A lipid associated with the antiphospholipid syndrome regulates endosome structure and function

Toshihide Kobayashi, Espen Stang, Karen S. Fang, Philippe de Moerloose, Robert G. Parton and Jean Gruenberg ()
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Toshihide Kobayashi: Sciences II
Espen Stang: Centre for Microscopy and Microanalysis, University of Queensland
Karen S. Fang: Sciences II
Philippe de Moerloose: University Hospital of Geneva
Robert G. Parton: Centre for Microscopy and Microanalysis, University of Queensland
Jean Gruenberg: Sciences II

Nature, 1998, vol. 392, issue 6672, 193-197

Abstract: Abstract Little is known about the structure and function of membrane domains in the vacuolar apparatus of animal cells. A unique feature of late endosomes, which are part of the pathway that leads to lysosomes, is that they contain a complex system of poorly characterized internal membranes in their lumen. These endosomes are therefore known as multivesicular or multilamellar organelles1,2. Some proteins distribute preferentially within these internal membranes, whereas others are exclusively localized to the organelle's limiting membrane3. The composition and function of this membrane system are poorly understood. Here we show that these internal membranes contain large amounts of a unique lipid, and thus form specialized domains within endosomes. These specialized domains are involved in sorting the multifunctional receptor4 for insulin-like growth factor 2 and ligands bearing mannose-6-phosphate, in particular lysosomal enzymes. We also show that this unique lipid is a specific antigen for human antibodies associated with the antiphospholipid syndrome5,6. These antibodies may act intracellularly by altering the protein-sorting functions of endosomes.

Date: 1998
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DOI: 10.1038/32440

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