Ezrin, moesin, and radixin are highly related proteins (
ERM protein family), but the other proteins in which the FERM domain is found do not share any region of similarity outside of this domain. ERM proteins are made of three domains, the FERM domain, a central
helical domain and a C-terminal tail domain, which binds
F-actin. The amino-acid
sequence of the FERM domain is highly conserved among ERM proteins and is responsible for
membrane association by direct binding to the cytoplasmic domain or tail of
integral membrane proteins. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail
domains that masks their
binding sites for other
molecules. For cytoskeleton-membrane cross-linking, the dormant molecules becomes activated and the FERM domain attaches to the membrane by binding specific membrane proteins, while the last 34
residues of the tail bind
actin filaments. Aside from binding to membranes, the activated FERM domain of ERM proteins can also bind the
guaninenucleotide dissociation inhibitor of Rho
GTPase (RhoDGI), which suggests that in addition to functioning as a cross-linker, ERM proteins may influence Rho
signalling pathways. The
crystal structure of the FERM domain reveals that it is composed of three
structural modules (F1, F2, and F3) that together form a compact clover-shaped
structure.[3] The N-terminal module is
ubiquitin-like. The C-terminal module is a
PH-like domain.
The FERM domain has also been called the amino-terminal domain, the 30kDa domain, 4.1N30, the membrane-cytoskeletal-linking domain, the ERM-like domain, the ezrin-like domain of the band 4.1 superfamily, the
conserved N-terminal region, and the membrane attachment domain.[1]
Ezrin, a component of the undercoat of the
microvilli plasma membrane.
Moesin, which is probably involved in binding major
cytoskeletal structures to the plasma membrane.
Radixin, which is involved in the binding of the barbed end of
actin filaments to the plasma membrane in the undercoat of the cell-to-cell
Adherens junction.
Talin, a
cytoskeletal protein concentrated in regions of cell-substratum contact and, in
lymphocytes, of cell-cell contacts.
^
abcChishti AH, Kim AC, Marfatia SM, Lutchman M, Hanspal M, Jindal H, Liu SC, Low PS, Rouleau GA, Mohandas N, Chasis JA, Conboy JG, Gascard P, Takakuwa Y, Huang SC, Benz EJ, Bretscher A, Fehon RG, Gusella JF, Ramesh V, Solomon F, Marchesi VT, Tsukita S, Tsukita S, Hoover KB (August 1998). "The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane". Trends Biochem. Sci. 23 (8): 281–2.
doi:
10.1016/S0968-0004(98)01237-7.
PMID9757824.
Ezrin, moesin, and radixin are highly related proteins (
ERM protein family), but the other proteins in which the FERM domain is found do not share any region of similarity outside of this domain. ERM proteins are made of three domains, the FERM domain, a central
helical domain and a C-terminal tail domain, which binds
F-actin. The amino-acid
sequence of the FERM domain is highly conserved among ERM proteins and is responsible for
membrane association by direct binding to the cytoplasmic domain or tail of
integral membrane proteins. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail
domains that masks their
binding sites for other
molecules. For cytoskeleton-membrane cross-linking, the dormant molecules becomes activated and the FERM domain attaches to the membrane by binding specific membrane proteins, while the last 34
residues of the tail bind
actin filaments. Aside from binding to membranes, the activated FERM domain of ERM proteins can also bind the
guaninenucleotide dissociation inhibitor of Rho
GTPase (RhoDGI), which suggests that in addition to functioning as a cross-linker, ERM proteins may influence Rho
signalling pathways. The
crystal structure of the FERM domain reveals that it is composed of three
structural modules (F1, F2, and F3) that together form a compact clover-shaped
structure.[3] The N-terminal module is
ubiquitin-like. The C-terminal module is a
PH-like domain.
The FERM domain has also been called the amino-terminal domain, the 30kDa domain, 4.1N30, the membrane-cytoskeletal-linking domain, the ERM-like domain, the ezrin-like domain of the band 4.1 superfamily, the
conserved N-terminal region, and the membrane attachment domain.[1]
Ezrin, a component of the undercoat of the
microvilli plasma membrane.
Moesin, which is probably involved in binding major
cytoskeletal structures to the plasma membrane.
Radixin, which is involved in the binding of the barbed end of
actin filaments to the plasma membrane in the undercoat of the cell-to-cell
Adherens junction.
Talin, a
cytoskeletal protein concentrated in regions of cell-substratum contact and, in
lymphocytes, of cell-cell contacts.
^
abcChishti AH, Kim AC, Marfatia SM, Lutchman M, Hanspal M, Jindal H, Liu SC, Low PS, Rouleau GA, Mohandas N, Chasis JA, Conboy JG, Gascard P, Takakuwa Y, Huang SC, Benz EJ, Bretscher A, Fehon RG, Gusella JF, Ramesh V, Solomon F, Marchesi VT, Tsukita S, Tsukita S, Hoover KB (August 1998). "The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane". Trends Biochem. Sci. 23 (8): 281–2.
doi:
10.1016/S0968-0004(98)01237-7.
PMID9757824.