 posse
ssing a sizeable hydrophilic domain of 63 amino acids that is C-termin
al 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 Gels. 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 traffickin
g. Based on these findings we propose that Tlg2p is a t-SNARE that fun
ctions in transport from the endosome to the late Golgi and on the end
ocytic pathway.