Intracellular fate of LDL receptor family members depends on the cooperation between their ligand-binding and EGF domains.

@article{Hoof2005IntracellularFO,
  title={Intracellular fate of LDL receptor family members depends on the cooperation between their ligand-binding and EGF domains.},
  author={Dennis van Hoof and Kees C W Rodenburg and Dick J van der Horst},
  journal={Journal of cell science},
  year={2005},
  volume={118 Pt 6},
  pages={1309-20}
}
The insect low-density lipoprotein (LDL) receptor (LDLR) homologue LpR mediates endocytosis of an insect lipoprotein (lipophorin) that is structurally related to LDL. Despite these similarities, lipophorin and LDL follow distinct intracellular routes upon endocytosis by their receptors. Whereas LDL is degraded in lysosomes, lipophorin is recycled in a transferrin-like manner. We constructed several hybrid receptors composed of Locusta migratoria LpR and human LDLR regions to identify the… CONTINUE READING
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