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Figure 6.
FIGURE 6. Comparison of FERM-binding modes of NEP and
ICAM-2 peptides bound to the FERM domain. A, comparison of NEP
and ICAM-2 cytoplasmic peptides bound to the radixin FERM
domain. Superposition of the ICAM-2 cytoplasmic tail (magenta)
in the FERM-ICAM-2 complex on the NEP (blue)-FERM (gray)
complex. The N-terminal (ICAM-2) or C-terminal (NEP) regions
that would be linked to the trans-membrane helix is indicated
with dotted lines. B, schematic representation of ERM proteins
bound to type I and II membrane proteins on the plasma membrane.
ERM proteins have the N-terminal FERM (blue triangle) and
C-terminal F-actin binding (red block) domains. The FERM domain
of membrane-recruited ERM proteins binds the cytoplasmic tails,
whereas the C-terminal domain binds actin filaments (cyan). The
FERM domain binds the juxtamembrane region (a yellow arrow,
Motif-1) of the C-terminal cytoplasmic tail of type I membrane
proteins such as adhesion molecules CD44 and ICAM-2. In the case
of type II membrane protein NEP, the FERM domain binds the
N-terminal cytoplasmic tail at a distal region (a pink arrow,
Motif-1  ) from the membrane.
These two binding interactions interfere with one another by
direct competition for binding to the same groove of the FERM
domain.
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