Journal
SCIENCE
Volume 329, Issue 5995, Pages 1085-1088Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1191026
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Funding
- National Sciences and Engineering Council of Canada (NSERC)
- Canadian Institute of Health Research (CIHR)
- Michael Smith Foundation for Health Research (MSFHR)
- Canada Foundation for Innovation
- British Columbia Knowledge Development Fund
- National Institute of Diabetes and Digestive and Kidney Diseases
- Singapore National Research Foundation [2007-04]
- Biomedical Research Council of Singapore [R-183-000-211-305]
- National Medical Research Council [R-183-000-224-213]
- SystemsX.ch RTD project LipidX
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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.
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