Signal transduction termination

Noncatalytic phosphotyrosine binding (PTB) domains are 100-150 residue modules, which bind Asn-Pro-X-Tyr motifs. PTB-domain binding specificity is determined by residues at the amino-terminal side of the phosphotyrosine. In most cases, the tyrosine residue must be phosphorylated in order to mediate binding. PTB domain containing proteins are often found in signal transduction pathways. 

As discussed above, for all smooth muscle cells, the terminal sequence of the signal transduction pathways which regulates contraction seems to be the same. As... 

Ruan Y, Chen C, Cao Y, Garofalo RS 1995 The Drosophila insulin receptor contains a novel carboxyl-terminal extension likely to play an important role in signal transduction. J Biol Chem 270 4236-4243... 

Halavaty, A. S. and K. Moffat (2007). N- and C-terminal flanking regions modulate light-induced signal transduction in the LOV2 domain of the blue-light sensor photo tropin 1 from Avena sativa. Biochemistry 46 14001-14009. 

Numerous studies have shown that EGF binding to EGFR triggers receptor dimerization. This is considered a crucial step in intracellular signal transduction [98]. Inspired by this mechanism, we designed EGF chimeric proteins that spontaneously dimerized (dEGF-His). These dimers were terminally anchored to the substrate. We expected that these preformed dimeric EGF structures would facilitate the formation of EGF-EGFR dimer complexes more efficiently than monomeric EGF structures. 

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