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Volumn 148, Issue 2, 2007, Pages 124-138

Characterization of protein 4.1R in erythrocytes of zebrafish (Danio rerio): Unique binding properties with transmembrane proteins and calmodulin

Author keywords

Calmodulin; FERM domain; Membrane protein; Protein 4.1R; Zebrafish

Indexed keywords

CALMODULIN; GLYCOPHORIN C; MEMBRANE PROTEIN;

EID: 34547423260     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2007.05.001     Document Type: Article
Times cited : (15)

References (31)
  • 1
    • 0030463473 scopus 로고    scopus 로고
    • Modulation of band 3-ankyrin interaction by protein 4.1. Functional implications in regulation of erythrocyte membrane mechanical properties
    • An X.L., Takakuwa Y., Nunomura Y., Manno M., and Mohandas N. Modulation of band 3-ankyrin interaction by protein 4.1. Functional implications in regulation of erythrocyte membrane mechanical properties. J. Biol. Chem. 271 (1996) 33187-33191
    • (1996) J. Biol. Chem. , vol.271 , pp. 33187-33191
    • An, X.L.1    Takakuwa, Y.2    Nunomura, Y.3    Manno, M.4    Mohandas, N.5
  • 2
    • 0026801368 scopus 로고
    • Red blood cell glycophorins
    • Chasis J.A., and Mohandas N. Red blood cell glycophorins. Blood 80 (1992) 1869-1879
    • (1992) Blood , vol.80 , pp. 1869-1879
    • Chasis, J.A.1    Mohandas, N.2
  • 3
    • 34547395351 scopus 로고    scopus 로고
    • Chen, Y., Peng, J., Huang, C.-H., 2004. http://www.ncbi.nlm.nih.gov/entrez/viewer.fcgi?db=nucleotide_and_val=37928731.
  • 4
    • 0007170020 scopus 로고
    • Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells
    • Conboy J.G., Chan J., and Mohandas N. Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 9062-9065
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 9062-9065
    • Conboy, J.G.1    Chan, J.2    Mohandas, N.3
  • 5
    • 0027366806 scopus 로고
    • The resonant mirror: a novel optical biosensor for direct sensing of biomolecular interactions: Part I. Principle of operation and associated instrumentation
    • Cush R., Cronin J.M., Stewart W.J., Maule C.H., Molloy J., and Goddard N.J. The resonant mirror: a novel optical biosensor for direct sensing of biomolecular interactions: Part I. Principle of operation and associated instrumentation. Biosens. Bioelectron. 8 (1993) 347-353
    • (1993) Biosens. Bioelectron. , vol.8 , pp. 347-353
    • Cush, R.1    Cronin, J.M.2    Stewart, W.J.3    Maule, C.H.4    Molloy, J.5    Goddard, N.J.6
  • 6
    • 0032895115 scopus 로고    scopus 로고
    • Functional aspects of red cell antigens
    • Daniels G. Functional aspects of red cell antigens. Blood Rev. 13 (1999) 14-35
    • (1999) Blood Rev. , vol.13 , pp. 14-35
    • Daniels, G.1
  • 7
    • 0025320809 scopus 로고
    • Selective modulation of Band 4.1 binding to erythrocyte membranes by protein kinase C.J
    • Danilov Y.N., Fennell R., Ling E., and Cohen C.M. Selective modulation of Band 4.1 binding to erythrocyte membranes by protein kinase C.J. Biol. Chem. 265 (1990) 2556-2562
    • (1990) Biol. Chem. , vol.265 , pp. 2556-2562
    • Danilov, Y.N.1    Fennell, R.2    Ling, E.3    Cohen, C.M.4
  • 8
    • 0033953154 scopus 로고    scopus 로고
    • New insights into functions of erythroid proteins in nonerythroid cells
    • Gascard P., and Mohandas N. New insights into functions of erythroid proteins in nonerythroid cells. Curr. Opin. Hematol. 7 (2000) 123-129
    • (2000) Curr. Opin. Hematol. , vol.7 , pp. 123-129
    • Gascard, P.1    Mohandas, N.2
  • 9
    • 0032400833 scopus 로고    scopus 로고
