메뉴 건너뛰기




Volumn 47, Issue 3, 2000, Pages 565-578

Interaction of membrane skeletal proteins with membrane lipid domain

Author keywords

Cytoskeleton; Membrane lipid domains; Membrane skeleton; Non erythroid cells; Red blood cells

Indexed keywords

ANKYRIN; CYTOSKELETON PROTEIN; ERYTHROCYTE BAND 4.1 PROTEIN; MEMBRANE LIPID; MEMBRANE PROTEIN; NEURONAL MEMBRANE CYTOSKELETAL PROTEIN 4.1; NEUROPEPTIDE; PHOSPHOLIPID; SPECTRIN;

EID: 0034569607     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.2000_3979     Document Type: Review
Times cited : (29)

References (102)
  • 1
    • 0028263839 scopus 로고
    • Mechanochemical properties of the red cell membrane in relation to molecular structure and genetic defects
    • Mohandas, N. & Evans, E. (1994) Mechanochemical properties of the red cell membrane in relation to molecular structure and genetic defects. Annu. Rev. Biophys. Biomol. Struct. 23, 787-818.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 787-818
    • Mohandas, N.1    Evans, E.2
  • 2
    • 0022615147 scopus 로고
    • The human erythrocyte membrane skeleton may be an ionic gel. I. Membrane mechanochemical properties
    • Stokke, B.T., Mikkelsen, A. & Elgsaeter, A. (1986) The human erythrocyte membrane skeleton may be an ionic gel. I. Membrane mechanochemical properties. Eur. Biophys. J. 13, 203-218.
    • (1986) Eur. Biophys. J. , vol.13 , pp. 203-218
    • Stokke, B.T.1    Mikkelsen, A.2    Elgsaeter, A.3
  • 7
    • 0022344550 scopus 로고
    • Visualization of the protein associations in the erythrocyte membrane skeleton
    • Byers, T. & Branton, D. (1985) Visualization of the protein associations in the erythrocyte membrane skeleton. Proc. Natl. Acad. Sci. U.S.A. 82, 6153-6157.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 6153-6157
    • Byers, T.1    Branton, D.2
  • 8
    • 0023150141 scopus 로고
    • Visualization of the hexagonal lattice in the erythrocyte membrane skeleton
    • Liu, S.-C., Derick, L.H. & Palek, J. (1987) Visualization of the hexagonal lattice in the erythrocyte membrane skeleton. J. Cell. Biol. 104, 527-536.
    • (1987) J. Cell. Biol. , vol.104 , pp. 527-536
    • Liu, S.-C.1    Derick, L.H.2    Palek, J.3
  • 9
    • 0018075434 scopus 로고
    • Triton shells of intact erythrocytes
    • Sheetz, M.P. & Sawyer, P. (1978) Triton shells of intact erythrocytes. J. Supramol. Structure 8, 399-412.
    • (1978) J. Supramol. Structure , vol.8 , pp. 399-412
    • Sheetz, M.P.1    Sawyer, P.2
  • 11
    • 0346761425 scopus 로고
    • Syndeins: Spectrin-binding protein(s) from the human erythrocyte membrane
    • Yu, J. & Goodman, S.R. (1979) Syndeins: Spectrin-binding protein(s) from the human erythrocyte membrane. Proc. Natl. Acad. Sci. U.S.A. 76, 2340-2344.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 2340-2344
    • Yu, J.1    Goodman, S.R.2
  • 12
    • 0018759538 scopus 로고
    • The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membrane
    • Bennett, V. & Stenbuck, P. (1979) The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membrane. Nature 280, 468-473.
    • (1979) Nature , vol.280 , pp. 468-473
    • Bennett, V.1    Stenbuck, P.2
  • 13
    • 0019321291 scopus 로고
    • Association between ankyrin and the cytoplasmic domains of band 3 isolated from human erythrocyte membrane
    • Bennett, V. & Stenbuck, P. (1980) Association between ankyrin and the cytoplasmic domains of band 3 isolated from human erythrocyte membrane. J. Biol. Chem. 255, 6424-6432.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6424-6432
    • Bennett, V.1    Stenbuck, P.2
  • 14
    • 0027525199 scopus 로고
    • Membrane attachment sites for the membrane cytoskeletal protein 4.1 of the red blood cell
    • Pinder, J.C., Chung, A., Reid, M.E. & Gratzer, W.B. (1993) Membrane attachment sites for the membrane cytoskeletal protein 4.1 of the red blood cell. Blood 82, 3482-3488.
    • (1993) Blood , vol.82 , pp. 3482-3488
    • Pinder, J.C.1    Chung, A.2    Reid, M.E.3    Gratzer, W.B.4
  • 15
    • 0028237630 scopus 로고
    • In vitro binding studies suggest a membrane-associated complex between erythroid p55, protein 4.1, and glycophorin C
    • Marfatia, S.M., Lue, R.A., Branton, D. & Chishti, A.H. (1994) In vitro binding studies suggest a membrane-associated complex between erythroid p55, protein 4.1, and glycophorin C. J. Biol. Chem. 269, 8631-8634.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8631-8634
    • Marfatia, S.M.1    Lue, R.A.2    Branton, D.3    Chishti, A.H.4
  • 17
    • 0028679744 scopus 로고
    • Actin-binding proteins 1: Spectrin superfamily
    • Hartwig, J.H. (1994) Actin-binding proteins 1: Spectrin superfamily. Protein Profile 1, 706-778.
