Fig. 1

MARCKS protein structure and electrostatic switch. a MARCKS protein has three protein domains, the N-Terminal domain (ND), which can be myristoylated (Myr), an MH2 domain (MH2D) and an effector domain (ED). The ED (amino acids 152–176 in human MARCKS) is magnified in the inset showing that it is highly positively charged and has 4 potential phosphorylation sites, one of which (asterisk) is poorly phosphorylated. b In the unphosphorylated state and in the absence of Calcium-calmodulin (CaM) binding, MARCKS is tethered to the membrane but becomes released into the cytosol when phosphorylated by protein kinase C (PKC) or Rho kinase (ROCK) or after Calcium-CaM binding. Modified from [8]