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. 2020 Aug 11;39(19):e104743. doi: 10.15252/embj.2020104743

Figure EV2. Known PI(4,5)P2‐binding sites in FAK support membrane placement.

Figure EV2

  1. The KAKTLRK sequences (colored red) known to interact with PI(4,5)P2 lipid membranes (Cai et al, 2008; Goni et al, 2014) align in all FERM domains of the cryo‐EM particle in one plane allowing positioning of the membrane as shown in Fig 1F.
  2. Unmodeled density at the KAKTLRK sites (red) in FERM domains (light arrowheads) and unmodeled density at K621/K627 residues (cyan) in the kinase domains (dark arrowheads) coincide with the position of the modeled membrane and likely represent lipid molecules with restricted mobility due to their interactions with FAK.