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Lrp6 asymmetry is controlled by Wnt (show WNT2 Proteins)/PCP (show PRCP Proteins) signaling, indicating that this pathway regulates not only planar- but also apicobasal cell polarity.
PTK7 (show PTK7 Proteins) and LRP6 proteins physically interact, suggesting that PTK7 (show PTK7 Proteins) stabilization of LRP6 protein reciprocally regulates both canonical and noncanonical Wnt (show WNT2 Proteins) activities in the embryo.
Results suggest that Rap2 (show RAP2A Proteins) acts via TNIK (show TNIK Proteins) to regulate the stability of LRP6 receptor for Wnt (show WNT2 Proteins) signaling.
The extracellular domains of Lrp5 (show LRP5 Proteins)/6 behave as physiologically relevant inhibitors of noncanonical Wnt (show WNT2 Proteins) signaling during Xenopus and mouse development in vivo.
Lrp6 plays a critical role in the switch from Wnt (show WNT2 Proteins)/PCP (show PRCP Proteins) to Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling.
Kremen2 (show KREMEN2 Proteins) knockdown specifically reduces LRP6 protein levels in neural crest explants.
Waif1a binds to the Wnt (show WNT2 Proteins) coreceptor LRP6 (show LRP5 Proteins) and inhibits Wnt (show WNT2 Proteins)-induced LRP6 (show LRP5 Proteins) internalization into endocytic vesicles, a process that is required for pathway activation.
Results identify GRK5 (show GRK5 Proteins)/6 as novel kinases for the single transmembrane receptor LRP6 (show LRP5 Proteins) during Wnt (show WNT2 Proteins) signaling.
identify ANGPTL4 (show ANGPTL4 Proteins) as a Wnt (show WNT2 Proteins) signaling antagonist that binds to syndecans and forms a ternary complex with the Wnt (show WNT2 Proteins) co-receptor Lipoprotein receptor-related protein 6
The authors show that folding of the Wnt (show WNT2 Proteins) signaling coreceptor LRP6 is promoted by ubiquitination of a specific lysine, retaining it in the ER while avoiding degradation.
Taken together, this study reveals evidence demonstrating a mechanism by which the LPR6/ GSK3beta/E2F1 (show E2F1 Proteins) axis-upregulated LSH (show HELLS Proteins) promoted gliomas.
Structure of the dual-mode Wnt (show WNT2 Proteins) regulator Kremen1 (show KREMEN1 Proteins) and insight into ternary complex formation with LRP6 and DKK1 (show DKK1 Proteins) have been presented.
VAP1 (show AOC3 Proteins) cleaved the extracellular region of LRP6 at Glu1196-Leu1197, the C-terminus of the 4th propeller domain. This cleavage removes four inhibito (show AOC3 Proteins)ry beta-propeller st (show CDH5 Proteins)ructures, resulting in activation of LRP5/6.
We identified a frameshift (c.4594delG, p.Cys1532fs) and a canonical splice-site mutation (c.3398-2A>C, p.?) in LRP6, respectively, in the patient with tooth agenesis (TA) and orofacial clefting (OFC) and in the patient with severe TA only. Mutations in LRP6 cause TA in humans
findings revealed an unrecognized role of Caprin-2 (show CAPRIN2 Proteins) in facilitating LRP5 (show LRP5 Proteins)/6 constitutive phosphorylation at G2/M through forming a quaternary complex with CDK14 (show CDK14 Proteins), Cyclin Y (show CCNY Proteins), and LRP5 (show LRP5 Proteins)/6.
results suggest that miR (show MLXIP Proteins)-29b inhibits expression of LRP6 and HuR (show ELAVL1 Proteins) post-transcriptionally, thus playing a role in the regulation of IEC proliferation and intestinal epithelial homoeostasis.
Mutant LRP6 Impairs Endothelial Cell Functions Associated with Familial Normolipidemic Coronary Artery Disease.
LncRNA PTCSC3 inhibits the proliferation and migration of glioma cells and suppresses Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling pathway by targeting LRP6
VAP1 (show AOC3 Proteins) cleaved recombinant mouse LRP6, producing a 140-kDa fragment. An antibody against a peptide including the LRP6-cleavage site inhibited VAP1 (show AOC3 Proteins)-induced VE-cadherin (show CDH5 Proteins) relocation and disruption of cell-cell adhesions and blocked haemorrhage in mice in vivo.
we identified Lrp6, the gene encoding the coreceptor to Frizzled in the Wnt (show WNT2 Proteins) pathway, as a potential negative regulator of precursor proliferation. Overexpression and siRNA silencing confirmed the regulatory role of Lrp6
These results revealed a new role of the canonical Lrp5 (show LRP5 Proteins)/6-beta-catenin (show CTNNB1 Proteins) pathway in regulating the morphogenesis of the cerebellum during postnatal development.
Data (including data from studies in knockout/transgenic mice) suggest Lrp6 is required for suppression of Sost (sclerostin (show SOST Proteins)) expression by parathyroid hormone (show PTH Proteins) (here, human PTH (show PTH Proteins) peptide 1-34); LRP6 regulates osteocytes expression of histone deacetylases.
Lrp5 (show LRP5 Proteins) binds to Frizzled, preventing Frz-regulated non-canonical Wnt (show WNT2 Proteins) pathway activation and further non-canonical pathway-mediated tumour metastasis.
Wt1 (show WT1 Proteins) expression levels in podocytes regulate Wnt (show WNT2 Proteins)/beta-catenin (show CTNNB1 Proteins) signaling through modulating the endocytic fate of LRP6, and this indicates a potential target for the therapy of CKD.
N-cadherin (show CDH2 Proteins) modulates Lrp6/PTHR1 (show PTH1R Proteins) interaction, restraining the intensity of parathyroid hormone (show PTH Proteins)-induced beta-catenin (show CTNNB1 Proteins) signaling
LRP6 restrains vascular smooth muscle lineage noncanonical signals that promote osteochondrogenic differentiation, mediated in part via USF1 (show USF1 Proteins)- and arginine methylation-dependent relays.
Urotensin II (show UTS2 Proteins) inhibited the proliferation of cardiac side population cells by JNK (show MAPK8 Proteins)/LRP6 signalling during pressure overload.
Hgf (show HGF Proteins) as an important transactivator of canonical Wnt (show WNT2 Proteins) signaling that is mediated by Met-stimulated, Gsk3-dependent Lrp5 (show LRP5 Proteins)/6 phosphorylation
This gene encodes a member of the low density lipoprotein (LDL) receptor gene family. LDL receptors are transmembrane cell surface proteins involved in receptor-mediated endocytosis of lipoprotein and protein ligands. The protein encoded by this gene functions as a receptor or, with Frizzled, a co-receptor for Wnt and thereby transmits the canonical Wnt/beta-catenin signaling cascade. Through its interaction with the Wnt/beta-catenin signaling cascade this gene plays a role in the regulation of cell differentiation, proliferation, and migration and the development of many cancer types. This protein undergoes gamma-secretase dependent RIP- (regulated intramembrane proteolysis) processing but the precise locations of the cleavage sites have not been determined.
low density lipoprotein receptor-related protein 6
, lipoprotein receptor-related protein 6
, low-density lipoprotein receptor-related protein 6
, low-density lipoprotein receptor-related protein 6-like
, low density lipoprotein receptor-related protein 6; low density lipoprotein-related protein 6
, low density lipoprotein-related protein 6