ArticleFEMS yeast research2013
Characterization of an M28 metalloprotease family member residing in the yeast vacuole.
Article in FEMS yeast research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Unveiling antibiofilm potential: proteins from Priestia sp. targeting Staphylococcus aureus biofilm formation.Antonie van Leeuwenhoek · 2024Article
- The Capture of a Disabled Proteasome Identifies Erg25 as a Substrate for Endoplasmic Reticulum Associated Degradation.Molecular & cellular proteomics : MCP · 2020Article
- TORC1 regulates vacuole membrane composition through ubiquitin- and ESCRT-dependent microautophagy.The Journal of cell biology · 2020Article
- Review
- Yeast as a tool to explore cathepsin D function.Microbial cell (Graz, Austria) · 2015Review
- Non-repair pathways for minimizing protein isoaspartyl damage in the yeast Saccharomyces cerevisiae.The Journal of biological chemistry · 2014Article
- The proteolytic landscape of the yeast vacuole.Cellular logistics · 2014Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The systematic and complete characterization of the Saccharomyces cerevisiae genome and proteome has been stalled in some cases by misannotated genes. One such gene is YBR074W, which was initially annotated as two independent open reading frames (ORFs). We now report on Ybr074, a metalloprotease family member that was initially predicted to reside in the endoplasmic reticulum (ER). Therefore, we tested the hypothesis that Ybr074 may be an ER quality control protease. Instead, indirect immunofluorescence images indicate that Ybr074 is a vacuolar protein, and by employing protease protection assays, we demonstrate that a conserved M28 metalloprotease domain is oriented within the lumen. Involvement of Ybr074 in ER protein quality control was ruled out by examining the stabilities of several well-characterized substrates in strains lacking Ybr074. Finally, using a proteomic approach, we show that disrupting Ybr074 function affects the levels of select factors implicated in vacuolar trafficking and osmoregulation. Together, our data indicate that Ybr074 is the only multispanning vacuolar membrane protease found in the yeast Saccharomyces cerevisiae.
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Registered trials
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