IndraLab

Statements

LDLR binds LRP6. 9 / 9
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"LRP6 forms a complex with LDLR, clathrin, and autosomal recessive hypercholesterolemia protein, and is required for clathrin mediated vesicular LDL uptake."
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"Here, we further show that Wnt ligand stimulation induces conformational change of the Frz-LRP6 complex and leads to hexamer formation containing the core LDLR domain-mediated LRP6 homodimer that is stabilized by two pairs of Wnt3a and Frz8, that is, Wnt3a-Frz8-LRP6-LRP6-Frz8-Wnt3a."
24412751
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"It was shown that LRP6 (WT) forms a complex with LDLR and autosomal recessive hyperlipidaemia protein (ARH), which upon stimulation with LDL undergoes a clathrin-mediated internalization process ( xref )."
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"Further analysis revealed that LRP6 forms a complex with LDLR, clathrin, and ARH and undergoes a clathrin-mediated internalization after stimulation with LDL [52]."
33969358
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"Once LDL-C binds to LDLR, LRP6 forms a complex with LDLR, LDLRAP1, and clathrin to initiate a clathrin dependent endocytosis."
26318398
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"LRP6 can form a complex with LDLR, facilitating receptor-mediated endocytosis of LDL particles [ xref , xref ], and also directly bind apolipoprotein E-containing lipoproteins."
28723729
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"In vitro evidence showed that LRP6 knockdown in LDLR-deficient CHO cells caused a modest reduction of LDL binding and uptake, while its knockdown in regular CHO cells resulted in a much greater decline in LDL levels, suggesting an interaction between LRP6 and LDLR."
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"Furthermore, co-localization and complex formation between LRP6 and LDLR in LRP6 mutant fibroblast showed impaired internalization of LDL particles."
26046396
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"In vitro evidence showed that LRP6 knockdown in LDLR-deficient CHO cells caused a modest reduction of LDL binding and uptake, while its knockdown in regular CHO cells resulted in a much greater decline in LDL levels, suggesting an interaction between LRP6 and LDLR."
33081636