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

Protein Phosphatase Sit4 Affects Lipid Droplet Synthesis and Soraphen A Resistance Independent of Its Role in Regulating Elongator Dependent tRNA Modification.

Biomolecules - 11 Jul 2018

Bozaquel-Morais Bruno Leonardo, Vogt Leonie, D'Angelo Valentina, Schaffrath Raffael, Klassen Roland, Montero-Lomelí Mónica

Abstract excerpt

The protein phosphatase Sit4 has been shown to be required for lipogenesis and resistance against the acetyl-CoA carboxylase inhibitor soraphen A. Since Sit4 is also required for biosynthesis of Elongator dependent tRNA modifications such as 5-methoxycarbonylmethyluridine (mcm⁵U), we investigated the relevance of tRNA modifications in lipogenesis and soraphen A response. While sit4 and Elongator (elp3) mutants...

Read the complete abstract on PubMed

Topics

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

Share to Drug Resistance, Fungal
Share to Histone Acetyltransferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Lipid Droplets

Share to Lipogenesis

Share to Lipolysis

Share to Macrolides

Share to Protein Phosphatase 2

Share to Uridine

Source

Open in PubMed Open full text

Identifiers

PMID: 29997346
DOI: 10.3390/biom8030049
PMCID: PMC6165401

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Protein Phosphatase Sit4 Affects Lipid Droplet Synthesis and Soraphen A Resistance Independent of Its Role in Regulating Elongator Dependent tRNA Modification.PMID 29997346Read ↗

Elongator function depends on antagonistic regulation by casein kinase Hrr25 and protein phosphatase Sit4.Semantic proximity Read ↗

Loss of Elongator- and KEOPS-Dependent tRNA Modifications Leads to Severe Growth Phenotypes and Protein Aggregation in YeastSemantic proximity Read ↗

The m6A methyltransferase Ime4 epitranscriptionally regulates triacylglycerol metabolism and vacuolar morphology in haploid yeast cells.Semantic proximity Read ↗

Loss of Elongator- and KEOPS-Dependent tRNA Modifications Leads to Severe Growth Phenotypes and Protein Aggregation in Yeast.Semantic proximity Read ↗

A novel Sit4 phosphatase complex is involved in the response to ceramide stress in yeast.Semantic proximity Read ↗

Fission yeast poly(A) polymerase active site mutation Y86D alleviates the rad24Δ asp1-H397A synthetic growth defect and up-regulates mRNAs targeted by MTREC and Mmi1.Semantic proximity Read ↗

Lipid Biosynthesis Perturbation Impairs Endoplasmic Reticulum-Associated DegradationSemantic proximity Read ↗

RNA Polymerase III Output Is Functionally Linked to tRNA Dimethyl-G26 Modification.Semantic proximity Read ↗

Lipid biosynthesis perturbation impairs endoplasmic reticulum-associated degradation.Semantic proximity Read ↗

Elongator-dependent modification of cytoplasmic tRNALysUUU is required for mitochondrial function under stress conditions.Semantic proximity Read ↗

Sit4 phosphatase is functionally linked to the ubiquitin-proteasome system.Semantic proximity Read ↗

Connecting mutations of the RNA polymerase II C-terminal domain to complex phenotypic changes using combined gene expression and network analyses.Semantic proximity Read ↗

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