    • (1994) Protein Profile , vol.1 , pp. 706-778
    • Hartwig, J.H.1
  • 18
    • 0014938422 scopus 로고
    • Interaction of erythrocyte-membrane protein, spectrin, with model membrane systems
    • Sweet, C. & Zull, J.E. (1970) Interaction of erythrocyte-membrane protein, spectrin, with model membrane systems. Biochem. Biophys. Res. Commun. 41, 135-141.
    • (1970) Biochem. Biophys. Res. Commun. , vol.41 , pp. 135-141
    • Sweet, C.1    Zull, J.E.2
  • 21
    • 0026545859 scopus 로고
    • Fluorescence quenching of spectrin and other red cell membrane cytoskeletal proteins. Relation to hydrophobic binding sites
    • Kahana, E., Pinder, J.C., Smith, K. & Gratzer, W.B. (1992) Fluorescence quenching of spectrin and other red cell membrane cytoskeletal proteins. Relation to hydrophobic binding sites. Biochem. J. 282, 75-80.
    • (1992) Biochem. J. , vol.282 , pp. 75-80
    • Kahana, E.1    Pinder, J.C.2    Smith, K.3    Gratzer, W.B.4
  • 22
    • 0038885879 scopus 로고
    • Interaction of erythrocyte spectrin with amphipathic coumpounds
    • Sikorski, A.F., Michalak, K., Bobrowska, M. & Kozubek, A. (1987) Interaction of erythrocyte spectrin with amphipathic coumpounds. Stud. Biophys. 121, 20-26.
    • (1987) Stud. Biophys. , vol.121 , pp. 20-26
    • Sikorski, A.F.1    Michalak, K.2    Bobrowska, M.3    Kozubek, A.4
  • 24
    • 0023682864 scopus 로고
    • Interaction of spectrin with hydrophobic agaroses
    • Sikorski, A.F. (1988) Interaction of spectrin with hydrophobic agaroses. Acta Biochim. Polon. 35, 19-27.
    • (1988) Acta Biochim. Polon. , vol.35 , pp. 19-27
    • Sikorski, A.F.1
  • 25
    • 0039478610 scopus 로고
    • Interactin of spectrin with membrane intrinsic domain
    • Haest, C.W.M. (1981) Interactin of spectrin with membrane intrinsic domain. Biochim. Biophys. Acta 694, 331-352.
    • (1981) Biochim. Biophys. Acta , vol.694 , pp. 331-352
    • Haest, C.W.M.1
  • 26
    • 0022345549 scopus 로고
    • Labelling of erythrocyte spectrin 'in situ' with phenylisothiocyanate
    • Sikorski, A.F. & Kuczek, M. (1985) Labelling of erythrocyte spectrin 'in situ' with phenylisothiocyanate. Biochim. Biophys. Acta 820, 147-153.
    • (1985) Biochim. Biophys. Acta , vol.820 , pp. 147-153
    • Sikorski, A.F.1    Kuczek, M.2
  • 27
    • 0023100809 scopus 로고
    • Hydrophobic labelling of spectrin in erythrocytes using arylisothiocyanates
    • Sikorski, A.F., Kuczek, M., Nyczka, Z. & Kubiak, Z.J. (1987) Hydrophobic labelling of spectrin in erythrocytes using arylisothiocyanates. Biomed. Biochim. Acta 46, 76-82.
    • (1987) Biomed. Biochim. Acta , vol.46 , pp. 76-82
    • Sikorski, A.F.1    Kuczek, M.2    Nyczka, Z.3    Kubiak, Z.J.4
  • 28
    • 0039478558 scopus 로고
    • The effect of spectrin on the erythrocyte membrane fluidity
    • Sikorski, A.F. & Jezierski, A. (1987) The effect of spectrin on the erythrocyte membrane fluidity. Studia Biophys. 113, 193-201.
    • (1987) Studia Biophys. , vol.113 , pp. 193-201
    • Sikorski, A.F.1    Jezierski, A.2
  • 29
    • 0027585160 scopus 로고
    • Interaction of bovine erythrocyte spectrin with aminophospholipid liposomes
    • Michalak, K., Bobrowska, M. & Sikorski, A.F. (1993) Interaction of bovine erythrocyte spectrin with aminophospholipid liposomes. Gen. Physiol. Biophys. 12, 163-170.
    • (1993) Gen. Physiol. Biophys. , vol.12 , pp. 163-170
    • Michalak, K.1    Bobrowska, M.2    Sikorski, A.F.3
  • 30
    • 0018404318 scopus 로고
    • The interaction of spectrin-actin and synthetic phospholipids. II. The interaction with phosphatidylserine
    • Mombers, C., van Dijck, P., van Deenen, L.L.M., deGier, J. & Verkleij, A. (1979) The interaction of spectrin-actin and synthetic phospholipids. II. The interaction with phosphatidylserine. Biochim. Biophys. Acta 551, 271-281.
