However, we should consider other independently reported docking proteins, such as Dok1, SH2B1 and SH2B2 to the macromolecular docking process.
Taken together, a series of studies over the last decade has shown that the tyrosine phosphorylation and signalling potential of docking proteins such as those of Gab, IRS, FRS and SLP families is counteracted by their Ser/Thr-phosphorylation, which usually represents the endpoint of feedback loops from cytoplasmic signalling cascades [ 13, 15, 49, 81, 169, 177, 181].
This notion is further supported by recent phospho-proteomic analyses of other large docking proteins such as Gab1 [ 56, 57] or SLP-65/BLNK [ 58].
The regulatory subunit contains two SH2 domains that bind specifically to pYXXM motifs in a variety of cellular proteins, including receptor tyrosine kinases such as the PDGF (platelet-derived growth factor) receptor, and c-kit and docking proteins such as IRS (insulin receptor substrate) 1, IRS2 and Gab1.
Several docking proteins such as KSR, SLP-76 and IRS proteins have been described as 14-3-3 14-3-3 14-3-3ns [ 4, 15, 181] and we reclient reproteinshat Gab2 interacts with 14-3-3 proteins in a phosphorylation-dependent manner [ 49].
This is followed by activation of second messengers, also called docking proteins, such as the insulin receptor substrates-1, -2, -3 and -4, (IRS-1, -2, -3 and -4) [ 23- 26] via a series of phosphorylation-dephosphorylation reactions that result in stimulation of glucose metabolism [ 27].
Upon cell contact, Ca2+-dependent homotypic engagement of cadherins occurs, which allows for the docking of other proteins such as catenins.
Ligand induced phosphorylation of EGF receptor creates docking sites for adaptor proteins, such as EPS15, epsin and AP-2 [ 6, 7].
This motif is also a docking site for cytosolic proteins, such as Fe65, that regulate APP metabolism and signaling [12].
In addition to FcεRI subunits, SHIP has several other potential docking partners, including adaptor proteins such as Shc, Grb2, and Dok.
JAK2 activation is followed by tyrosine phosphorylation within the receptor cytoplasmic domain which generates docking sites for SH2 domain containing proteins such as STAT3 or STAT5, so that the docked protein is phosphorylated and activated.
