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Lysosomal integral membrane protein-2 as a phospholipid receptor revealed by biophysical and cellular studies.

著者 Conrad KS , Cheng TW , Ysselstein D , Heybrock S , Hoth LR , Chrunyk BA , Am Ende CW , Krainc D , Schwake M , Saftig P , Liu S , Qiu X , Ehlers MD
Nat Commun.2017 Dec 04 ; 8(1):1908.
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Lysosomal integral membrane protein-2 (LIMP-2/SCARB2) contributes to endosomal and lysosomal function. LIMP-2 deficiency is associated with neurological abnormalities and kidney failure and, as an acid glucocerebrosidase receptor, impacts Gaucher and Parkinson's diseases. Here we report a crystal structure of a LIMP-2 luminal domain dimer with bound cholesterol and phosphatidylcholine. Binding of these lipids alters LIMP-2 from functioning as a glucocerebrosidase-binding monomer toward a dimeric state that preferentially binds anionic phosphatidylserine over neutral phosphatidylcholine. In cellular uptake experiments, LIMP-2 facilitates transport of phospholipids into murine fibroblasts, with a strong substrate preference for phosphatidylserine. Taken together, these biophysical and cellular studies define the structural basis and functional importance of a form of LIMP-2 for lipid trafficking. We propose a model whereby switching between monomeric and dimeric forms allows LIMP-2 to engage distinct binding partners, a mechanism that may be shared by SR-BI and CD36, scavenger receptor proteins highly homologous to LIMP-2.
PMID: 29199275 [PubMed - in process]
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