    • (1979) Biochim. Biophys. Acta , vol.551 , pp. 271-281
    • Mombers, C.1    Van Dijck, P.2    Van Deenen, L.L.M.3    DeGier, J.4    Verkleij, A.5
  • 32
    • 0039478557 scopus 로고
    • Interactions of the isolated spectrin peptides (bands 1 and 2) with phosholipid monolayers
    • (Peeters, H., ed.) Pergamon Press, Oxford, New York, Toronto, Paris, Frankfurt, Sydney
    • th Colloquium (Peeters, H., ed.) Pergamon Press, Oxford, New York, Toronto, Paris, Frankfurt, Sydney.
    • (1981) th Colloquium
    • Schubert, D.1    Herbst, F.2    Marie, H.3    Rudloff, V.4
  • 33
    • 2442752589 scopus 로고    scopus 로고
    • Interaction of spectrin with phospholipids is inhibited by isolated erythrocyte ankyrin
    • Białkowska, K., Leśniewski, J. Nietubyć, M. & Sikorski, A.F. (1999) Interaction of spectrin with phospholipids is inhibited by isolated erythrocyte ankyrin. Cell. Mol. Biol. Lett. 4, 203-218.
    • (1999) Cell. Mol. Biol. Lett. , vol.4 , pp. 203-218
    • Białkowska, K.1    Leśniewski, J.2    Nietubyć, M.3    Sikorski, A.F.4
  • 34
    • 0023270477 scopus 로고
    • Electrostatic coupling of spectrin dimers to phosphatidylserine containing lipid lamellae
    • Maksymiw, R., Sui, S., Gaub, H. & Sackmann, E. (1987) Electrostatic coupling of spectrin dimers to phosphatidylserine containing lipid lamellae. Biochemistry 26, 2983-2990.
    • (1987) Biochemistry , vol.26 , pp. 2983-2990
    • Maksymiw, R.1    Sui, S.2    Gaub, H.3    Sackmann, E.4
  • 35
    • 0022998463 scopus 로고
    • Ultrastructural studies of the interaction of spectrin with phosphatidylserine liposomes
    • Cohen, A.M., Liu, S.C., Derick, L.H. & Palek, J. (1986) Ultrastructural studies of the interaction of spectrin with phosphatidylserine liposomes. Blood 68, 920-926.
    • (1986) Blood , vol.68 , pp. 920-926
    • Cohen, A.M.1    Liu, S.C.2    Derick, L.H.3    Palek, J.4
  • 36
    • 0005458823 scopus 로고    scopus 로고
    • Regulation of the mechanical properties of the red cell membrane by protein-protein and protein-lipid interactions
    • DeWolf, C., McCauley, P. & Pinder, J.C. (1996) Regulation of the mechanical properties of the red cell membrane by protein-protein and protein-lipid interactions. Cell. Mol. Biol. Lett. 1, 89-96.
    • (1996) Cell. Mol. Biol. Lett. , vol.1 , pp. 89-96
    • DeWolf, C.1    McCauley, P.2    Pinder, J.C.3
  • 37
    • 0023642603 scopus 로고
    • Interaction of spectrin with phospholipids. Quenching of the intrinsic fluorescence by phospholipid suspensions
    • Sikorski, A.F., Michalak, K. & Bobrowska, M. (1987) Interaction of spectrin with phospholipids. Quenching of the intrinsic fluorescence by phospholipid suspensions. Biochim. Biophys. Acta 904, 55-60.
    • (1987) Biochim. Biophys. Acta , vol.904 , pp. 55-60
    • Sikorski, A.F.1    Michalak, K.2    Bobrowska, M.3
  • 38
    • 0028215013 scopus 로고
    • Ankyrin inhibits binding of erythrocyte spectrin to phospholipid vesicles
    • Białkowska, K., Zembroń, A. & Sikorski, A.F. (1994) Ankyrin inhibits binding of erythrocyte spectrin to phospholipid vesicles. Biochim. Biophys. Acta 1191, 21-26.
    • (1994) Biochim. Biophys. Acta , vol.1191 , pp. 21-26
    • Białkowska, K.1    Zembroń, A.2    Sikorski, A.F.3
  • 39
    • 0034213003 scopus 로고    scopus 로고
    • Investigations of spectrin-lipid interactions using fluoresceinphosphatidylethanolamine as a membrane probe
    • O'Toole, P.J., Morrison, I.E.G. & Cherry, R.J. (2000) Investigations of spectrin-lipid interactions using fluoresceinphosphatidylethanolamine as a membrane probe. Biochim. Biophys. Acta 1466, 39-46.
    • (2000) Biochim. Biophys. Acta , vol.1466 , pp. 39-46
    • O'Toole, P.J.1    Morrison, I.E.G.2    Cherry, R.J.3
  • 40
    • 0025647431 scopus 로고
    • Investigation of spectrin binding to phospholipid vesicles with the use of isoindole fluorescent probe. Thermal properties of bound and unbound protein
    • Michalak, K., Bobrowska, M. & Sikorski, A.F. (1990) Investigation of spectrin binding to phospholipid vesicles with the use of isoindole fluorescent probe. Thermal properties of bound and unbound protein. Gen. Physiol. Biophys. 9, 615-624.