    • Characterization ofmultiple 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., and Chasis J.A. Characterization ofmultiple isoforms of protein 4.1R expressed during erythroid terminal differentiation. Blood 92 (1998) 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
  • 10
    • 0033790239 scopus 로고    scopus 로고
    • Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization
    • Han B.G., Nunomura W., Takakuwa Y., Mohandas N., and Jap B.K. Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization. Nat. Struct. Biol. 7 (2000) 871-875
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 871-875
    • Han, B.G.1    Nunomura, W.2    Takakuwa, Y.3    Mohandas, N.4    Jap, B.K.5
  • 11
    • 0034089870 scopus 로고    scopus 로고
    • The genetics of the protein 4.1family: organizers of the membrane and cytoskeleton
    • Hoover K.B., and Bryant P.J. The genetics of the protein 4.1family: organizers of the membrane and cytoskeleton. Curr. Opin. Cell Biol. 12 (2000) 229-234
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 229-234
    • Hoover, K.B.1    Bryant, P.J.2
  • 12
    • 0026772154 scopus 로고
    • Identification of the binding interface involved in linkage of cytoskeletal protein 4.1 to the erythrocyte anion exchanger
    • Jöns T., and Drenckhahn D. Identification of the binding interface involved in linkage of cytoskeletal protein 4.1 to the erythrocyte anion exchanger. EMBO J. 11 (1992) 2863-2867
    • (1992) EMBO J. , vol.11 , pp. 2863-2867
    • Jöns, T.1    Drenckhahn, D.2
  • 13
    • 0021240155 scopus 로고
    • A structural model of human erythrocyte protein 4.1.J
    • Leto T.L., and Marchesi V.T. A structural model of human erythrocyte protein 4.1.J. Biol. Chem. 259 (1984) 4603-4608
    • (1984) Biol. Chem. , vol.259 , pp. 4603-4608
    • Leto, T.L.1    Marchesi, V.T.2
  • 14
    • 0034535593 scopus 로고    scopus 로고
    • Hereditary spherocytosis in zebrafish riesling illustrates evolution of erythroid beta-spectrin structure, and function in red cell morphogenesis and membrane stability
    • Liao E.C., Paw B.H., Peters L.L., Zapata A., Pratt S.J., Do C.P., Lieschke G., and Zon L.I. Hereditary spherocytosis in zebrafish riesling illustrates evolution of erythroid beta-spectrin structure, and function in red cell morphogenesis and membrane stability. Development 127 (2000) 5123-5132
    • (2000) Development , vol.127 , pp. 5123-5132
    • Liao, E.C.1    Paw, B.H.2    Peters, L.L.3    Zapata, A.4    Pratt, S.J.5    Do, C.P.6    Lieschke, G.7    Zon, L.I.8
  • 15
    • 0034951712 scopus 로고    scopus 로고
    • Antigenic properties of human glycophorins-An update
    • Lisowska E. Antigenic properties of human glycophorins-An update. Adv. Exp. Med. Biol. 491 (2001) 155-169
    • (2001) Adv. Exp. Med. Biol. , vol.491 , pp. 155-169
    • Lisowska, E.1
  • 16
    • 0028558651 scopus 로고
    • Calmodulin modulates protein 4.1 binding to human erythrocyte membranes
    • Lombardo C.R., and Low P.S. Calmodulin modulates protein 4.1 binding to human erythrocyte membranes. Biochim. Biophys. Acta 1196 (1994) 139-144
    • (1994) Biochim. Biophys. Acta , vol.1196 , pp. 139-144
    • Lombardo, C.R.1    Low, P.S.2
  • 17
    • 14844314119 scopus 로고    scopus 로고
    • Modulation of erythrocyte membrane mechanical function by protein 4.1 phosphorylation
    • Manno S., Takakuwa Y., and Mohandas N. Modulation of erythrocyte membrane mechanical function by protein 4.1 phosphorylation. J. Biol. Chem. 280 (2005) 7581-7587
    • (2005) J. Biol. Chem. , vol.280 , pp. 7581-7587
    • Manno, S.1    Takakuwa, Y.2    Mohandas, N.3
  • 18
    • 0028917977 scopus 로고
    • Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein
    • Marfatia S.M., Leu R.A., Branton D., and Chishti A.H. Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein. J. Biol. Chem. 270 (1995) 715-719
