Frodo proteins: modulators of Wnt signaling in vertebrate development

• Published in: Differentiation (London) Vol. 73; no. 7; pp. 323 - 329
• Main Authors: Brott, Barbara K., Sokol, Sergei Y.
• Format: Journal Article
• Language: English
• Published: Malden, USA Elsevier B.V 01.09.2005; Blackwell Publishing Inc
• Subjects: Amino Acid Motifs; Amino Acid Sequence; Animals; Carrier Proteins - chemistry; Carrier Proteins - metabolism; Dapper; Dbf4; Disheveled; Embryo, Nonmammalian; epithelial–mesenchymal transition; Frd; Frodo; mesoderm; Models, Biological; Molecular Sequence Data; neural induction; nodal; organizer; Protein Structure, Tertiary; RNA, Messenger - metabolism; scaffold; Sequence Homology, Amino Acid; Signal Transduction; signaling; Sox2; vertebrate; Vertebrates - growth & development; Wnt; Wnt Proteins - metabolism; Xenopus - embryology; Xenopus - genetics; Xenopus - metabolism; Xenopus Proteins - chemistry; Xenopus Proteins - metabolism; Zebrafish - embryology; Zebrafish - genetics; Zebrafish - metabolism; Frodo; epithelial–mesenchymal transition; signaling; vertebrate; nodal; Dbf4; mesoderm; Sox2; scaffold; organizer; Frd; Disheveled; Wnt; Dapper; neural induction
• ISSN: 0301-4681; 1432-0436
• DOI: 10.1111/j.1432-0436.2005.00032.x

The Frodo/ dapper (Frd) proteins are recently discovered signaling adaptors, which functionally and physically interact with Wnt and Nodal signaling pathways during vertebrate development. The Frd1 and Frd2 genes are expressed in dynamic patterns in early embryos, frequently in cells undergoing epithelial–mesenchymal transition. The Frd proteins function in multiple developmental processes, including mesoderm and neural tissue specification, early morphogenetic cell movements, and organogenesis. Loss-of-function studies using morpholino antisense oligonucleotides demonstrate that the Frd proteins regulate Wnt signal transduction in a context-dependent manner and may be involved in Nodal signaling. The identification of Frd-associated factors and cellular targets of the Frd proteins should shed light on the molecular mechanisms underlying Frd functions in embryonic development and in cancer.