    • (1990) Gen. Physiol. Biophys. , vol.9 , pp. 615-624
    • Michalak, K.1    Bobrowska, M.2    Sikorski, A.F.3
  • 41
    • 0024244139 scopus 로고
    • Proteolysis of spectrin in the presence of phospholipid suspensions with trypsin and pronase
    • Sikorski, A.F., Kozubek, A. & Szopa, J. (1988) Proteolysis of spectrin in the presence of phospholipid suspensions with trypsin and pronase. Acta Biochim. Polon. 35, 71-82.
    • (1988) Acta Biochim. Polon. , vol.35 , pp. 71-82
    • Sikorski, A.F.1    Kozubek, A.2    Szopa, J.3
  • 44
    • 0022629302 scopus 로고
    • Immunofluorescent patterns in lymphocyte cell lines
    • Pauly, J.R., Bankert, R.B. & Repasky, E.A. (1986) Immunofluorescent patterns in lymphocyte cell lines. J. Immunol. 136, 246-253.
    • (1986) J. Immunol. , vol.136 , pp. 246-253
    • Pauly, J.R.1    Bankert, R.B.2    Repasky, E.A.3
  • 45
    • 0026770096 scopus 로고
    • Relationship between membrane lipid mobility and spectrin distribution in lymphocytes
    • Langner, M., Repasky, E.A. & Hui, S.-W. (1992) Relationship between membrane lipid mobility and spectrin distribution in lymphocytes. FEBS Lett. 305, 197-205.
    • (1992) FEBS Lett. , vol.305 , pp. 197-205
    • Langner, M.1    Repasky, E.A.2    Hui, S.-W.3
  • 47
    • 0019971525 scopus 로고
    • Brain spectrin, a membrane associated protein related in structure and function to erythrocyte spectrin
    • Bennett, V., Davis, J. & Fowler, W.E. (1982) Brain spectrin, a membrane associated protein related in structure and function to erythrocyte spectrin. Nature 299, 126-131.
    • (1982) Nature , vol.299 , pp. 126-131
    • Bennett, V.1    Davis, J.2    Fowler, W.E.3
  • 48
    • 0027301038 scopus 로고
    • Erythroid and nonerythroid spectrins
    • Winkelmann, J. & Forget, B. (1993) Erythroid and nonerythroid spectrins. Blood 81, 3173-3185.
    • (1993) Blood , vol.81 , pp. 3173-3185
    • Winkelmann, J.1    Forget, B.2
  • 50
    • 0025254086 scopus 로고
    • Generation of diversity in nonerythroid spectrins
    • Moon, R.T. & McMahon, A. (1990) Generation of diversity in nonerythroid spectrins. J. Biol. Chem. 265, 4427-4433.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4427-4433
    • Moon, R.T.1    McMahon, A.2
  • 52
    • 0026732691 scopus 로고
    • Characterization of human brain cDNA encoding the general isoform of β-spectrin
    • Hu, R., Watanabe, M. & Bennett, V. (1992) Characterization of human brain cDNA encoding the general isoform of β-spectrin. J. Biol. Chem. 264, 18715-18722.
    • (1992) J. Biol. Chem. , vol.264 , pp. 18715-18722
    • Hu, R.1    Watanabe, M.2    Bennett, V.3
  • 53
    • 0021272595 scopus 로고
    • Erythrocyte spectrin is comprised of many homologous triple helical segments
    • Speicher, D.W. & Marchesi, V.T. (1984) Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature 311, 177-180.
    • (1984) Nature , vol.311 , pp. 177-180
    • Speicher, D.W.1    Marchesi, V.T.2
  • 54
    • 0023427237 scopus 로고
    • The 180 kD component of the neural cell adhesion molecule N-CAM is involved in cell-cell contacts and cytoskeleton-membrane interactions
    • Pollerberg, G.E., Burridge, K., Krebs, K.E., Goodman, S.R. & Schachner, M. (1987) The 180 kD component of the neural cell adhesion molecule N-CAM is involved in cell-cell contacts and cytoskeleton-membrane interactions. Cell Tissue Res. 250, 227-236.
    • (1987) Cell Tissue Res. , vol.250 , pp. 227-236
    • Pollerberg, G.E.1    Burridge, K.2    Krebs, K.E.3    Goodman, S.R.4    Schachner, M.5
  • 55
    • 0032980637 scopus 로고    scopus 로고
    • Immunolocalization of the fodrin, E-cadherin, and beta-catenin adhesion complex in infiltrating ductal carcinoma of the breast-comparison with an in vitro model
    • Somunen, R.T., Leong, A.S., Vaaranieni, J.P., Fernando, S.S. & Eskalinen, S.M. (1999) Immunolocalization of the fodrin, E-cadherin, and beta-catenin adhesion complex in infiltrating ductal carcinoma of the breast-comparison with an in vitro model. J. Pathol. 187, 416-423.
    • (1999) J. Pathol. , vol.187 , pp. 416-423
    • Somunen, R.T.1    Leong, A.S.2    Vaaranieni, J.P.3    Fernando, S.S.4    Eskalinen, S.M.5
  • 56
    • 0025602515 scopus 로고
    • Association of brain spectrin isoforms with microtubules
    • Riederer, B.M. & Goodman, S.R. (1990) Association of brain spectrin isoforms with microtubules. FEBS Lett. 277, 49-52.
