Leukemia-Related Protein 16 (LRP16), a member of the macro domain family, plays a crucial role in orchestrating genotoxicity-initiated NF-κB signaling in the colon and the pathophysiological relevance of NF-κB activation induced by LRP16 in colonic cell survival/recovery from extrinsic DNA damage.
Tyrosine phosphorylation of the intracellular domain of LRP1 serves as a molecular switch to regulate cellular cholesterol homeostasis through nuclear hormone receptor-mediated regulation of the cellular cholesterol exporter ABCA1.
Phosphorylation of the Wnt receptor LRP6 directly inhibits glycogen synthase kinase-3 by acting as a pseudosubstrate that stabilizes an active conformation of the enzyme, identical to autoinhibition by phosphorylation of its N terminus.
In oligodendrocyte progenitor cells, lipid metabolism and peroxisome biogenesis are regulated by the low-density lipoprotein related-receptor-1, and if disrupted, impair proper white matter development and adult repair.
Cryo-EM structure of monomeric human Frizzled5 was determined with a universal fiducial antibody at 3.7 Å overall resolution, which supports a simple Fzd/LRP6 heterodimerization mechanism of canonical Wnt/β-catenin signaling.
The secreted sugar-binding protein galectin-8 causes osteoblasts to secrete factors that promote the differentiation of bone marrow cells into osteoclasts; targeting this protein could therefore potentially help treat diseases associated with excessive bone loss.