Molecular analysis of UFE1, a Saccharomyces cerevisiae gene essential for spore formation and vegetative growth

Downing, Thomas A.; Storms, Reg K.

doi:10.1007/s002940050148

Cited by 3 publications

(3 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Because key regulators of the secretory pathway are encoded by essential housekeeping genes, the consequences of their absence are usually lethal and can therefore yield little information about their mode of action. This is indeed the case for the null mutants of Sed5p and Ufe1p in yeast (22,32,(66)(67)(68).…”

Section: Discussionmentioning

confidence: 54%

The Syntaxins SYP31 and SYP81 Control ER–Golgi Trafficking in the Plant Secretory Pathway

Bubeck

Scheuring

Hummel

et al. 2008

Traffic

View full text Add to dashboard Cite

†These authors contributed equally to this work.Overexpression of the Golgi and endoplasmic reticulum (ER) syntaxins SYP31 and SYP81 strongly inhibits constitutive secretion. By comparing the secreted reporter a-amylase with the ER-retained reporter a-amylase-HDEL, it was concluded that SYP81 overexpression inhibits both retrograde and anterograde transport, while SYP31 overexpression mainly affected anterograde transport. Of the other interacting SNAREs investigated, only the overexpression of MEMB11 led to an inhibition of protein secretion. Although the position of a fluorescent tag does not influence the correct localization of the fusion protein, only N-terminal-tagged SYP31 retained the ability of the untagged SNARE to inhibit transport. C-terminal-tagged SYP31 failed to exhibit this effect. Overexpression of both wild-type and N-terminal-tagged syntaxins caused standard Golgi marker proteins to redistribute into the ER. Nevertheless, green fluorescent protein (GFP)-SYP31 was still visible as fluorescent punctae, which, unlike SYP31-GFP, were resistant to brefeldin A treatment. Immunogold electron microscopy showed that endogenous SYP81 is not only present at the ER but also in the cis Golgi, indicating that this syntaxin cycles between these two organelles. However, when expressed at non-inhibitory levels, YFP-SYP81 was seen to locate principally to subdomains of the ER. These punctate structures were physically separated from the Golgi, suggesting that they might possibly reflect the position of ER import sites.

show abstract

Section: Discussionmentioning

confidence: 54%

The Syntaxins SYP31 and SYP81 Control ER–Golgi Trafficking in the Plant Secretory Pathway

Bubeck

Scheuring

Hummel

et al. 2008

Traffic

View full text Add to dashboard Cite

show abstract

“…In S. cerevisiae, Ufe1p (Qa-SNARE; Downing and Storms, 1996), Sec20p (Qb-SNARE; Sweet and Pelham, 1992), Use1p (Qc-SNARE; Dilcher et al, 2003) and Sec22p (R-SNARE; Lewis et al, 1997) predominantly localize at the endoplasmic reticulum (ER), and function in retrograde transport from the Golgi apparatus to the ER. The putative SNARE orthologs of A. fumigatus, A. nidulans, and N. crassa were collected by blastp search against the respective databases.…”

Section: Four Putative Snares That Localize To Ermentioning

confidence: 99%

Systematic analysis of SNARE localization in the filamentous fungus Aspergillus oryzae

Kuratsu¹,

Taura²,

Shoji³

et al. 2007

Fungal Genetics and Biology

View full text Add to dashboard Cite

“…Membrane fusion and vesicular transport is crucially controlled by SNARE proteins, which are typically single spanning transmembrane proteins (Jahn & Scheller, 2006). In Saccharomyces cerevisiae , the syntaxin (Qa‐SNARE) Ufe1 controls homotypic membrane fusion of endoplasmic reticulum (ER) membranes and retrograde transport of coatomer (COPI)‐coated vesicles from the cis ‐Golgi to the ER (Downing & Storms, 1996; Lewis et al , 1997; Patel et al , 1998). By contrast, the related Qa‐SNARE Sed5 mediates anterograde transport of COPII‐coated vesicles from the ER to the Golgi, and also the fusion of Golgi membranes (Hardwick & Pelham, 1992; Peng & Gallwitz, 2002).…”

Section: Introductionmentioning

confidence: 99%

SM‐protein‐controlled ER‐associated degradation discriminates between different SNAREs

Braun

Jentsch

2007

EMBO Reports

View full text Add to dashboard Cite

Endoplasmic reticulum (ER)-associated degradation (ERAD) is a specialized activity of the ubiquitin-proteasome system that is involved in clearing the ER of aberrant proteins and regulating the levels of specific ER-resident proteins. Here we show that the yeast ER-SNARE Ufe1, a syntaxin (Qa-SNARE) involved in ER membrane fusion and retrograde transport from the Golgi to the ER, is prone to degradation by an ERAD-like mechanism. Notably, Ufe1 is protected against degradation through binding to Sly1, a known SNARE regulator of the Sec1-Munc18 (SM) protein family. This mechanism is specific for Ufe1, as the stability of another Sly1 partner, the Golgi Qa-SNARE Sed5, is not influenced by Sly1 interaction. Thus, our findings identify Sly1 as a discriminating regulator of SNARE levels and indicate that Sly1-controlled ERAD might regulate the balance between different Qa-SNARE proteins.

show abstract

Molecular analysis of UFE1, a Saccharomyces cerevisiae gene essential for spore formation and vegetative growth

Cited by 3 publications

References 25 publications

The Syntaxins SYP31 and SYP81 Control ER–Golgi Trafficking in the Plant Secretory Pathway

The Syntaxins SYP31 and SYP81 Control ER–Golgi Trafficking in the Plant Secretory Pathway

Systematic analysis of SNARE localization in the filamentous fungus Aspergillus oryzae

SM‐protein‐controlled ER‐associated degradation discriminates between different SNAREs

Contact Info

Product

Resources

About