    • (1990) FEBS Lett. , vol.277 , pp. 49-52
    • Riederer, B.M.1    Goodman, S.R.2
  • 57
    • 0026524937 scopus 로고
    • Actin and neurofilament binding domain of brain spectrin β subunit
    • Frappier, T., Derancourt, J. & Pradel, L. (1992) Actin and neurofilament binding domain of brain spectrin β subunit. Eur. J. Biochem. 205, 85-91.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 85-91
    • Frappier, T.1    Derancourt, J.2    Pradel, L.3
  • 58
    • 0025754337 scopus 로고
    • Interaction of domains of neurofilament light chain and spectrin
    • Frapier, T., Stetzkowski Marden, F. & Pradel, L. (1991) Interaction of domains of neurofilament light chain and spectrin. Biochem. J. 275, 521-527.
    • (1991) Biochem. J. , vol.275 , pp. 521-527
    • Frapier, T.1    Stetzkowski Marden, F.2    Pradel, L.3
  • 59
    • 0023757432 scopus 로고
    • The cytoskeleton as a barrier to exocytosis in secretory cells
    • Aunis, D. & Bader, M.-F. (1988) The cytoskeleton as a barrier to exocytosis in secretory cells. J. Exp. Biol. 139, 253-266.
    • (1988) J. Exp. Biol. , vol.139 , pp. 253-266
    • Aunis, D.1    Bader, M.-F.2
  • 60
    • 0024002576 scopus 로고
    • The organization of the cytoplasm at the presynaptic active zone of a central nervous system synapse
    • Landis, D.M., Hall, A.K., Weinstein, L.A. & Reese, T.S. (1988) The organization of the cytoplasm at the presynaptic active zone of a central nervous system synapse. Neuron 1, 201-209.
    • (1988) Neuron , vol.1 , pp. 201-209
    • Landis, D.M.1    Hall, A.K.2    Weinstein, L.A.3    Reese, T.S.4
  • 61
    • 0025807554 scopus 로고
    • Synapsin I mediated interaction of brain spectrin with small synaptic vesicles
    • Sikorski, A.F., Terlecki, G., Zagon, I.S. & Goodman, S.R. (1991) Synapsin I mediated interaction of brain spectrin with small synaptic vesicles. J. Cell Biol. 114, 313-318.
    • (1991) J. Cell Biol. , vol.114 , pp. 313-318
    • Sikorski, A.F.1    Terlecki, G.2    Zagon, I.S.3    Goodman, S.R.4
  • 62
    • 0025992234 scopus 로고
    • The effect of synapsin I phosphorylation upon binding synaptic vesicles to spectrin
    • Sikorski, A.F. & Goodman, S.R. (1991) The effect of synapsin I phosphorylation upon binding synaptic vesicles to spectrin. Brain Res. Bull. 27, 195-198.
    • (1991) Brain Res. Bull. , vol.27 , pp. 195-198
    • Sikorski, A.F.1    Goodman, S.R.2
  • 63
    • 0033621545 scopus 로고    scopus 로고
    • Spectrin (bSpIIS1) is an essential component of synaptic transmission
    • Sikorski, A.F., Sangerman, J., Goodman, S.R. & Critz, S.D. (2000) Spectrin (bSpIIS1) is an essential component of synaptic transmission. Brain Res. 852, 161-166.
    • (2000) Brain Res. , vol.852 , pp. 161-166
    • Sikorski, A.F.1    Sangerman, J.2    Goodman, S.R.3    Critz, S.D.4
  • 64
    • 0032577702 scopus 로고    scopus 로고
    • Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of associations of tyrosine kinases with the spectrin-based membrane skeleton
    • Ziemnicka-Kotula, D., Xu, J., Gu, H., Potempska, A., Kim, S., Jenkins, E.C., Trenkner, E. & Kotula, L. (1998) Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of associations of tyrosine kinases with the spectrin-based membrane skeleton. J. Biol. Chem. 273, 13681-13692.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13681-13692
    • Ziemnicka-Kotula, D.1    Xu, J.2    Gu, H.3    Potempska, A.4    Kim, S.5    Jenkins, E.C.6    Trenkner, E.7    Kotula, L.8
  • 65
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • De Matteis, M.A. & Morrow, J.S. (2000) Spectrin tethers and mesh in the biosynthetic pathway. J. Cell. Sci. 113, 2331-2343.
    • (2000) J. Cell. Sci. , vol.113 , pp. 2331-2343
    • De Matteis, M.A.1    Morrow, J.S.2
  • 66
    • 0028253918 scopus 로고
    • Brain spectrin interacts with phospholipids
    • Diakowski, W. & Sikorski, A.F. (1994) Brain spectrin interacts with phospholipids. Acta Biochim. Polon. 41, 153-154.
    • (1994) Acta Biochim. Polon. , vol.41 , pp. 153-154
    • Diakowski, W.1    Sikorski, A.F.2
  • 67
    • 0028784721 scopus 로고
    • Interaction of brain spectrin (fodrin) with phospholipids
    • Diakowski, W. & Sikorski, A.F. (1995) Interaction of brain spectrin (fodrin) with phospholipids. Biochemistry 34, 13252-13258.
