Schematic representation of ERM protein activation in leukocytes In their inactive conformation, the

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Schematic representation of ERM protein
activation in leukocytesIn their inactive
conformation, the N-terminal domain of ERM
proteins (red) binds to the C-terminal
actin-binding domain (green) either via an
intramolecular or intermolecular interaction
(forming either folded monomers or anti-parallel
dimmers, respectively). The alpha helical domain
is coloured in orange. Binding of phosphatidyl
inositol 4, 5, bisphosphate (PIP2) to the
N-terminal domain and phosphorylation of the
critical C-terminal threonine (amino acid
position indicated for each ERM protein) induce
and stabilize the unfolded active conformation of
ERM proteins, allowing the N-terminal domain to
bind to transmembrane receptors and the
actin-binding domain to interact with actin
filaments (F-actin). Activation of ERM proteins
can be stimulated by the RhoGTPase, RhoA.
Conversely, dephosphorylation of the C-terminal
threonine may be regulated by Rac. Yellow star
indicates phosphorylation of critical C-terminal
residue. Taken from Ivetic Ridley 2004
Immunology 112 (2) p165-76.