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. 2021 Sep 8;297(4):101177. doi: 10.1016/j.jbc.2021.101177

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© 2021 The Authors

This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

LDLR and ASGR1 form a complex that is not limited to lectin binding.A, coimmunoprecipitation of endogenous LDLR and ASGR1 in HepG2-PCSK9-KO cells. Pull-downs with ASGR1 antibody were analyzed by TrueBlot for ASGR1 and LDLR and for CD36 and IR (shown as IR-β) as negative controls for membrane-bound receptors. To “Beads only” negative control addition of ASGR1 antibody was omitted. “Input” represents 10% of the original material subjected to coimmunoprecipitation. B, coimmunoprecipitation from liver extracts of WT and PCSK9-KO mice. Pull-downs with ASGR1 antibody were analyzed by Western blot for LDLR and ASGR1. To “Beads only” negative control addition of ASGR1 antibody was omitted. “Control” (IgG migration control) consists of WT mouse liver lysate (30 μg) plus ASGR1 antibody. C, coimmunoprecipitation from HEK293 cells transfected with vector (V), V5-tagged LDLR or Flag-tagged ASGR1, WT or mutant Q240A/W244A/E253A (QA/WA/EA), or a combination of ASGR1 and LDLR. Pull-downs with Flag M2 antibody (left panel) or V5 antibody (right panel) were analyzed by Western blot for LDLR and ASGR1. “Input” represents 10% of the original material subjected to coimmunoprecipitation. Data are representative of two independent experiments.