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PMID:21718540

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Citation

Kivimäe, S, Yang, XY and Cheyette, BN (2011) All Dact (Dapper/Frodo) scaffold proteins dimerize and exhibit conserved interactions with Vangl, Dvl, and serine/threonine kinases. BMC Biochem. 12:33

Abstract

The Dact family of scaffold proteins was discovered by virtue of binding to Dvl proteins central to Wnt and Planar Cell Polarity (PCP) signaling. Subsequently Dact proteins have been linked to a growing list of potential partners implicated in β-catenin-dependent and β-catenin-independent forms of Wnt and other signaling. To clarify conserved and non-conserved roles for this protein family, we systematically compared molecular interactions of all three murine Dact paralogs by co-immunoprecipitation of proteins recombinantly expressed in cultured human embryonic kidney cells.

Links

PubMed PMC3141656 Online version:10.1186/1471-2091-12-33

Keywords

Adaptor Proteins, Signal Transducing/genetics; Adaptor Proteins, Signal Transducing/metabolism; Animals; Carrier Proteins/metabolism; Casein Kinase Idelta/metabolism; Casein Kinase Iepsilon/metabolism; Catenins/metabolism; Cell Line; Dimerization; Electrophoresis, Polyacrylamide Gel; Glycogen Synthase Kinase 3/metabolism; Hepatocyte Nuclear Factor 1-alpha/metabolism; Histone Deacetylase 1/metabolism; Humans; Immunoprecipitation; Intracellular Signaling Peptides and Proteins/genetics; Intracellular Signaling Peptides and Proteins/metabolism; Membrane Proteins/metabolism; Mice; Molecular Weight; Nerve Tissue Proteins/metabolism; Phosphoproteins/chemistry; Phosphoproteins/metabolism; Protein Interaction Maps; Protein-Serine-Threonine Kinases/metabolism; Receptors, Transforming Growth Factor beta/metabolism; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; T Cell Transcription Factor 1/metabolism

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