ArticleEukaryotic cell2011
The putative Saccharomyces cerevisiae hydrolase Ldh1p is localized to lipid droplets.
Article in Eukaryotic cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- The Lack of a COPII Cargo Receptor Erv14 Impacts Physiological Functions of the Vacuole in Saccharomyces cerevisiae.Traffic (Copenhagen, Denmark) · 2026Article
- Pex3 promotes formation of peroxisome-peroxisome and peroxisome-lipid droplet contact sites.Scientific reports · 2025Article
- Analysis of the response mechanism in lipid degradation of key gene LDH1 knockout strains of Saccharomyces cerevisiae under levulinic acid stress.Archives of microbiology · 2025Article
- Article
- Lipid droplet-mediated lipid and protein homeostasis in budding yeast.FEBS letters · 2018Review
- Pex35 is a regulator of peroxisome abundance.Journal of cell science · 2017Article
- Lipid droplet dynamics in budding yeast.Cellular and molecular life sciences : CMLS · 2015Review
- The important ergot alkaloid intermediate chanoclavine-I produced in the yeast Saccharomyces cerevisiae by the combined action of EasC and EasE from Aspergillus japonicus.Microbial cell factories · 2014Article
- High confidence proteomic analysis of yeast LDs identifies additional droplet proteins and reveals connections to dolichol synthesis and sterol acetylation.Journal of lipid research · 2014Article
- Screening for hydrolytic enzymes reveals Ayr1p as a novel triacylglycerol lipase in Saccharomyces cerevisiae.The Journal of biological chemistry · 2013Article
- Involvement of the Saccharomyces cerevisiae hydrolase Ldh1p in lipid homeostasis.Eukaryotic cell · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Here, we report the identification of a novel hydrolase in Saccharomyces cerevisiae. Ldh1p (systematic name, Ybr204cp) comprises the typical GXSXG-type lipase motif of members of the α/β-hydrolase family and shares some features with the peroxisomal lipase Lpx1p. Both proteins carry a putative peroxisomal targeting signal type1 (PTS1) and can be aligned with two regions of homology. While Lpx1p is known as a peroxisomal enzyme, subcellular localization studies revealed that Ldh1p is predominantly localized to lipid droplets, the storage compartment of nonpolar lipids. Ldh1p is not required for the function and biogenesis of peroxisomes, and targeting of Ldh1p to lipid droplets occurs independently of the PTS1 receptor Pex5p.
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Registered trials
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