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cPLA2α and EHD1 interact and regulate the vesiculation of cholesterol-rich, GPI-anchored, protein-containing endosomes

Cai, Bishuang, Caplan, Steve, Naslavsky, Naava·2012·Molecular Biology of the Cell
DOI 10.1091/mbc.e11-10-0881PMC PMC3350552
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Abstract

The lipid modifier phospholipase A2 catalyzes the hydrolysis of phospholipids to inverted-cone–shaped lysophospholipids that contribute to membrane curvature and/or tubulation. Conflicting findings exist regarding the function of cytosolic phospholipase A2 (cPLA2) and its role in membrane regulation at the Golgi and early endosomes. However, no studies addressed the role of cPLA2 in the regulation of cholesterol-rich membranes that contain glycosylphosphatidylinositol-anchored proteins (GPI-APs). Our studies support a role for cPLA2α in the vesiculation of GPI-AP–containing membranes, using endogenous CD59 as a model for GPI-APs. On cPLA2α depletion, CD59-containing endosomes became hypertubular. Moreover, accumulation of lysophospholipids induced by a lysophospholipid acyltransferase inhibitor extensively vesiculated CD59-containing endosomes. However, overexpression of cPLA2α did not increase the endosomal vesiculation, implying a requirement for additional factors. Indeed, depletion of the “pinchase” EHD1, a C-terminal Eps15 homology domain (EHD) ATPase, also induced hypertubulation of CD59-containing endosomes. Furthermore, EHD1 and cPLA2α demonstrated in situ proximity (<40 nm) and interacted in vivo. The results presented here provide evidence that the lipid modifier cPLA2α and EHD1 are involved in the vesiculation of CD59-containing endosomes. We speculate that cPLA2α induces membrane curvature and allows EHD1, possibly in the context of a complex, to sever the curved membranes into vesicles.

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Metadata

Authors
Cai, B., Caplan, S., & Naslavsky, N.
Affiliations
Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, NE 68198
Venue
Molecular Biology of the Cell
Publisher
American Society for Cell Biology (ASCB)
Published
2012-05-15
Volume
23
Issue
10
Pages
1874-1888
ISSN
  • 1059-1524
  • 1939-4586
DOI
10.1091/mbc.e11-10-0881
PMC
PMC3350552
Cited by
51
References
1
Language
en

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