    • (1995) Biochemistry , vol.34 , pp. 13252-13258
    • Diakowski, W.1    Sikorski, A.F.2
  • 68
    • 0033557901 scopus 로고    scopus 로고
    • Brain spectrin (fodrin) interacts with phospholipids as revealed by intrinsic fluorescence quenching and monolayer experiments
    • Diakowski, W., Prychidny, A., Świstak, M., Nietubyc, M., Białkowska, K., Szopa, J. & Sikorski, A.F. (1999) Brain spectrin (fodrin) interacts with phospholipids as revealed by intrinsic fluorescence quenching and monolayer experiments. Biochem. J. 338, 83-90.
    • (1999) Biochem. J. , vol.338 , pp. 83-90
    • Diakowski, W.1    Prychidny, A.2    Świstak, M.3    Nietubyc, M.4    Białkowska, K.5    Szopa, J.6    Sikorski, A.F.7
  • 70
    • 0027183541 scopus 로고
    • The PH domain. A comon piece in the structural patchwork of signaling proteins
    • Musacchio, A., Gibson, T., Rice., Thompson, J. & Saraste, M. (1993) The PH domain. A comon piece in the structural patchwork of signaling proteins. Trends Biochem. Sci. 18, 343-348.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 343-348
    • Musacchio, A.1    Gibson, T.2    Thompson, J.3    Saraste, M.4
  • 72
    • 0029563928 scopus 로고
    • The association of the C-terminal region of beta I sigma II spectrin to brain membranes is mediated by a PH domain, does not require membrane proteins and coincides with a inositol-1,4,5-trisphosphate binding site
    • Wang, D.-S. & Shaw, G. (1995) The association of the C-terminal region of beta I sigma II spectrin to brain membranes is mediated by a PH domain, does not require membrane proteins and coincides with a inositol-1,4,5-trisphosphate binding site. Biochem. Biophys. Res. Commun. 217, 608-615.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 608-615
    • Wang, D.-S.1    Shaw, G.2
  • 73
    • 0030583283 scopus 로고    scopus 로고
    • The pleckstrin homology domain is targeted to the plasma membrane in vivo
    • Wang, D.-S., Miller, R., Shaw, R. & Shaw, G. (1996) The pleckstrin homology domain is targeted to the plasma membrane in vivo. Biochem. Biophys. Res. Commun. 225, 420-426.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 420-426
    • Wang, D.-S.1    Miller, R.2    Shaw, R.3    Shaw, G.4
  • 74
    • 0022454882 scopus 로고
    • Brain spectrin (240/235) and brain spectrin(240235E): Two distinct subtypes with different localization within mammalian neural cells
    • Riederer, B.M., Zagon, I.S. & Goodman, S.R. (1986) Brain spectrin (240/235) and brain spectrin(240235E): Two distinct subtypes with different localization within mammalian neural cells. J. Cell Biol. 102, 2088-2097.
    • (1986) J. Cell Biol. , vol.102 , pp. 2088-2097
    • Riederer, B.M.1    Zagon, I.S.2    Goodman, S.R.3
  • 77
    • 0032400833 scopus 로고    scopus 로고
    • Characterization of multiple isoforms of protein 4.1R expressed during erythroid terminal differentiation
    • Gascard, P., Lee, G., Coulombel, L., Auffray, I., Lum, M., Parra, M., Conboy, J.G., Mohandas, N. & Chasis, J.A. (1998) Characterization of multiple isoforms of protein 4.1R expressed during erythroid terminal differentiation. Blood 92, 4404-4414.
    • (1998) Blood , vol.92 , pp. 4404-4414
    • Gascard, P.1    Lee, G.2    Coulombel, L.3    Auffray, I.4    Lum, M.5    Parra, M.6    Conboy, J.G.7    Mohandas, N.8    Chasis, J.A.9
  • 78
    • 0029162126 scopus 로고
    • Mechanochemistry of protein 4.1's spectrin-actin-binding domain: Ternary complex interactions, membrane binding, network integration, structural strengthening
    • Discher, D.E., Winardi, R., Schischmanoff, P.O., Parra, M., Conboy, J.G. & Mohandas, N. (1995) Mechanochemistry of protein 4.1's spectrin-actin-binding domain: Ternary complex interactions, membrane binding, network integration, structural strengthening. J. Cell Biol. 130, 897-907.
    • (1995) J. Cell Biol. , vol.130 , pp. 897-907
    • Discher, D.E.1    Winardi, R.2    Schischmanoff, P.O.3    Parra, M.4    Conboy, J.G.5    Mohandas, N.6
  • 79
    • 0028944110 scopus 로고
    • Identification of the membrane attachment sites for protein 4.1 in the human erythrocyte
    • Hemming, N.J., Anstee, D.J., Staricoff, M.A., Tanner, M.J., Mohandas, N. (1995) Identification of the membrane attachment sites for protein 4.1 in the human erythrocyte. J. Biol. Chem. 270, 5360-5366.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5360-5366
    • Hemming, N.J.1    Anstee, D.J.2    Staricoff, M.A.3    Tanner, M.J.4    Mohandas, N.5
  • 80
    • 0030763609 scopus 로고    scopus 로고
    • The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C. Analysis of the binding interface by in vitro mutagenesis
    • Marfatia, S.M., Morais-Cabral, J.H., Kim, A.C., Byron, O. & Chishti, A.H. (1997) The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C. Analysis of the binding interface by in vitro mutagenesis. J. Biol. Chem. 272, 24191-24197.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24191-24197
    • Marfatia, S.M.1    Morais-Cabral, J.H.2    Kim, A.C.3    Byron, O.4    Chishti, A.H.5
  • 81
    • 0021106576 scopus 로고
    • Interaction of a peripheral protein of the erythrocyte membrane, band 4.1, with phosphatidylserine-containing liposomes and erythrocyte inside-out vesicles
    • Sato, S.B. & Ohnishi, S. (1983) Interaction of a peripheral protein of the erythrocyte membrane, band 4.1, with phosphatidylserine-containing liposomes and erythrocyte inside-out vesicles. Eur. J. Biochem. 130, 19-25.
