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Volumn 362, Issue 3, 2006, Pages 403-413

Opening of Holes in Liposomal Membranes Is Induced by Proteins Possessing the FERM Domain

Author keywords

band 4.1 superfamily; giant liposome; membrane perturbation; membrane protein interaction; optical microscopy

Indexed keywords

EZRIN; LIPOSOME;

EID: 33748102835     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.07.071     Document Type: Article
Times cited : (23)

References (55)
  • 4
    • 0016377872 scopus 로고
    • Bending resistance and chemically induced moments in membrane bilayers
    • Evans E.A. Bending resistance and chemically induced moments in membrane bilayers. Biophys. J. 14 (1974) 923-931
    • (1974) Biophys. J. , vol.14 , pp. 923-931
    • Evans, E.A.1
  • 5
    • 0025968124 scopus 로고
    • The conformation of membranes
    • Lipowsky R. The conformation of membranes. Nature 349 (1991) 475-481
    • (1991) Nature , vol.349 , pp. 475-481
    • Lipowsky, R.1
  • 6
    • 0029444559 scopus 로고
    • Surrogate cells or Trojan horses. The discovery of liposomes
    • Bangham A.D. Surrogate cells or Trojan horses. The discovery of liposomes. BioEssays 17 (1995) 1081-1088
    • (1995) BioEssays , vol.17 , pp. 1081-1088
    • Bangham, A.D.1
  • 7
    • 77957030218 scopus 로고
    • Applications of liposomes
    • Lipowsky R., and Sackmann E. (Eds), Elsevier Science, B.V., Amsterdam
    • Lasic D.D. Applications of liposomes. In: Lipowsky R., and Sackmann E. (Eds). Structure and Dynamics of Membranes, Handbook of Biological Physics vol. 1A (1995), Elsevier Science, B.V., Amsterdam 491-519
    • (1995) Structure and Dynamics of Membranes, Handbook of Biological Physics , vol.1 A , pp. 491-519
    • Lasic, D.D.1
  • 8
    • 0030569732 scopus 로고    scopus 로고
    • Supported membranes: scientific and practical applications
    • Sackmann E. Supported membranes: scientific and practical applications. Science 271 (1996) 43-48
    • (1996) Science , vol.271 , pp. 43-48
    • Sackmann, E.1
  • 9
    • 0031036238 scopus 로고    scopus 로고
    • Structure of DNA-cationic liposome complexes: DNA intercalation in multilamellar membranes in distinct interhelical packing regimes
    • Rädler J.O., Koltover I., Salditt T., and Safinya R.C. Structure of DNA-cationic liposome complexes: DNA intercalation in multilamellar membranes in distinct interhelical packing regimes. Science 275 (1997) 810-814
    • (1997) Science , vol.275 , pp. 810-814
    • Rädler, J.O.1    Koltover, I.2    Salditt, T.3    Safinya, R.C.4
  • 11
    • 77957815991 scopus 로고
    • Electroporation and electrofusion of membranes
    • Lipowsky R., and Sackmann E. (Eds), Elsevier Science, B.V., Amsterdam
    • Dimitrov D.S. Electroporation and electrofusion of membranes. In: Lipowsky R., and Sackmann E. (Eds). Structure and Dynamics of Membranes, Handbook of Biological Physics vol. 1B (1995), Elsevier Science, B.V., Amsterdam 851-901
    • (1995) Structure and Dynamics of Membranes, Handbook of Biological Physics , vol.1 B , pp. 851-901
    • Dimitrov, D.S.1
  • 12
    • 0022534722 scopus 로고
    • Interaction of plasma membrane fibronectin receptor with talin-A- transmembrane linkage
    • Horwitz A., Duggan K., Buck C., Beckerle M.C., and Burridge K. Interaction of plasma membrane fibronectin receptor with talin-A- transmembrane linkage. Nature 320 (1986) 531-533
    • (1986) Nature , vol.320 , pp. 531-533
    • Horwitz, A.1    Duggan, K.2    Buck, C.3    Beckerle, M.C.4    Burridge, K.5
  • 13
    • 0023803639 scopus 로고
    • Dynamic membrane-cytoskeletal interactions: specific association of integrin and talin arises in vivo after phorbol ester treatment of peripheral blood lymphocytes
    • Burn P., Kupher A., and Singer S.J. Dynamic membrane-cytoskeletal interactions: specific association of integrin and talin arises in vivo after phorbol ester treatment of peripheral blood lymphocytes. Proc. Natl Acad. Sci. USA 85 (1988) 497-501
