The N-terminal domain (also called
FERM domain) binds sodium-hydrogen exchanger regulatory factor (
NHERF) protein (involving long-range
allostery).[7] This binding can happen only when ezrin is in its active state. The activation of ezrin occurs in synergism of the two factors: 1) binding of the N-terminal domain to phosphatidylinositol(4,5)bis-phosphate (
PIP2) and 2) phosphorylation of threonine T567 in the C-terminal domain.[8][9] Binding to
actin filaments (via C-terminal) and to membrane proteins (via N-terminal) stabilizes the protein's conformation in its active mode. The membrane proteins like
CD44 and
ICAM-2 are indirect binding partners of ezrin, while EBP50 (ERM binding protein 50) can associate with ezrin directly.[10]
^Serrador JM, Nieto M, Alonso-Lebrero JL, del Pozo MA, Calvo J, Furthmayr H, Schwartz-Albiez R, Lozano F, González-Amaro R, Sánchez-Mateos P, Sánchez-Madrid F (June 1998). "CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts". Blood. 91 (12): 4632–44.
doi:
10.1182/blood.V91.12.4632.
PMID9616160.
^Grönholm M, Sainio M, Zhao F, Heiska L, Vaheri A, Carpén O (March 1999). "Homotypic and heterotypic interaction of the neurofibromatosis 2 tumor suppressor protein merlin and the ERM protein ezrin". J. Cell Sci. 112 (6): 895–904.
doi:
10.1242/jcs.112.6.895.
PMID10036239.
^Granés F, Urena JM, Rocamora N, Vilaró S (April 2000). "Ezrin links syndecan-2 to the cytoskeleton". J. Cell Sci. 113 (7): 1267–76.
doi:
10.1242/jcs.113.7.1267.
PMID10704377.
Martin TA, Harrison G, Mansel RE, Jiang WG (2004). "The role of the CD44/ezrin complex in cancer metastasis". Crit. Rev. Oncol. Hematol. 46 (2): 165–86.
doi:
10.1016/S1040-8428(02)00172-5.
PMID12711360.
The N-terminal domain (also called
FERM domain) binds sodium-hydrogen exchanger regulatory factor (
NHERF) protein (involving long-range
allostery).[7] This binding can happen only when ezrin is in its active state. The activation of ezrin occurs in synergism of the two factors: 1) binding of the N-terminal domain to phosphatidylinositol(4,5)bis-phosphate (
PIP2) and 2) phosphorylation of threonine T567 in the C-terminal domain.[8][9] Binding to
actin filaments (via C-terminal) and to membrane proteins (via N-terminal) stabilizes the protein's conformation in its active mode. The membrane proteins like
CD44 and
ICAM-2 are indirect binding partners of ezrin, while EBP50 (ERM binding protein 50) can associate with ezrin directly.[10]
^Serrador JM, Nieto M, Alonso-Lebrero JL, del Pozo MA, Calvo J, Furthmayr H, Schwartz-Albiez R, Lozano F, González-Amaro R, Sánchez-Mateos P, Sánchez-Madrid F (June 1998). "CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts". Blood. 91 (12): 4632–44.
doi:
10.1182/blood.V91.12.4632.
PMID9616160.
^Grönholm M, Sainio M, Zhao F, Heiska L, Vaheri A, Carpén O (March 1999). "Homotypic and heterotypic interaction of the neurofibromatosis 2 tumor suppressor protein merlin and the ERM protein ezrin". J. Cell Sci. 112 (6): 895–904.
doi:
10.1242/jcs.112.6.895.
PMID10036239.
^Granés F, Urena JM, Rocamora N, Vilaró S (April 2000). "Ezrin links syndecan-2 to the cytoskeleton". J. Cell Sci. 113 (7): 1267–76.
doi:
10.1242/jcs.113.7.1267.
PMID10704377.
Martin TA, Harrison G, Mansel RE, Jiang WG (2004). "The role of the CD44/ezrin complex in cancer metastasis". Crit. Rev. Oncol. Hematol. 46 (2): 165–86.
doi:
10.1016/S1040-8428(02)00172-5.
PMID12711360.