IndraLab

Statements

LRP6 binds LDLR. 15 / 15
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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."
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"Furthermore, co-localization and complex formation between LRP6 and LDLR in LRP6 mutant fibroblast showed impaired internalization of LDL particles."
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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."
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"We recently found that Frz prevents LRP6-induced canonical pathway activation by direct binding to LRP6–LDLR domain (manuscript in submission)."
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"We previously identified a canonical pathway inhibitor IGFBP-4, which strongly bound to LRP6–LDLR domain [12] ."
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"Here, we demonstrate that contrary to current view, Wnt3a induces hexamer formation containing the core LDLR domain-mediated LRP6 homodimer that is stabilized by two pairs of Wnt3a and Frz8, that is, [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Our findings provide new insight into the regulation of canonical pathway by LRP6–LDLR domain."
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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]."
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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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"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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"LRP6 forms a complex with LDLR, clathrin, and autosomal recessive hypercholesterolemia (ARH) protein, and this complex is required for clathrin-mediated vesicular LDL uptake [ 78 ]."
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"Finally, LRP6 can bind and regulate the function of the LDL-R [50] ."
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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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"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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"These results indicated that Wnt3a-induced LRP6 dimerization is mediated by LRP6–LDLR domain."
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