Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10903748 | Experimental Cell Research | 2016 | 10 Pages |
Abstract
EHD3 is localized on the tubular structures of early endosomes, and it regulates their trafficking pathway. However, the regulatory mechanism of EHD3-containing tubular structures remains poorly understood. An in vitro liposome co-sedimentation assay revealed that EHD3 interacted with phosphatidic acid through its helical domain and this interaction induced liposomal tubulations. Additionally, inhibiting phosphatidic acid synthesis with diacylglycerol kinase inhibitor or lysophosphatidic acid acyltransferase inhibitor significantly reduced the number of EHD3-containing tubules and impaired their trafficking from early endosomes. These results suggest that EHD3 and phosphatidic acid cooperatively regulate membrane deformation and trafficking from early endosomes.
Keywords
PLDPhosphatidylinositol-4-phosphateFIPILPAATERC5-fluoro-2-indolyl des-chlorohalopemidePtdIns(3)PPLA2DGKLPAEHDPISPtdIns(4)PPtdIns(4,5)P2phospholipase A2phosphatidic acidlysophosphatidic acidEndosomesearly endosomeReceptor recyclingdiacylglycerol kinasediacylglycerolDAGPlasma membranephosphatidylethanolaminePhosphatidylserinephosphatidylinositol-3-phosphatephosphatidylinositol-4,5-bisphosphatePhosphoinositidesPhospholipase Dlysophosphatidic acid acyltransferaseEndocytic Recycling Compartment
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Authors
Yuji Henmi, Natsuko Oe, Nozomu Kono, Tomohiko Taguchi, Kohji Takei, Kenji Tanabe,