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 497-501
    • Burn, P.1    Kupher, A.2    Singer, S.J.3
  • 14
    • 0026483847 scopus 로고
    • Talin anchors and nucleates actin filaments at lipid membranes. A direct demonstration
    • Kaufmann S., Käs J., Goldmann H., Sackmann E., and Isenberg G. Talin anchors and nucleates actin filaments at lipid membranes. A direct demonstration. FEBS Letters 314 (1992) 203-205
    • (1992) FEBS Letters , vol.314 , pp. 203-205
    • Kaufmann, S.1    Käs, J.2    Goldmann, H.3    Sackmann, E.4    Isenberg, G.5
  • 16
    • 21044443928 scopus 로고    scopus 로고
    • Inositol-lipid binding motifs: signal integrators through protein-lipid and protein-protein interactions
    • Balla T. Inositol-lipid binding motifs: signal integrators through protein-lipid and protein-protein interactions. J. Cell Sci. 118 (2005) 2093-2104
    • (2005) J. Cell Sci. , vol.118 , pp. 2093-2104
    • Balla, T.1
  • 17
    • 0031683065 scopus 로고    scopus 로고
    • The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane
    • Chishti A.H., Kim A.C., Marfatia S.M., Lutchman M., Hanspal M., Jindal H., et al. The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane. Trends Biochem. Sci. 23 (1998) 281-282
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 281-282
    • Chishti, A.H.1    Kim, A.C.2    Marfatia, S.M.3    Lutchman, M.4    Hanspal, M.5    Jindal, H.6
  • 18
    • 0031043523 scopus 로고    scopus 로고
    • ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction
    • Sa T., Yonemura S., and Sh. T. ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction. Curr. Opin. Cell Biol. 9 (1997) 70-75
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 70-75
    • Sa, T.1    Yonemura, S.2    Sh., T.3
  • 19
    • 0029121577 scopus 로고
    • Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site
    • Gary R., and Bretscher A. Ezrin self-association involves binding of an N-terminal domain to a normally masked C-terminal domain that includes the F-actin binding site. Mol. Biol. Cell 6 (1995) 1061-1075
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1061-1075
    • Gary, R.1    Bretscher, A.2
  • 20
    • 0033005974 scopus 로고    scopus 로고
    • Regulation of cortical structure by the ezrin-radixin-moesin protein family
    • Bretscher A. Regulation of cortical structure by the ezrin-radixin-moesin protein family. Curr. Opin. Cell Biol. 11 (1999) 109-116
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 109-116
    • Bretscher, A.1
  • 21
    • 0032940071 scopus 로고    scopus 로고
    • ERM proteins in cell adhesion and membrane dynamics
    • Mangeat P., Roy C., and Martin M. ERM proteins in cell adhesion and membrane dynamics. Trends Cell Biol. 9 (1999) 187-192
    • (1999) Trends Cell Biol. , vol.9 , pp. 187-192
    • Mangeat, P.1    Roy, C.2    Martin, M.3
  • 22
    • 19644363077 scopus 로고    scopus 로고
    • Ezrin oligomers are the membrane-bound dormant form in gastric parietal cells
    • Zhu L., Liu Y., and Forte J.G. Ezrin oligomers are the membrane-bound dormant form in gastric parietal cells. Am. J. Physiol. Cell Physiol. 288 (2005) C1242-C1254
    • (2005) Am. J. Physiol. Cell Physiol. , vol.288
    • Zhu, L.1    Liu, Y.2    Forte, J.G.3
  • 24
    • 0033677862 scopus 로고    scopus 로고
    • The actin cytoskeleton and plasma membrane connection: PtdIns(4,5)P(2) influences cytoskeletal protein activity at the plasma membrane
    • Sechi A.S., and Wehland J. The actin cytoskeleton and plasma membrane connection: PtdIns(4,5)P(2) influences cytoskeletal protein activity at the plasma membrane. J. Cell Sci. 113 (2000) 3685-3695
    • (2000) J. Cell Sci. , vol.113 , pp. 3685-3695
    • Sechi, A.S.1    Wehland, J.2
  • 25
    • 0024990759 scopus 로고
    • Sequence and domain structure of talin
    • Rees D., Ades S., Singer S., and Hynes R. Sequence and domain structure of talin. Nature 347 (1990) 685-689
    • (1990) Nature , vol.347 , pp. 685-689
    • Rees, D.1    Ades, S.2    Singer, S.3    Hynes, R.4
