TY - JOUR
T1 - Endoplasmic reticulum stress affects the transport of phosphatidylethanolamine from mitochondria to the endoplasmic reticulum in S. cerevisiae
AU - Kannan, Muthukumar
AU - Sivaprakasam, Chinnarasu
AU - Prinz, William A.
AU - Nachiappan, Vasanthi
N1 - Funding Information:
The financial support from Bharathidasan University, Tiruchirappalli , Council of Scientific & Industrial Research-CSIR, India , and the instrumentation facility provided by the Department of Science & Technology (DST) under the DST-PURSE and DST-FIST programsare gratefully acknowledged. The authors sincerely thank Prof. Ram Rajasekharan, Dept of Biochemistry, Indian Institute of Science (Bangalore - India), for his critical comments about this manuscript and also for generously providing the reagents used in this study. We thank Prof. Ewald H. Hettema, (University of Sheffield, Sheffield, UK) for providing the OM45-GFP yeast strains, as well as Prof. Yoshinori Ohsumi, Prof. Kuninori Suzuki (University of Tokyo, Japan), Prof. Jeffrey Brodsky (University of Pittsburgh, PA, USA), and Prof. Marco Foiani, (University of Milan, Italy) for providing Ape1, Atg8, Kar2 and Pgk1 antiserum, respectively.
Publisher Copyright:
© 2016
PY - 2016/12/1
Y1 - 2016/12/1
N2 - Phosphatidylcholine (PC) and phosphatidylethanolamine (PE) are two of the most abundant phospholipids in cells. Although both lipids can be synthesized in the endoplasmic reticulum (ER), in S. cerevisiae PE can also be produced in mitochondria and endosomes; this PE can be transported back to the ER where it is converted to PC. In this study we found that dithiothreitol (DTT), which induces ER stress, decreases PE export from mitochondria to the ER. This results in decreased levels of total cellular PC and mitochondrial PC. These decreases were not caused by changes in levels of PC synthesizing or degrading enzymes. PE export from mitochondria to the ER during ER stress was further reduced in cells lacking Mdm10p, a component of an ER-mitochondrial tethering complex that may facilitated lipid exchange between these compartments. We also found that reducing mitochondrial PC levels induces mitophagy. In conclusion, we show that ER stress affected PE export from mitochondria to ER and the Mdm10p is important for this process.
AB - Phosphatidylcholine (PC) and phosphatidylethanolamine (PE) are two of the most abundant phospholipids in cells. Although both lipids can be synthesized in the endoplasmic reticulum (ER), in S. cerevisiae PE can also be produced in mitochondria and endosomes; this PE can be transported back to the ER where it is converted to PC. In this study we found that dithiothreitol (DTT), which induces ER stress, decreases PE export from mitochondria to the ER. This results in decreased levels of total cellular PC and mitochondrial PC. These decreases were not caused by changes in levels of PC synthesizing or degrading enzymes. PE export from mitochondria to the ER during ER stress was further reduced in cells lacking Mdm10p, a component of an ER-mitochondrial tethering complex that may facilitated lipid exchange between these compartments. We also found that reducing mitochondrial PC levels induces mitophagy. In conclusion, we show that ER stress affected PE export from mitochondria to ER and the Mdm10p is important for this process.
KW - ER stress
KW - ERMES
KW - Lipid transport
KW - Mitochondria
KW - Phosphatidylcholine
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U2 - 10.1016/j.bbalip.2016.09.015
DO - 10.1016/j.bbalip.2016.09.015
M3 - Article
C2 - 27678054
AN - SCOPUS:84992195137
SN - 1388-1981
VL - 1861
SP - 1959
EP - 1967
JO - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
JF - Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
IS - 12
ER -