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J. Biol. Chem., Vol. 276, Issue 13, 9861-9867, March 30, 2001
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From the Department of Physiology, Emory University School of
Medicine, Atlanta, Georgia 30322
The yeast Saccharomyces
cerevisiae readily accumulates short-chain, fluorescent
7-nitrobenz-2-oxa-1,3-diazol-4-yl (NBD)-labeled phosphatidylcholine and phosphatidylethanolamine at the nuclear envelope/endoplasmic reticulum and mitochondria. The net intracellular accumulation reflects the sum of their inwardly and outwardly directed
transbilayer translocation across the plasma membrane (flip and flop,
respectively). The rate of flop is negligible in energy-depleted cells
as well as at low temperature (2 °C). Although flip is reduced at
2 °C, it can still be measured by flow cytometry, allowing the rate
of flip, independent of flop, to be characterized at this temperature.
Flip requires the energy of the plasma membrane proton electrochemical
gradient and is down-regulated as cells pass through the diauxic shift
and enter stationary phase. Furthermore, drug-resistant,
gain-of-function mutations in the transcription factors,
PDR1 and PDR3, result in a dramatic
down-regulation of flip in addition to their already established
up-regulation of flop. These results imply that down-regulation of the
NBD-phospholipid flip pathway is a physiological response to
environmental stress.
Energy-dependent Flip of Fluorescence-labeled
Phospholipids Is Regulated by Nutrient Starvation and Transcription
Factors, PDR1 and PDR3*
and
*
This work was supported in part by National Institutes of
Health Grant GM52410 and a grant from the University Research Committee of Emory University (to J. W. N.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by a National Institutes of Health training grant GM08367.
§
To whom correspondence should be addressed: 1648 Pierce Dr., Dept.
of Physiology, Emory University School of Medicine, Atlanta, GA 30322. Tel.: 404-727-7422; Fax: 404-727-2648; E-mail: wnichols@ physio.emory.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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