High impact information on Fzd1

• Several members of the Wnt family, as well as other molecules involved in Wnt signaling, including Frizzled receptors, LDL-related protein co-receptors, members of the Dishevelled and Dickkopf families, are known to be expressed in the lens during embryonic or postembryonic development [1].
• Localization of disulfide bonds in the frizzled module of Ror1 receptor tyrosine kinase [2].
• With an eye toward defining the structure of this important module family, we have expressed the FRZ domain of rat Ror1 receptor tyrosine kinase in Pichia pastoris [2].
• A review of prior data on other receptors suggests that this receptor may belong to a unique class of seven-transmembrane receptors (including somatostatin SSTR1, dopamine D3, and frizzled protein Fz) for which G protein coupling has not been demonstrated [3].
• Frizzled related proteins (Frps) are secreted proteins structurally similar to frizzled receptors; they bind Wnt via the cysteine-rich domain and antagonize the Wnt signaling pathway [4].

Biological context of Fzd1

• A PCR screening of a rat cochlea cDNA library performed with degenerate primers allowed us to isolate five members of the Wnt gene family (RWnt-2B, -4, -5A, -5B, and -7A) and six members of the Frizzled gene family (Rfz1, Rfz2, Rfz3, Rfz4, Rfz6, Rfz9) [5].

Anatomical context of Fzd1

• Expression of members of Wnt and Frizzled gene families in the postnatal rat cochlea [5].

Associations of Fzd1 with chemical compounds

• The study also points to the existence of novel uterine signaling pathways, including Wnt/frizzled and receptor activator of nuclear factor-kappaB (RANK) and its ligand, as well as the involvement of novel signaling molecules such as estrogen-responsive gene 1, decay-accelerating factor 1, and ebnerin [6].

Analytical, diagnostic and therapeutic context of Fzd1

• Circular dichroism and differential scanning calorimetry studies on the recombinant protein indicate that the disulfide-bonded FRZ module corresponds to a single, compact, and remarkably stable folding domain possessing both alpha-helices and beta-strands [2].

References