Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5995
pubmed:dateCreated
2010-8-27
pubmed:abstractText
Recognition of lipids by proteins is important for their targeting and activation in many signaling pathways, but the mechanisms that regulate such interactions are largely unknown. Here, we found that binding of proteins to the ubiquitous signaling lipid phosphatidic acid (PA) depended on intracellular pH and the protonation state of its phosphate headgroup. In yeast, a rapid decrease in intracellular pH in response to glucose starvation regulated binding of PA to a transcription factor, Opi1, that coordinately repressed phospholipid metabolic genes. This enabled coupling of membrane biogenesis to nutrient availability.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glucose, http://linkedlifedata.com/resource/pubmed/chemical/Inositol, http://linkedlifedata.com/resource/pubmed/chemical/Liposomes, http://linkedlifedata.com/resource/pubmed/chemical/OPI1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/PMA1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidic Acids, http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1, http://linkedlifedata.com/resource/pubmed/chemical/Proton-Translocating ATPases, http://linkedlifedata.com/resource/pubmed/chemical/REG1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/TRK1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Vacuolar Proton-Translocating...
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1095-9203
pubmed:author
pubmed:issnType
Electronic
pubmed:day
27
pubmed:volume
329
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1085-8
pubmed:meshHeading
pubmed-meshheading:20798321-Active Transport, Cell Nucleus, pubmed-meshheading:20798321-Cation Transport Proteins, pubmed-meshheading:20798321-Cell Membrane, pubmed-meshheading:20798321-Cell Nucleus, pubmed-meshheading:20798321-Endoplasmic Reticulum, pubmed-meshheading:20798321-Gene Expression Regulation, Fungal, pubmed-meshheading:20798321-Genes, Fungal, pubmed-meshheading:20798321-Glucose, pubmed-meshheading:20798321-Hydrogen-Ion Concentration, pubmed-meshheading:20798321-Inositol, pubmed-meshheading:20798321-Liposomes, pubmed-meshheading:20798321-Mutation, pubmed-meshheading:20798321-Phosphatidic Acids, pubmed-meshheading:20798321-Protein Binding, pubmed-meshheading:20798321-Protein Phosphatase 1, pubmed-meshheading:20798321-Proton-Translocating ATPases, pubmed-meshheading:20798321-Recombinant Fusion Proteins, pubmed-meshheading:20798321-Repressor Proteins, pubmed-meshheading:20798321-Saccharomyces cerevisiae, pubmed-meshheading:20798321-Saccharomyces cerevisiae Proteins, pubmed-meshheading:20798321-Signal Transduction, pubmed-meshheading:20798321-Transcription, Genetic, pubmed-meshheading:20798321-Vacuolar Proton-Translocating ATPases
pubmed:year
2010
pubmed:articleTitle
Phosphatidic acid is a pH biosensor that links membrane biogenesis to metabolism.
pubmed:affiliation
Department of Cellular and Physiological Sciences, University of British Columbia, Vancouver, British Columbia, V6T 1Z3, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Intramural