Open AccessHeterologous Expression of Syntaxin 6 in Saccharomyces cerevisiae
Author(s) -
Martin Götte,
Andrea Stadtbäumer
Publication year - 2002
Publication title -
biological research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.127
H-Index - 55
eISSN - 0717-6287
pISSN - 0716-9760
DOI - 10.4067/s0716-97602002000300009
Subject(s) - syntaxin , syntaxin 3 , microbiology and biotechnology , saccharomyces cerevisiae , biology , mutant , vacuolar protein sorting , cytoplasm , golgi apparatus , retromer , yeast , vacuole , membrane protein , gene , endoplasmic reticulum , genetics , membrane
The molecular mechanisms of vesicular protein transport in eukaryotic cells are highly conserved. Members of the syntaxin family play a pivotal role in the membrane fusion process. We have expressed rat syntaxin 6 and its cytoplasmic domain in wild-type and pep12 mutant strains of Saccharomyces cerevisiae to elucidate the role of the syntaxin 6-dependent vesicular trafficking step in yeast. Immunofluorescence microscopy revealed a punctate, Golgi-like staining pattern for syntaxin 6, which only partially overlapped with Pep12p in wild-type yeast cells. In contrast to Pep12p, syntaxin 6 was not mislocalized to the vacuole upon expression from 2 micron vectors, which might be attributed to conserved sorting and retention signals. Syntaxin 6 was not capable of complementing the sorting and maturation defects of the vacuolar hydrolase CPY in pep12 null mutants. No dominant negative effects of either syntaxin 6 or syntaxin 6 delta C overexpression on CPY sorting and maturation were observed in wild-type yeast cells. We conclude that syntaxin 6 and Pep12p do not act at the same vesicular trafficking step(s) in yeast and higher eukaryotes.