The wheat ABC transporter Lr34 modifies the lipid environment at the plasma membrane
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The wheat ABC transporter Lr34 modifies the lipid environment at the plasma membrane. / Deppe, Johannes P.; Rabbat, Ritta; Hörtensteiner, Stefan; Keller, Beat; Martinoia, Enrico; Lopéz-Marqués, Rosa L.
In: Journal of Biological Chemistry, Vol. 293, No. 48, 30.11.2018, p. 18667-18679.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - The wheat ABC transporter Lr34 modifies the lipid environment at the plasma membrane
AU - Deppe, Johannes P.
AU - Rabbat, Ritta
AU - Hörtensteiner, Stefan
AU - Keller, Beat
AU - Martinoia, Enrico
AU - Lopéz-Marqués, Rosa L.
PY - 2018/11/30
Y1 - 2018/11/30
N2 - Phospholipids (PLs) are emerging as important factors that initiate signal transduction cascades at the plasma membrane. Their distribution within biological membranes is tightly regulated, e.g. by ATP-binding cassette (ABC) transporters, which preferably translocate PLs from the cytoplasmic to the exoplasmic membrane leaflet and are therefore called PL-floppases. Here, we demonstrate that a plant ABC transporter, Lr34 from wheat (Triticum aestivum), is involved in plasma membrane remodeling characterized by an intracellular accumulation of phosphatidic acid and enhanced outward translocation of phosphatidylserine. In addition, the content of phosphatidylinositol 4,5-bisphosphate in the cytoplasmic leaflet of the plasma membrane was reduced in the presence of the ABC transporter. When heterologously expressed in Saccharomyces cerevisiae, Lr34 promoted oil body formation in a mutant defective in PL-transfer in the secretory pathway. Our results suggest that PL redistribution by Lr34 potentially affects the membrane-bound proteome and contributes to the previously reported stimuli-independent activation of biotic and abiotic stress responses and neutral lipid accumulation in transgenic Lr34-expressing barley plants.
AB - Phospholipids (PLs) are emerging as important factors that initiate signal transduction cascades at the plasma membrane. Their distribution within biological membranes is tightly regulated, e.g. by ATP-binding cassette (ABC) transporters, which preferably translocate PLs from the cytoplasmic to the exoplasmic membrane leaflet and are therefore called PL-floppases. Here, we demonstrate that a plant ABC transporter, Lr34 from wheat (Triticum aestivum), is involved in plasma membrane remodeling characterized by an intracellular accumulation of phosphatidic acid and enhanced outward translocation of phosphatidylserine. In addition, the content of phosphatidylinositol 4,5-bisphosphate in the cytoplasmic leaflet of the plasma membrane was reduced in the presence of the ABC transporter. When heterologously expressed in Saccharomyces cerevisiae, Lr34 promoted oil body formation in a mutant defective in PL-transfer in the secretory pathway. Our results suggest that PL redistribution by Lr34 potentially affects the membrane-bound proteome and contributes to the previously reported stimuli-independent activation of biotic and abiotic stress responses and neutral lipid accumulation in transgenic Lr34-expressing barley plants.
UR - http://www.scopus.com/inward/record.url?scp=85057551335&partnerID=8YFLogxK
U2 - 10.1074/jbc.RA118.002532
DO - 10.1074/jbc.RA118.002532
M3 - Journal article
C2 - 30327425
AN - SCOPUS:85057551335
VL - 293
SP - 18667
EP - 18679
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 48
ER -
ID: 213856148