    • (1995) J. Biol. Chem. , vol.270 , pp. 715-719
    • Marfatia, S.M.1    Leu, R.A.2    Branton, D.3    Chishti, A.H.4
  • 21
    • 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 (2000) 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
  • 22
    • 0034637458 scopus 로고    scopus 로고
    • Regulation of protein 4.1R, p55, and glycophorin C ternary complex in human erythrocyte membrane
    • Nunomura W., Takakuwa Y., Parra M., Conboy J.G., and Mohandas N. Regulation of protein 4.1R, p55, and glycophorin C ternary complex in human erythrocyte membrane. J. Biol. Chem. 275 (2000) 24540-24546
    • (2000) J. Biol. Chem. , vol.275 , pp. 24540-24546
    • Nunomura, W.1    Takakuwa, Y.2    Parra, M.3    Conboy, J.G.4    Mohandas, N.5
  • 23
    • 5444270911 scopus 로고    scopus 로고
    • Regulation of 135 kDa protein 4.1R interactions with membrane proteins by its head-piece region
    • 500a (suppl.)
    • Nunomura W., An X., Gascard P., Parra M., Narla M., and Takakuwa Y. Regulation of 135 kDa protein 4.1R interactions with membrane proteins by its head-piece region. Mol. Biol. Cell 13 (2002) 500a (suppl.)
    • (2002) Mol. Biol. Cell , vol.13
    • Nunomura, W.1    An, X.2    Gascard, P.3    Parra, M.4    Narla, M.5    Takakuwa, Y.6
  • 25
    • 0036745638 scopus 로고    scopus 로고
    • Characterization of zebrafish merlot/chablis as non-mammalian vertebrate models for severe congenital anemia due to protein 4.1 deficiency
    • Shafizadeh E., Paw B.H., Foott H., Liao E.C., Barut BruceA., Cope B.A., and Lin Zon.L.I. Characterization of zebrafish merlot/chablis as non-mammalian vertebrate models for severe congenital anemia due to protein 4.1 deficiency. Development 129 (2002) 4359-4370
    • (2002) Development , vol.129 , pp. 4359-4370
    • Shafizadeh, E.1    Paw, B.H.2    Foott, H.3    Liao, E.C.4    Barut, BruceA.5    Cope, B.A.6    Lin, Zon.L.I.7
  • 27
    • 0025924751 scopus 로고
    • 2+-dependent regulation of the spectrin/actin interaction by calmodulin and protein 4.1
    • 2+-dependent regulation of the spectrin/actin interaction by calmodulin and protein 4.1. J. Biol. Chem. 266 (1991) 1134-1140
    • (1991) J. Biol. Chem. , vol.266 , pp. 1134-1140
    • Tanaka, T.1    Kadowaki, K.2    Lazarides, E.3    Sobue, K.4
  • 28
    • 0022518092 scopus 로고
    • Restoration of normal membrane stability to unstable protein 4.1-deficient erythrocyte membranes by incorporation of purified protein 4.1
    • Takakuwa Y., Tchernia G., Rossi M., Benabadji M., and Mohandas N. Restoration of normal membrane stability to unstable protein 4.1-deficient erythrocyte membranes by incorporation of purified protein 4.1. J. Clin. Invest. 78 (1986) 80-85
    • (1986) J. Clin. Invest. , vol.78 , pp. 80-85
    • Takakuwa, Y.1    Tchernia, G.2    Rossi, M.3    Benabadji, M.4    Mohandas, N.5
  • 30
    • 0019406583 scopus 로고
    • Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability
    • Tchernia G., Mohandas N., and Shohet S.B. Deficiency of skeletal membrane protein band 4.1 in homozygous hereditary elliptocytosis. Implications for erythrocyte membrane stability. J. Clin. Invest. 68 (1981) 454-460
    • (1981) J. Clin. Invest. , vol.68 , pp. 454-460
    • Tchernia, G.1    Mohandas, N.2    Shohet, S.B.3
  • 31
    • 0028487452 scopus 로고
    • Optical biosensor for monitoring microbial cells
    • Watts H.J., and Lowe C.R. Optical biosensor for monitoring microbial cells. Anal. Chem. 66 (1994) 2465-2470
    • (1994) Anal. Chem. , vol.66 , pp. 2465-2470
    • Watts, H.J.1    Lowe, C.R.2


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