Regulation of Lyn and Lyn pathways.A) Domain architecture of Lyn. Schematic of Lyn protein functional domains and motifs, unique (UN), Src Homology 3 (SH3), Src Homology 2 (SH2), and Kinase domains, proline motif in the hinge region (P), amino terminal lipid modifications are indicated; myristoylation (navy blue) and palmitoylation (cyan). Important pY motifs that are phosphorylated in the inactive (pY508, red) and active (pY397, green) kinase are indicated, as is the LynA/p56 isoform-specific motif pY32 that may modulate activity/interactions. Intramolecular interactions between the SH3 domain and the hinge (P) region, as well as the SH2 domain and the C-terminal pY508 motif are shown. B) Lyn regulation of positive and negative signaling pathways. Lyn regulates multiple signaling pathways by interacting with and/or phosphorylating different molecules that can mediate both the activation/enhancement as well as the inhibition/termination of signaling networks, as illustrated.
Ingley Cell Communication and Signaling 2012 10:21 doi:10.1186/1478-811X-10-21