  • 27
    • 0034724536 scopus 로고    scopus 로고
    • Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain
    • Pearson M.A., Reczek D., Bretscher A., and Karplus P.A. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell 101 (2000) 259-270
    • (2000) Cell , vol.101 , pp. 259-270
    • Pearson, M.A.1    Reczek, D.2    Bretscher, A.3    Karplus, P.A.4
  • 28
    • 0029062869 scopus 로고
    • Interaction of the 47-kDa talin fragment and the 32-kDa vinculin fragment with acidic phospholipids: a computer analysis
    • Tempel M., Goldmann H., Isenberg G., and Sackmann E. Interaction of the 47-kDa talin fragment and the 32-kDa vinculin fragment with acidic phospholipids: a computer analysis. Biophys. J. 69 (1995) 228-241
    • (1995) Biophys. J. , vol.69 , pp. 228-241
    • Tempel, M.1    Goldmann, H.2    Isenberg, G.3    Sackmann, E.4
  • 29
    • 0034283003 scopus 로고    scopus 로고
    • Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain
    • Hamada K., Shimizu T., Matsui T., Tsukita Sh., Tsukita S., and Hakoshima T. Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J. 19 (2000) 4449-4462
    • (2000) EMBO J. , vol.19 , pp. 4449-4462
    • Hamada, K.1    Shimizu, T.2    Matsui, T.3    Tsukita, Sh.4    Tsukita, S.5    Hakoshima, T.6
  • 30
    • 0029609581 scopus 로고
    • Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ezrin-radixin-moesin association domains
    • Bretscher A., Gary R., and Berryman M. Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ezrin-radixin-moesin association domains. Biochemistry 34 (1995) 16830-16837
    • (1995) Biochemistry , vol.34 , pp. 16830-16837
    • Bretscher, A.1    Gary, R.2    Berryman, M.3
  • 31
    • 0032053708 scopus 로고    scopus 로고
    • The synthesis and cellular roles of phosphatidylinositol 4,5-bisphosphate
    • Toker A. The synthesis and cellular roles of phosphatidylinositol 4,5-bisphosphate. Curr. Opin. Cell Biol. 10 (1998) 254-261
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 254-261
    • Toker, A.1
  • 32
    • 0034194271 scopus 로고    scopus 로고
    • Membrane cytoskeleton: PIP(2) pulls the strings
    • Nebl T., Oh S.W., and Luna E.J. Membrane cytoskeleton: PIP(2) pulls the strings. Curr. Biol. 10 (2000) R351-R354
    • (2000) Curr. Biol. , vol.10
    • Nebl, T.1    Oh, S.W.2    Luna, E.J.3
  • 33
    • 0035424240 scopus 로고    scopus 로고
    • PI(4,5)P(2) regulation of surface membrane traffic
    • Martin T.F. PI(4,5)P(2) regulation of surface membrane traffic. Curr. Opin. Cell Biol. 13 (2001) 493-499
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 493-499
    • Martin, T.F.1
  • 34
    • 0035975965 scopus 로고    scopus 로고
    • Modular phosphoinositide-binding domains: their role in signalling and membrane trafficking
    • Cullen P.J., Cozier G.E., Banting G., and Mellor H. Modular phosphoinositide-binding domains: their role in signalling and membrane trafficking. Curr. Biol. 11 (2001) R882-R893
    • (2001) Curr. Biol. , vol.11
    • Cullen, P.J.1    Cozier, G.E.2    Banting, G.3    Mellor, H.4
  • 35
    • 0030592694 scopus 로고    scopus 로고
    • Probing phosphatidylinositolphosphates and adenosinenucleotides on talin nucleated actin polymerization
    • Isenberg G., Niggli V., Pieper U., Kaufmann S., and Goldmann W.H. Probing phosphatidylinositolphosphates and adenosinenucleotides on talin nucleated actin polymerization. FEBS Letters 397 (1996) 316-320
    • (1996) FEBS Letters , vol.397 , pp. 316-320
    • Isenberg, G.1    Niggli, V.2    Pieper, U.3    Kaufmann, S.4    Goldmann, W.H.5
  • 36
    • 0033521010 scopus 로고    scopus 로고
    • Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins
    • Tsukita S., and Yonemura S. Cortical actin organization: lessons from ERM (ezrin/radixin/moesin) proteins. J. Biol. Chem. 274 (1999) 34507-34510
    • (1999) J. Biol. Chem. , vol.274 , pp. 34507-34510
    • Tsukita, S.1    Yonemura, S.2
  • 37
    • 0043198069 scopus 로고    scopus 로고
    • Why do worms need cholesterol?
