Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae are localized to lipid particles.

The Journal of biological chemistry - 11 Nov 2005

Athenstaedt Karin, Daum Günther

Abstract excerpt

Triacylglycerol (TAG) lipases are required for mobilization of TAG stored in lipid particles. Recently, Tgl3p was identified as a major TAG lipase of the yeast Saccharomyces cerevisiae (Athenstaedt, K., and Daum, G. (2003) J. Biol. Chem. 278, 23317-23323). Here, we report the identification of Tgl4p and Tgl5p as additional TAG lipases of the yeast. Both polypeptides, encoded by open reading frames YKR089c/TGL4...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Gene Deletion
Share to Gene Expression Regulation, Fungal

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Lipase

Share to Lipids

Share to Protein Transport

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 16135509
DOI: 10.1074/jbc.M507261200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae are localized to lipid particles.PMID 16135509Read ↗

Biosynthesis of phosphatidic acid in lipid particles and endoplasmic reticulum of Saccharomyces cerevisiae.Semantic proximity Read ↗

An Energy-Independent Pro-longevity Function of Triacylglycerol in Yeast.Semantic proximity Read ↗

A defect of the vacuolar putative lipase Atg15 accelerates degradation of lipid droplets through lipolysis.Semantic proximity Read ↗

The Saccharomyces cerevisiae YLL012/YEH1, YLR020/YEH2, and TGL1 genes encode a novel family of membrane-anchored lipases that are required for steryl ester hydrolysis.Semantic proximity Read ↗

The TGL2 gene of Saccharomyces cerevisiae encodes an active acylglycerol lipase located in the mitochondria.Semantic proximity Read ↗

Storage lipid synthesis is non-essential in yeast.Semantic proximity Read ↗

Identification of a triacylglycerol lipase in the diatom Phaeodactylum tricornutum.Semantic proximity Read ↗

Structural and biochemical properties of lipid particles from the yeast Saccharomyces cerevisiae.Semantic proximity Read ↗

Characterization of a lipid droplet protein from Yarrowia lipolytica that is required for its oleaginous phenotype.Semantic proximity Read ↗

Engineering of Saccharomyces cerevisiae for the accumulation of high amounts of triacylglycerol.Semantic proximity Read ↗

Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast.Semantic proximity Read ↗

Identification and characterization of a triacylglycerol lipase in Arabidopsis homologous to mammalian acid lipases.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.