Isolation of proteins that interact with the signal transduction molecule Dof and identification of a functional domain conserved between Dof and vertebrate BCAP.

Dof is a large molecule essential for signal transduction by the two FGF receptors in Drosophila. It contains two ankyrin repeats and a coiled-coil region, but has no other recognisable structural motif. Dof shares these features with its closest vertebrate relatives, the B-cell signalling molecules BCAP and BANK. In addition, ...
this family of proteins shares a region of homology upstream of the ankyrin repeats, which we call the Dof/BCAP/BANK (DBB) motif. We have identified 44 proteins that interact with Dof in a yeast two-hybrid screen. These include the Drosophila FGF-receptor Heartless and Dof itself. We show that the integrity of the DBB motif is required both for Dof and for BCAP to form dimers. Analysis of the interactions between a set of deletion constructs of Dof and the panel of interactors suggests that Dof may adopt different conformations, with a folded conformation stabilized by interactions between the DBB motif and the C-terminal part of the protein.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Motifs, Amino Acid Sequence, Animals, Binding Sites, Carrier Proteins, Cells, Cultured, Conserved Sequence, Dimerization, Drosophila, Drosophila Proteins, Gene Expression Regulation, Developmental, In Situ Hybridization, Insect Proteins, Membrane Proteins, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, RNA, Messenger, Receptors, Fibroblast Growth Factor, Signal Transduction, Two-Hybrid System Techniques
J. Mol. Biol.
Date: Jun. 06, 2003
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