A given RTK may contain on the order of 10 20 phosphorylatable tyrosine residues with additional sites available on associated scaffold proteins resulting in a large number of potential sites for recruiting binding partners.
The prototypical example of this class of +TIP are EBs (end-binding proteins), which are involved in recruiting binding partners such as Clip170 and the dynein regulator dynactin to plus ends in metazoans (Watson and Stephens, 2006; Bieling et al., 2007; Dixit et al., 2009; Zanic et al., 2009; Maurer et al., 2012; Moughamian et al., 2013).
Acetylation in this context affects both the ability of transcription factors to bind DNA, and also to recruit other binding proteins (Goodman and Smolik, 2000).
In the absence, but not the presence of doxycycline, Sgo1-GFP-TetR is expected to bind to the ectopic site and recruit its binding partners.
All these proteins can bind adaptor proteins through SH2, SH3 or proline rich domains to recruit actin binding proteins (vinculin, paxillin and α-actinin) as well as regulatory molecules PI3K to focal complexes [ 39, 40].
These changes of histone acetylation allow chromatin open structure to recruit repressor binding to the hTERT 5'-regulatory region [15], [19].
In addition, the hypermethylated protein will recruit m5CpG-binding domain (MBD) containing proteins, which will be an obstacle for the binding of transcriptional factors to the promoters, thus inhibit gene transcription (Hendrich and Bird, 1998).
TGFβ1 binds to the TGFβR-IΙ, which in turn recruits the binding of TGFβR-I to form a heterotetramer.
CENP-A would then be recruited by binding directly to the damaged DNA, or via binding to other repair proteins [7].
