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Fig. 1 | Cell Communication and Signaling

Fig. 1

From: Src family kinases, adaptor proteins and the actin cytoskeleton in epithelial-to-mesenchymal transition

Fig. 1

Primary structure of SRC family kinases. Domain and signal conservation within Src family kinases. Src family kinases are activated at the membrane, which involves lipid/myristate modification within the SH4 region and membrane binding. There is very little known about the UD, which might be also involved in membrane localization, activation and ligand substrate binding (see lower panel for LCK). SH3 and SH2 domain bind substrates and regulate the catalytic activity of the tyrosine kinase (domain). Posttranslational modifications in Src family kinases essential for membrane localization (myristylation and palmytoilation); activation (within kinase domain) and inhibition (C-terminal tail) (phosphorylation) are highlighted in the diagram. Domain/regulatory regions are depicted as lines and boxes: Src homology 1, SH1, tyrosine kinase/catalytic domain; SRC homology 2 or SH2; SRC homology 3, SH3; SRC homology 4, SH4, and unstructured Unique Domain, UD). Bottom panels: NMR Structural Ensemble of the C-terminal tail of (A) CD4 (red) or (B) CD8α (magenta) in complex with the intrinsically disordered Unique Domain of LCK (residues 7–35). Both complexes are very dynamic and are mediated by Zn (blue spheres). The pdb codes are 1Q68 and 1Q69 for CD4 and CD8α, respectively

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