    • Kurzchalia T.V., and Ward S. Why do worms need cholesterol?. Nature Cell Biol. 5 (2003) 684-688
    • (2003) Nature Cell Biol. , vol.5 , pp. 684-688
    • Kurzchalia, T.V.1    Ward, S.2
  • 38
    • 33645786777 scopus 로고    scopus 로고
    • Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304
    • Kitano K., Yusa F., and Hakoshima T. Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304. Acta Crystallog. sect. F 62 (2006) 340-345
    • (2006) Acta Crystallog. sect. F , vol.62 , pp. 340-345
    • Kitano, K.1    Yusa, F.2    Hakoshima, T.3
  • 39
    • 41349122163 scopus 로고    scopus 로고
    • Theoretical analysis of opening-up vesicles with single and two holes
    • Article No. 011913
    • Umeda T., Suezaki Y., Takiguchi K., and Hotani H. Theoretical analysis of opening-up vesicles with single and two holes. Phys. Rev. E 71 (2005) Article No. 011913
    • (2005) Phys. Rev. E , vol.71
    • Umeda, T.1    Suezaki, Y.2    Takiguchi, K.3    Hotani, H.4
  • 40
    • 1442281096 scopus 로고    scopus 로고
    • Lipid membranes with free edges
    • article No. 061915
    • Tu Z.C., and Ou-Yang Z.C. Lipid membranes with free edges. Phys. Rev. E 68 (2003) article No. 061915
    • (2003) Phys. Rev. E , vol.68
    • Tu, Z.C.1    Ou-Yang, Z.C.2
  • 42
    • 14944339213 scopus 로고    scopus 로고
    • Plasmalemmal phosphatidylinositol-4,5-bisphosphate level regulates the releasable vesicle pool size in chromaffin cells
    • Milosevic I., Sorensen J.B., Lang T., Krauss M., Nagy G., Haucke V., Jahn R., and Neher E. Plasmalemmal phosphatidylinositol-4,5-bisphosphate level regulates the releasable vesicle pool size in chromaffin cells. J. Neurosci. 25 (2005) 2557-2565
    • (2005) J. Neurosci. , vol.25 , pp. 2557-2565
    • Milosevic, I.1    Sorensen, J.B.2    Lang, T.3    Krauss, M.4    Nagy, G.5    Haucke, V.6    Jahn, R.7    Neher, E.8
  • 43
    • 0035881755 scopus 로고    scopus 로고
    • Actin cytoskeleton regulation through modulation of PI(4,5)P(2) rafts
    • Caroni P. Actin cytoskeleton regulation through modulation of PI(4,5)P(2) rafts. EMBO J. 20 (2001) 4332-4336
    • (2001) EMBO J. , vol.20 , pp. 4332-4336
    • Caroni, P.1
  • 44
    • 0035424240 scopus 로고    scopus 로고
    • PI(4,5)P(2) regulation of surface membrane traffic
    • Martin T.F. PI(4,5)P(2) regulation of surface membrane traffic. Curr. Opin. Cell Biol. 13 (2001) 493-499
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 493-499
    • Martin, T.F.1
  • 45
    • 0037376772 scopus 로고    scopus 로고
    • A role for moesin in polarity
    • Miller K.G. A role for moesin in polarity. Trends Cell Biol. 13 (2003) 165-168
    • (2003) Trends Cell Biol. , vol.13 , pp. 165-168
    • Miller, K.G.1
  • 47
    • 0019332747 scopus 로고
    • Associations of erythrocyte membrane proteins. Binding of purified bands 2.1 and 4.1 to spectrin
    • Tyler J.M., Reinhardt B.N., and Branton D. Associations of erythrocyte membrane proteins. Binding of purified bands 2.1 and 4.1 to spectrin. J. Biol. Chem. 255 (1980) 7034-7039
    • (1980) J. Biol. Chem. , vol.255 , pp. 7034-7039