    • (1983) Eur. J. Biochem. , vol.130 , pp. 19-25
    • Sato, S.B.1    Ohnishi, S.2
  • 82
    • 0023901506 scopus 로고
    • Human erythrocyte protein 4.1 is a phosphatidylserine binding protein
    • Rybicki, A.C., Heath, R., Lubin, B. & Schwartz, R.S. (1988) Human erythrocyte protein 4.1 is a phosphatidylserine binding protein. J. Clin. Invest. 81, 255-260.
    • (1988) J. Clin. Invest. , vol.81 , pp. 255-260
    • Rybicki, A.C.1    Heath, R.2    Lubin, B.3    Schwartz, R.S.4
  • 83
    • 0023871492 scopus 로고
    • Identification of the protein 4.1 binding site to phosphatidylserine vesicles
    • Cohen, A.M., Liu, S.C., Lawler, J., Derick, L., Palek, J. (1988) Identification of the protein 4.1 binding site to phosphatidylserine vesicles. Biochemistry 27, 614-619.
    • (1988) Biochemistry , vol.27 , pp. 614-619
    • Cohen, A.M.1    Liu, S.C.2    Lawler, J.3    Derick, L.4    Palek, J.5
  • 84
    • 0023849572 scopus 로고
    • Interaction of erythrocyte protein 4.1 with phospholipids. A monolayer and liposome study
    • Shiffer, K.A., Goerke, J., Duzgunes, N., Fedor, J. & Shohet, S.B. (1988) Interaction of erythrocyte protein 4.1 with phospholipids. A monolayer and liposome study. Biochim. Biophys. Acta 937, 269-280.
    • (1988) Biochim. Biophys. Acta , vol.937 , pp. 269-280
    • Shiffer, K.A.1    Goerke, J.2    Duzgunes, N.3    Fedor, J.4    Shohet, S.B.5
  • 85
    • 0343488536 scopus 로고    scopus 로고
    • Cytoskeletal protein binding kinetics at planar phospholipid membranes
    • Mc Kiernan, A.E., MacDonald, R.I., MacDonald, R.C. & Axelrod, D. (1997) Cytoskeletal protein binding kinetics at planar phospholipid membranes. Biophys. J. 73, 1987-1998.
    • (1997) Biophys. J. , vol.73 , pp. 1987-1998
    • Mc Kiernan, A.E.1    MacDonald, R.I.2    MacDonald, R.C.3    Axelrod, D.4
  • 86
    • 0033497987 scopus 로고    scopus 로고
    • Physiological roles of axonal ankyrins in survival of premyelinated axons and localization of voltage-gated sodium channels
    • Bennett, V. & Lambert, S. (1999) Physiological roles of axonal ankyrins in survival of premyelinated axons and localization of voltage-gated sodium channels. J. Neurocytol. 28, 303-318.
    • (1999) J. Neurocytol. , vol.28 , pp. 303-318
    • Bennett, V.1    Lambert, S.2
  • 88
    • 0034659956 scopus 로고    scopus 로고
    • The L1-type cell adhesion molecule neuroglian influences the stability of neural ankyrin in the Drosophila embryo but not its axonal localization
    • Bouley, M., Tian, M.Z., Paisley, K., Shen, Y.C., Malhorta, J.D. & Hortsch, M. (2000) The L1-type cell adhesion molecule neuroglian influences the stability of neural ankyrin in the Drosophila embryo but not its axonal localization. J. Neurosci. 20, 4515-4523.
    • (2000) J. Neurosci. , vol.20 , pp. 4515-4523
    • Bouley, M.1    Tian, M.Z.2    Paisley, K.3    Shen, Y.C.4    Malhorta, J.D.5    Hortsch, M.6
  • 90
    • 0028252062 scopus 로고
    • Ankyrin shares binding site with phospholipids on erythrocyte spectrin
    • Białkowska, K., Zembroń, A. & Sikorski, A.F. (1994) Ankyrin shares binding site with phospholipids on erythrocyte spectrin. Acta Biochim. Polon. 41, 155-157.
    • (1994) Acta Biochim. Polon. , vol.41 , pp. 155-157
    • Białkowska, K.1    Zembroń, A.2    Sikorski, A.F.3
  • 91
    • 0039247377 scopus 로고    scopus 로고
    • Interactions of spectrins with membrane intrinsic domain
    • Sikorski, A.F. & Białkowska, K. (1996) Interactions of spectrins with membrane intrinsic domain. Cell. Mol. Biol. Lett. 1, 97-104.
