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Maturation of a central brain flight circuit in Drosophila requires Fz2 and Ca2 (show CA2 Proteins)+ signaling.
The heterotrimeric G protein Go functions as a transducer of Wingless-Frizzled 2 signaling in the synapse and Ankyrin 2 as a target of Go signaling required for neuromuscular junction formation
Study finds that C-terminal fragments of the Wg receptor DFz2 accumulate in nuclear foci in association with large RNA granules localizing to the space between the inner & and outer nuclear membranes; granules are found at of inner membrane invaginations, are bounded by LamC, and can be seen leaving the nucleus.
Knockdown of Tc-fz1 (show FZD4 Proteins) alone interfered with the formation of the proximo-distal and the dorso-ventral axes during leg development, whereas no effect was observed with single Tc-fz2 or Tc-fz4 (show FZD4 Proteins) RNAi knockdowns.
Wnt-activated growth of the postsynaptic membrane is mediated by the synapse-to-nucleus translocation and active nuclear import of Fz2-C via a selective Importin-beta11/alpha2 pathway.
subcellular Fz localization, through the association with other membrane proteins, is a critical aspect in regulating the signaling specificity within the Wnt (show WNT4 Proteins)/Fz signaling pathways
Frizzled2 achieves ligand capture and internalization, whereas Arrow, and perhaps downstream signalling, are essential for lysosomal targeting.
concluded that, at synapses, Wingless signal transduction occurs through the nuclear localization of DFrizzled2-C for potential transcriptional regulation of synapse development
DFz2 functions as an endocytic receptor for Wingless in the Drosophila wing
Data show that GRIP is necessary for the trafficking of Frizzled-2 to the nucleus.
fzd2 are broadly expressed throughout the head, during zebrafish craniofacial development
frizzled 8c is a receptor for wnt8 (show WNT8A Proteins)
conserved role of a Wnt5 (show WNT5A Proteins)/Fz2 signaling pathway in islet formation during pancreatic development.
Treatment of the cell lines with Fzd2 siRNA resulted in significantly reduced migration and invasiveness but did not affect proliferation.Patients with high Fzd2 expression had significantly poorer recurrencefree survival than those with low expression
Fzd2 did not influence the proliferation of EC cells.
FZD2 was downregulated in an adenoid cystic carcinoma cell line with high metastatic potential, vs another with low potential. Knockdown of FZD2 downregulated the expression of PAI-1 (show SERPINE1 Proteins).
Sonazoid enhanced sonoporation of the cells with the diagnostic US device and the suppression of proliferation of both HCC (show FAM126A Proteins) cell lines by shRNA-Fz2.
the present study demonstrated that Fzd2 contributes to the migration and invasion of OSCC cells, at least partly through regulation of the STAT3 (show STAT3 Proteins) pathway
CD82 (show CD82 Proteins) enhanced the expression of miR (show MLXIP Proteins)-203 and directly downregulated FZD2 expression, suppressing cancer metastasis/cell migration by inhibiting the Wnt (show WNT2 Proteins) signaling pathway.
the FRIZZLED2 mutation is a de novo, novel cause for autosomal dominant omodysplasia.
Fz2 was positive in both the cell membrane and cytoplasm of gastric cancer tissues of moderately differentiated and poorly differentiated adenocarcinoma.Fz2 expression pattern in normal stomach tissues.
Pharmacologic and genetic perturbations reveal that Fzd2 drives epithelial-mesenchymal transition and cell migration through a previously unrecognized, noncanonical pathway that includes Fyn (show FYN Proteins) and Stat3 (show STAT3 Proteins).
Data suggest that an anti-Wnt5a antibody was capable of suppressing Wnt5a-dependent internalization of Fz2 receptor, resulting in the prevention of metastasis of gastric cancer cells by inhibiting the activation of Rac1 and the expression of laminin gamma2.
the Wnt5a (show WNT5A Proteins)/Frizzled-2 axis suppresses beta-catenin (show CTNNB1 Proteins) signaling in hepatocytes in an autocrine manner, thereby contributing to timely conclusion of the liver regeneration process
Fzd2 promotes changes in epithelial cell length and shape. These changes in cell morphology deform the developing lung epithelial tube to generate and maintain new domain branches.
Results provide further insight into the role of Wnt5a (show WNT5A Proteins) and Fzd2 in the pathogenesis of adult amyotrophic lateral sclerosis transgenic mice.
observed genetic interactions between Fz2 and Fz7 and five canonical and/or non-canonical signaling molecules: Dvl3 (show DVL3 Proteins), Wnt3a (show WNT3A Proteins), Wnt11 (show WNT11 Proteins), Vangl2 (show VANGL2 Proteins), and Wnt5a (show WNT5A Proteins).
Frizzled signaling is involved in diverse tissue closure processes, defects in which account for some of the most common congenital anomalies.
Indicate that myofibroblast migration and differentiation are modulated via Wnt (show WNT2 Proteins)/Fzd signalling.
Protein kinase (show CDK7 Proteins) G is a critical downstream effector of the noncanonical Wnt (show WNT2 Proteins)-Frizzled-2/cGMP/Ca2 (show CA2 Proteins)+ pathway
Preferential expression of Frizzled2 gene is detected in fetal liver kinase (Flk)1 (show KDR Proteins)-negative and Flk1 (show KDR Proteins)-positive cells under different culture conditions.
This intronless gene is a member of the frizzled gene family. Members of this family encode seven-transmembrane domain proteins that are receptors for the wingless type MMTV integration site family of signaling proteins. This gene encodes a protein that is coupled to the beta-catenin canonical signaling pathway. Competition between the wingless-type MMTV integration site family, member 3A and wingless-type MMTV integration site family, member 5A gene products for binding of this protein is thought to regulate the beta-catenin-dependent and -independent pathways.
, drosophila frizzled 2
, frizzled homolog 8
, frizzled homolog 2 (Drosophila)
, frizzled 2
, frizzled 2, seven transmembrane spanning receptor
, frizzled homolog 2
, Drosophila polarity gene (frizzled) homologue
, Drosophila polarity gene homolog 2