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.

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.

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.

A novel folding machinery assists transmembrane proteins from the cytosolic side of the endoplasmic reticulum.

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.

Two cancer related proteins, tyrosine phosphatase PTPRK and ubiquitin ligase ZNRF3, interact to downregulate Wnt receptors, thereby regulating Spemann organizer function during Xenopus development.

Receptors for two distinct pathways are linked to choreograph the dynamic interaction of Wnt on the stem cell membrane, which leads to the control of asymmetric cell division.