The cognate ligand for CD40, CD154 (CD40 ligand, CD40L, gp39, TRAP) does not bind other TNFR although it can interact with the soluble complement inhibitor C4b binding protein which may function as a competitive inhibitor of CD40 activation [8].
The involvement of a phosphorylated tyrosine residue in the functioning of Eps15 suggest the binding to a phosphotyrosine binding protein, which may recruit Eps15 either to the receptor or to the endocytic machinery.
It was shown by Haegebarth et al (2005) that PTK6 negatively regulates the activity of RNA-binding proteins, which may have an impact on the post-transcriptional regulation of gene expression (Haegebarth et al, 2005).
The efficient delivery and proper localization of the EGS in cells may be mediated by cellular tRNA-binding proteins, which may interact with the tRNA-like domains of the EGS and target the EGS for interactions with RNase P, a tRNA-processing enzyme [ 15].
The role of endocrine liver-derived and locally tissue produced IGF-I to promote protein synthesis in response to feeding is however unclear, in part due to complex conditions with different IGF-binding proteins, which may also have independent control functions of net protein metabolism at tissue levels [ 10- 12].
In 2003, STAT1 was shown to synergize with NF-κB at the promoter of the CXCL9 gene to bind the transcriptional co-activator, CREB-binding protein, which may in turn recruit the RNApolII complex [ 27].
Our reported increase in plasma retinol in this model of type 2 diabetes is in contrast to the type 1 diabetes data, but is consistent with previous reports of diabetes-induced increases in RBP4, a retinol-binding protein which may be a biomarker of type 2 diabetes and insulin resistance [17].
The mRNA encoding RBP10, an RNA-binding protein which may control the abundance of several mRNAs required for glycolysis (M. Wurst and R. Queiroz, ZMBH, unpublished results), varied in parallel with its possible targets.
