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

Abstract：

: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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Battersby A,Csiszár A,Leptin M,Wilson R

doi

10.1016/s0022-2836(03)00489-3

keywords:

subject

Has Abstract

pub_date

2003-06-06 00:00:00

pages

479-93

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022283603004893

journal_volume

329

pub_type

杂志文章

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