    • Tyler, J.M.1    Reinhardt, B.N.2    Branton, D.3
  • 48
    • 0021891875 scopus 로고
    • The membrane skeleton of human erythrocytes and its implications for more complex cells
    • Bennett V.A. The membrane skeleton of human erythrocytes and its implications for more complex cells. Annu. Rev. Biochem. 54 (1985) 273-304
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 273-304
    • Bennett, V.A.1
  • 49
    • 0022168490 scopus 로고
    • Stabilizing infrastructure of cell membranes
    • Marchesi V.T. Stabilizing infrastructure of cell membranes. Annu. Rev. Cell Biol. 1 (1985) 531-561
    • (1985) Annu. Rev. Cell Biol. , vol.1 , pp. 531-561
    • Marchesi, V.T.1
  • 50
    • 0024542907 scopus 로고
    • Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor
    • Bretscher A. Rapid phosphorylation and reorganization of ezrin and spectrin accompany morphological changes induced in A-431 cells by epidermal growth factor. J. Cell Biol. 108 (1989) 921-930
    • (1989) J. Cell Biol. , vol.108 , pp. 921-930
    • Bretscher, A.1
  • 51
    • 0024582302 scopus 로고
    • The effects of dephosphorylation on the structure of the projections of neurofilament
    • Hisanaga S., and Hirokawa N. The effects of dephosphorylation on the structure of the projections of neurofilament. J. Neurosci. 9 (1989) 959-966
    • (1989) J. Neurosci. , vol.9 , pp. 959-966
    • Hisanaga, S.1    Hirokawa, N.2
  • 52
    • 0027275994 scopus 로고
    • Moesin, like ezrin, colocalizes with actin in the cortical cytoskeleton in cultured cells, but its expression is more variable
    • Franck Z., Gary R., and Bretscher A. Moesin, like ezrin, colocalizes with actin in the cortical cytoskeleton in cultured cells, but its expression is more variable. J. Cell Sci. 105 (1993) 219-231
    • (1993) J. Cell Sci. , vol.105 , pp. 219-231
    • Franck, Z.1    Gary, R.2    Bretscher, A.3
  • 53
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 54
    • 0033605879 scopus 로고    scopus 로고
    • Morphogenesis of liposomes encapsulating actin depends on the type of actin-crosslinking
    • Honda M., Takiguchi K., Ishikawa S., and Hotani H. Morphogenesis of liposomes encapsulating actin depends on the type of actin-crosslinking. J. Mol. Biol. 287 (1999) 293-300
    • (1999) J. Mol. Biol. , vol.287 , pp. 293-300
    • Honda, M.1    Takiguchi, K.2    Ishikawa, S.3    Hotani, H.4
  • 55
    • 16244390882 scopus 로고    scopus 로고
    • Formation and maintenance of tubular membrane projections require mechanical force, but their elongation and shortening do not require additional force
    • Inaba T., Ishijima A., Honda M., Nomura F., Takiguchi K., and Hotani H. Formation and maintenance of tubular membrane projections require mechanical force, but their elongation and shortening do not require additional force. J. Mol. Biol. 348 (2005) 325-333
    • (2005) J. Mol. Biol. , vol.348 , pp. 325-333
    • Inaba, T.1    Ishijima, A.2    Honda, M.3    Nomura, F.4    Takiguchi, K.5    Hotani, H.6


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