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The closed conformation of the LDL receptor is destabilized by the low Ca++ concentration but favored by the high Mg++ concentration in the endosome

AuthorsMartínez-Oliván, J.; Arias-Moreno, X.; Hurtado-Guerrero, R.; Carrodeguas, José A.; Miguel-Romero, Laura ; Marina, Alberto ; Bruscolini, P.; Sancho, Javier
Issue Date2015
CitationFEBS Letters 589: 3534- 3540 (2015)
AbstractThe LDL receptor (LDLR) internalizes LDL and VLDL particles. In the endosomes, it adopts a closed conformation important for recycling, by interaction of two modules of the ligand binding domain (LR4-5) and a β-propeller motif. Here, we investigate by SPR the interactions between those two modules and the β-propeller. Our results indicate that the two modules cooperate to bind the β-propeller. The binding is favored by low pH and by high [Ca]. Our data show that Mg, at high concentration in the endosome, favors the formation of the closed conformation by replacing the structuring effect of Ca in LR5. We propose a sequential model of LDL release where formation of the close conformation follows LDL release.
Identifiersdoi: 10.1016/j.febslet.2015.10.014
issn: 1873-3468
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