High impact information on SLY1

• This mechanism likely involves the Sec1 homolog Sly1, which we identified in isolated docking complexes [1].
• Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes [2].
• The temperature-sensitive phenotype of sec34-2 is suppressed by the rab GTPase Ypt1p that functions early in the secretory pathway, or by the dominant form of the ER to Golgi complex target-SNARE (soluble N-ethylmaleimide sensitive fusion protein attachment protein receptor)-associated protein Sly1p, Sly1-20p [3].
• In the strain carrying our ts allele of SLY1, accumulation of the carboxypeptidase Y precursor was detected at the nonpermissive temperature, indicating that the secretory pathway is defective [4].
• Sequence analysis revealed that this gene is SLY1, encoding a protein essential for protein and vesicle transport between the endoplasmic reticulum and the Golgi apparatus [4].

Biological context of SLY1

• SLY1 is an essential gene for vesicular transport between the ER and the early Golgi apparatus in Saccharomyces cerevisiae [5].
• A temperature-sensitive sly1 mutant arrests the vesicular transport from the ER to Golgi compartments at 37 degrees C. We screened for multicopy suppressor genes that restore the colony formation of the sly1(ts) mutant to discover functionally interacting components [6].
• The temperature-sensitive phenotype of sec35-1 is efficiently suppressed by YPT1, which encodes the rab-like GTPase required early in the secretory pathway, or by SLY1-20, which encodes a dominant form of the ER to Golgi target -SNARE-associated protein Sly1p [7].
• Here we describe a systematic, structure-based mutational analysis of the yeast SM protein Sly1p, which was previously shown to function in anterograde endoplasmic reticulum (ER)-to-Golgi and intra-Golgi protein transport [8].

Anatomical context of SLY1

• In vitro formation of this complex on different membranes in yeast lysate was enhanced by the addition of recombinant Sly1 [5].

Associations of SLY1 with chemical compounds

• Assembly of v-SNARE-t-SNARE targeting complexes is modulated by members of the Sec1-Sly1 protein family, and by small guanosine triphosphatases termed Rabs [9].

Other interactions of SLY1

• In addition, overexpression of the small GTP-binding protein Ypt1p, or of a gain if function mutant (SLY1-20) of the t-SNARE associated protein Sly1p, also confers temperature resistance [10].
• Saccharomyces cerevisiae Sly1 protein is a member of the Sec1/Munc18-family proteins, which are essential for vesicular trafficking, but their exact biological roles are yet to be determined [6].
• DSL1 was identified through its genetic interaction with SLY1, which encodes a t-SNARE-interacting protein that functions in endoplasmic reticulum (ER)-to-Golgi traffic [11].
• These results indicate that binding of Sly1 to Sed5 enhances trans-SNARE complex formation [5].
• In the wildtype, a detectable amount of Sly1 was found in the complex between Sed5 and the v-SNARE Bet1 [5].

References