    • (1996) Cell. Mol. Biol. Lett. , vol.1 , pp. 97-104
    • Sikorski, A.F.1    Białkowska, K.2
  • 92
    • 0024415776 scopus 로고
    • Biogenesis of the red blood cell membrane skeleton and the control of erythroid morphogenesis
    • Lazarides, E. & Woods, C. (1989) Biogenesis of the red blood cell membrane skeleton and the control of erythroid morphogenesis. Annu. Rev. Cell. Biol. 5, 427-452.
    • (1989) Annu. Rev. Cell. Biol. , vol.5 , pp. 427-452
    • Lazarides, E.1    Woods, C.2
  • 93
    • 0021704597 scopus 로고
    • Spectrin-deficient inherited hemolytic anemias in the mouse: Characterization by spectrin synthesis and mRNA activity in reticulocytes
    • Bodine, M., Birkenmeier, C.S. & Barker, J.E. (1984) Spectrin-deficient inherited hemolytic anemias in the mouse: characterization by spectrin synthesis and mRNA activity in reticulocytes. Cell 37, 721-728.
    • (1984) Cell , vol.37 , pp. 721-728
    • Bodine, M.1    Birkenmeier, C.S.2    Barker, J.E.3
  • 94
    • 0026785211 scopus 로고
    • Fetal compensation of the hemolytic anemia in mice homozygous for the normoblastosis (nb) mutation
    • Peters, L.I., Birkenmeier, C.S. & Barker, J.E. (1992) Fetal compensation of the hemolytic anemia in mice homozygous for the normoblastosis (nb) mutation. Blood 80, 2122-2127.
    • (1992) Blood , vol.80 , pp. 2122-2127
    • Peters, L.I.1    Birkenmeier, C.S.2    Barker, J.E.3
  • 95
    • 0030806488 scopus 로고    scopus 로고
    • Red cell membranes of ankyrin-deficient nb/nb mice lack band 3 tetramers but contain normal skeletons
    • Yi, S., Liu, S.-C., Derick, L.H., Murray, J., Barker, J.E., Cho, M.R., Palek, J. & Golan, D.E. (1997) Red cell membranes of ankyrin-deficient nb/nb mice lack band 3 tetramers but contain normal skeletons. Biochemistry 36, 9596-9604.
    • (1997) Biochemistry , vol.36 , pp. 9596-9604
    • Yi, S.1    Liu, S.-C.2    Derick, L.H.3    Murray, J.4    Barker, J.E.5    Cho, M.R.6    Palek, J.7    Golan, D.E.8
  • 96
    • 0022388397 scopus 로고
    • Phosphorylation of ankyrin decreases its affinity for spectrin tetramer
    • Lu, P., Soong, C.-J. & Tao, M. (1985) Phosphorylation of ankyrin decreases its affinity for spectrin tetramer. J. Biol. Chem. 260, 14958-14964.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14958-14964
    • Lu, P.1    Soong, C.-J.2    Tao, M.3
  • 97
    • 0029821217 scopus 로고    scopus 로고
    • Targeted disruption of the murine band 3 gene results in spherocytosis and severe hemolytic anemia despite a normal membrane skeleton
    • Southgate, C.D., Chishti, A.H., Mitchell, B., Yi, S.J. & Palek, J. (1996) Targeted disruption of the murine band 3 gene results in spherocytosis and severe hemolytic anemia despite a normal membrane skeleton. Nature Genet. 14, 227-230.
    • (1996) Nature Genet. , vol.14 , pp. 227-230
    • Southgate, C.D.1    Chishti, A.H.2    Mitchell, B.3    Yi, S.J.4    Palek, J.5
  • 99
    • 0034096197 scopus 로고    scopus 로고
    • 2+-independent calmodulin binding sites in erythrocyte protein 4.1. Implications for regulation of protein 4.1 interactions with transmembrane proteins
    • 2+-independent calmodulin binding sites in erythrocyte protein 4.1. Implications for regulation of protein 4.1 interactions with transmembrane proteins. J. Biol Chem. 275, 6360-6367.
    • (2000) J. Biol Chem. , vol.275 , pp. 6360-6367
    • Nunomura, W.1    Takakuwa, Y.2    Parra, M.3    Conboy, J.G.4    Mohandas, N.5
  • 100
    • 0027993053 scopus 로고
    • Golgi spectrin: Identification of an erythroid beta-spectrin homolog associated with the Golgi complex
    • Beck, K.A., Buchanan, J.A., Malhorta, V. & Nelson, W.J. (1994) Golgi spectrin: Identification of an erythroid beta-spectrin homolog associated with the Golgi complex. J. Cell Biol. 127, 707-723.
    • (1994) J. Cell Biol. , vol.127 , pp. 707-723
    • Beck, K.A.1    Buchanan, J.A.2    Malhorta, V.3    Nelson, W.J.4
  • 102
    • 0034647753 scopus 로고    scopus 로고
    • Identification of βV spectrin, a mammalian ortholog of Drosophila beta H spectrin
    • Stabach, P.R. & Morrow, J.S. (2000) Identification of βV spectrin, a mammalian ortholog of Drosophila beta H spectrin. J. Biol. Chem. 275, 21385-21395.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21385-21395
    • Stabach, P.R.1    Morrow, J.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.