TY - JOUR
T1 - Opening of Holes in Liposomal Membranes Is Induced by Proteins Possessing the FERM Domain
AU - Takeda, Shuichi
AU - Saitoh, Akihiko
AU - Furuta, Mayumi
AU - Satomi, Nao
AU - Ishino, Atsushi
AU - Nishida, Gakushi
AU - Sudo, Hiroaki
AU - Hotani, Hirokazu
AU - Takiguchi, Kingo
N1 - Funding Information:
We thank Professor Keiji Naruse (Okayama University), and the Hoshi-ga-oka Maternity Clinic, the Shibata Obstetrician and Gynecological Clinic, and the Chubu Medical Co. for providing specimens of human placenta. Human placentas were obtained from these medical facilities appropriately. This study was supported by the Ministry of Education, Science, Sports and Culture of Japan.
PY - 2006/9/22
Y1 - 2006/9/22
N2 - The destabilization of vesicles caused by interactions between lipid bilayers and proteins was studied by direct, real-time observation using high-intensity dark-field microscopy. We previously reported that talin, a cytoskeletal submembranous protein, can reversibly open stable large holes in giant liposomes made of neutral and acidic phospholipids. Talin and other proteins belonging to the band 4.1 superfamily have the FERM domain at their N-terminal and interact with lipid membranes via that domain. Here, we observed that band 4.1, ezrin and moesin, members of the band 4.1 superfamily, are also able to open stable holes in liposomes. However, truncation of their C-terminal domains, which can interact with the N-terminal FERM domain, impaired their hole opening activities. Oligomeric states of ezrin affected the capability of the membrane hole formation. Phosphatidylinositol bisphosphate (PIP2), which binds to the FERM domain and disrupts the interaction between the N and C termini of the band 4.1 superfamily, down-regulates their membrane opening activity. These results suggest that the intermolecular interaction plays a key role in the observed membrane hole formation.
AB - The destabilization of vesicles caused by interactions between lipid bilayers and proteins was studied by direct, real-time observation using high-intensity dark-field microscopy. We previously reported that talin, a cytoskeletal submembranous protein, can reversibly open stable large holes in giant liposomes made of neutral and acidic phospholipids. Talin and other proteins belonging to the band 4.1 superfamily have the FERM domain at their N-terminal and interact with lipid membranes via that domain. Here, we observed that band 4.1, ezrin and moesin, members of the band 4.1 superfamily, are also able to open stable holes in liposomes. However, truncation of their C-terminal domains, which can interact with the N-terminal FERM domain, impaired their hole opening activities. Oligomeric states of ezrin affected the capability of the membrane hole formation. Phosphatidylinositol bisphosphate (PIP2), which binds to the FERM domain and disrupts the interaction between the N and C termini of the band 4.1 superfamily, down-regulates their membrane opening activity. These results suggest that the intermolecular interaction plays a key role in the observed membrane hole formation.
KW - band 4.1 superfamily
KW - giant liposome
KW - membrane perturbation
KW - membrane-protein interaction
KW - optical microscopy
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U2 - 10.1016/j.jmb.2006.07.071
DO - 10.1016/j.jmb.2006.07.071
M3 - Article
C2 - 16934293
AN - SCOPUS:33748102835
SN - 0022-2836
VL - 362
SP - 403
EP - 413
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 3
ER -