VLDLR Protein, Mouse (HEK293, His)

The VLDLR protein operates as a multifunctional cell surface receptor pivotal in energy metabolism, particularly by binding VLDL and facilitating its cellular uptake through endocytosis. Beyond its role in lipid transport, VLDLR exhibits a broad binding affinity for various molecules, including Reelin/RELN, apolipoprotein E/APOE-containing ligands, and clusterin/CLU. In the inactive state of the pathway, VLDLR forms homo or heterooligomers with LRP8. Upon ligand binding, these homooligomers rearrange into higher-order receptor clusters, transducing the extracellular RELN signal to intracellular signaling processes through DAB1 binding on its cytoplasmic tail. This interaction triggers DAB1 phosphorylation, orchestrating the cell responses crucial for the correct positioning of newly generated neurons. Additionally, VLDLR serves as a stop signal for migrating neurons, preventing entry into the marginal zone. Interactions with various proteins, including LDLRAP1, SNX17, PCSK9, PAFAH1B3, PAFAH1B2, STX5, and CLU, further highlight the intricate regulatory network of VLDLR in cellular processes.