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. 2019 Dec 17;6:144. doi: 10.3389/fmolb.2019.00144

Figure 2.

Figure 2

Autoinhibition of focal adhesion proteins. (A–C) Schematic diagrams of active and autoinhibited (A) talin, (B) vinculin, and (C) FAK. Insets: The crystal structures of the autoinhibitory interactions are shown. (A) Talin: F3 of the FERM domain and R9 of the rod are the primary interacting domains in talin autoinhibition. K318 and E1770 are required for this interaction to take place, forming a key buried salt bridge. Adapted from crystal structure PDB ID: 4F7G (Song et al., 2012). (B) Vinculin: the vinculin tail, Vt, interacts with both Vd1 and Vd4 domains of the head to form a strong autoinhibitory conformation. Mutating residues D974, K975, R976, R978 (Cohen et al., 2005) results in a constitutively active vinculin by disrupting the interaction between Vt and Vd4. Adapted from crystal structure PDB ID: 1TR2 (Borgon et al., 2004). (C) Focal adhesion kinase: F2 of the FERM domain of FAK interacts with the C-lobe of the kinase domain to keep FAK in a closed conformation, rendering a key tyrosine in the linker between these domains (Y397) inaccessible to phosphorylation. Adapted from crystal structure PDB ID: 2J0J (Lietha et al., 2007). Images made using PyMOL.