The phospholipase D1 pathway modulates macroautophagy

Claudia Dall'Armi, Andrés Hurtado-Lorenzo, Huasong Tian, Etienne Morel, Akiko Nezu, Robin B. Chan, W. Haung Yu, Kimberly S. Robinson, Oladapo Yeku, Scott A. Small, Karen Duff, Michael A. Frohman, Markus R. Wenk, Akitsugu Yamamoto and Gilbert Di Paolo ()
Additional contact information
Claudia Dall'Armi: Columbia University Medical Center
Andrés Hurtado-Lorenzo: Columbia University Medical Center
Huasong Tian: Columbia University Medical Center
Etienne Morel: Columbia University Medical Center
Akiko Nezu: Faculty of Bio-Science, Nagahama Institute of Bio-Science and Technology, 1266 Tamura-cho, Nagahama, Shiga 526-0829, Japan.
Robin B. Chan: Columbia University Medical Center
W. Haung Yu: Columbia University Medical Center
Kimberly S. Robinson: Columbia University Medical Center
Oladapo Yeku: Stony Brook University
Scott A. Small: Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University Medical Center
Karen Duff: Columbia University Medical Center
Michael A. Frohman: Stony Brook University
Markus R. Wenk: The Yong Loo Lin School of Medicine, National University of Singapore
Akitsugu Yamamoto: Faculty of Bio-Science, Nagahama Institute of Bio-Science and Technology, 1266 Tamura-cho, Nagahama, Shiga 526-0829, Japan.
Gilbert Di Paolo: Columbia University Medical Center

Nature Communications, 2010, vol. 1, issue 1, 1-11

Abstract: Abstract Although macroautophagy is known to be an essential degradative process whereby autophagosomes mediate the engulfment and delivery of cytoplasmic components into lysosomes, the lipid changes underlying autophagosomal membrane dynamics are undetermined. Here, we show that phospholipase D1 (PLD1), which is primarily associated with the endosomal system, partially relocalizes to the outer membrane of autophagosome-like structures upon nutrient starvation. The localization of PLD1, as well as the starvation-induced increase in PLD activity, are altered by wortmannin, a phosphatidylinositol 3-kinase inhibitor, suggesting PLD1 may act downstream of Vps34. Pharmacological inhibition of PLD and genetic ablation of PLD1 in mouse cells decreased the starvation-induced expansion of LC3-positive compartments, consistent with a role of PLD1 in the regulation of autophagy. Furthermore, inhibition of PLD results in higher levels of Tau and p62 aggregates in organotypic brain slices. Our in vitro and in vivo findings establish a role for PLD1 in autophagy.

Date: 2010
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DOI: 10.1038/ncomms1144

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