Schematics of autoinhibited and activated forms of other integrin-based adhesion-associated proteins. Cartoon representation of some of the known adhesion proteins that are regulated by autoinhibition. Top: Autoinhibited (Off) conformation; Bottom: Active (On) conformation. (A) RIAM, comprised of two Talin-Binding Sites (TBS), and an INhibition motif (IN), a Ras-Association domain (RA), a Pleckstrin Homology (PH), and a Poly-proline motif. Autoinhibition is mediated by interaction between the IN and RA domains (Chang et al., 2019). (B) Src, comprised of a Kinase domain (SH1), a Src homology 2 domain (SH2) and a Src homology 3 domain (SH3). Autoinhibition is mediated by interaction between the SH2 domain and phosphorylated Tyr527 at the C-terminus (Shenoy et al., 1992). (C) Zyxin, comprised of an N-terminal region with Proline-rich “ActA” repeats, Nuclear Export Sequences (NES), and three LIM domains. Autoinhibition is mediated by interaction between the ActA and LIM domains (Nix et al., 2001; Call et al., 2011). (D) DLC1, comprised of a Sterile Alpha Motif (SAM), a Rho-GTPase Activating Protein domain (RhoGAP) and a STeroidogenic Acute Regulatory protein-related lipid-Transfer domain (START). Autoinhibition is mediated by interaction between the SAM and RhoGAP domains (Kim et al., 2008). (E) FHOD1, comprised of a GTPase-Binding Domain (GBD), a DAD Interacting Domain (DID), a Formin-Homology 2 (FH2) and a Diaphanous-Autoregulatory Domain (DAD). Autoinhibition is mediated by interaction between the DID and DAD domains (Takeya et al., 2008). (F) WASP, comprised of an Ena/VASP Homology-1 domain (EVH1), a GTPase-Binding Domain (GBD), and a Verprolin homology, Central hydrophobic and Acidic domain (VCA). Autoinhibition is mediated by interaction between the GBD and VCA domains (Kim et al., 2000).