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The effect of ethylene upon the ERS1 complex is reminiscent of ligand-induced changes in complexes formed by animal receptor tyrosine kinases, where ligand binding induces autophosphorylation and the recruitment of proteins that bind to the phosphorylated sites [32], [47].
Mammalian SWI/SNF complexes participate in DNA double-strand break repair as they bind to the phosphorylated H2A histone family, member X (H2AX), histone variant, and promote its phosphorylation [ 11].
Neither of these Axin mutants is expected to bind to the phosphorylated PPPSPXS motif because the DIX domain, which is deleted in both Axin mutants (Figure 4), is required for such binding [36; H. H. and X. H., unpublished results].
To investigate whether the Axin-bound GSK3β is able to bind to the phosphorylated LRP6 fragments (miniCL), we incubated GSK3β with excess Axin GBD protein to saturate its binding to GSK3β and then tested the binding of GSK3β and LRP6 using the same far western blot analysis (Fig. 4B).
SOCS proteins can directly bind to the phosphorylated forms of JAKs via their central domain SH2 and the C-terminal SOCS box region.
Various adaptor molecules bind to the phosphorylated receptors, resulting in signal transduction initiation that ultimately regulates gene transcription (Yarden and Sliwkowski, 2001).
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STAT5 proteins bind to the tyrosine phosphorylated Epo receptor and gets phosphorylation.
Since Axin is a scaffolding protein critical for GSK3 phosphorylation of β-catenin and binds to the phosphorylated PPPSPXS motif [34], [35], [37], we considered the possibility whether inhibition of β-catenin phosphorylation by the phosphorylated PPPSPXP motif involves the binding between Axin and the phosphorylated PPPSPXS motif.
Among these interacting proteins, PI3K which binds to the phosphorylated tyrosine 740/751 residues (739/750 in the mouse) of PDGFRβ through its p85 regulatory subunit [9], is particularly important for regulating actin organization [10], [11], cell growth and migration [12].
Activated PDGFRβ undergoes tyrosine phosphorylation and subsequently interacts with various signaling molecules, including phosphatidylinositol 3-kinase (PI3K), which binds to the phosphorylated tyrosine 739/750 residues in mice, and thus regulates actin polymerization and cell movement.
The c-Cbl TKB domain consists of three tightly-connected domains: a divergent SH2 domain that binds to the phosphorylated tyrosine; a four-helix bundle (4H) which packs against the SH2 domain and completes the phosphotyrosine binding pocket; and a calcium-binding EF-hand, which wedges between the SH2 and 4H domains [10].
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