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Volumn 19, Issue 15, 1999, Pages 6457-6467

A novel neuron-enriched homolog of the erythrocyte membrane cytoskeletal protein 4.1

Author keywords

Ankyrin; Cytoskeleton synapse; Neuron; Protein 4.1; Red blood cell

Indexed keywords

ERYTHROCYTE BAND 4.1 PROTEIN; GLUTAMATE RECEPTOR; ISOPROTEIN;

EID: 0033179416     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.19-15-06457.1999     Document Type: Article
Times cited : (126)

References (55)
  • 1
    • 0032054473 scopus 로고    scopus 로고
    • Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: Differential attachment of NMDA versus AMPA receptors
    • Allison DW, Gelfand VI, Spector I, Craig AM (1998) Role of actin in anchoring postsynaptic receptors in cultured hippocampal neurons: differential attachment of NMDA versus AMPA receptors. J Neurosci 18:2423-2436.
    • (1998) J Neurosci , vol.18 , pp. 2423-2436
    • Allison, D.W.1    Gelfand, V.I.2    Spector, I.3    Craig, A.M.4
  • 2
    • 0027291592 scopus 로고
    • Evidence that red blood cell protein p55 may participate in the skeleton-membrane linkage that involves protein 4.1 and glycophorin C
    • Alloisio N, Dalla Venezia N, Rana A, Andrabi K, Texier P, Gilsanz F, Cartron JP, Delaunay J, Chishti AH (1993) Evidence that red blood cell protein p55 may participate in the skeleton-membrane linkage that involves protein 4.1 and glycophorin C. Blood 82:1323-1327.
    • (1993) Blood , vol.82 , pp. 1323-1327
    • Alloisio, N.1    Dalla Venezia, N.2    Rana, A.3    Andrabi, K.4    Texier, P.5    Gilsanz, F.6    Cartron, J.P.7    Delaunay, J.8    Chishti, A.H.9
  • 4
    • 0022986547 scopus 로고
    • Purification of brain analogs of red blood cell membrane skeletal proteins: Ankyrin, protein 4.1 (synapsin), spectrin, and spectrin subunits
    • Bennett V, Baines AJ, Davis J (1986) Purification of brain analogs of red blood cell membrane skeletal proteins: ankyrin, protein 4.1 (synapsin), spectrin, and spectrin subunits, Methods Enzymol 134:55-69.
    • (1986) Methods Enzymol , vol.134 , pp. 55-69
    • Bennett, V.1    Baines, A.J.2    Davis, J.3
  • 5
    • 0030862358 scopus 로고    scopus 로고
    • Developmental expression pattern of phototransduction components in mammalian pineal implies a light-sensing function
    • Blackshaw S, Snyder SH (1997) Developmental expression pattern of phototransduction components in mammalian pineal implies a light-sensing function. J Neurosci 17:8074-8082.
    • (1997) J Neurosci , vol.17 , pp. 8074-8082
    • Blackshaw, S.1    Snyder, S.H.2
  • 6
    • 0028810956 scopus 로고
    • Synaptic structure and function: Dynamic organization yields architectural precision
    • Burns ME, Augustine GJ (1995) Synaptic structure and function: dynamic organization yields architectural precision. Cell 83:187-194.
    • (1995) Cell , vol.83 , pp. 187-194
    • Burns, M.E.1    Augustine, G.J.2
  • 7
    • 0026739575 scopus 로고
    • Regulation and post-translational modification of erythrocyte membrane and membrane-skeletal proteins
    • Cohen CM, Gascard P (1992) Regulation and post-translational modification of erythrocyte membrane and membrane-skeletal proteins. Semin Hematol 29:244-292.
    • (1992) Semin Hematol , vol.29 , pp. 244-292
    • Cohen, C.M.1    Gascard, P.2
  • 8
    • 0011727270 scopus 로고
    • Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton
    • Conboy J, Kan YW, Shohet SB, Mohandas N (1986a) Molecular cloning of protein 4.1, a major structural element of the human erythrocyte membrane skeleton. Proc Natl Acad Sci USA 83:9512-9516.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 9512-9516
    • Conboy, J.1    Kan, Y.W.2    Shohet, S.B.3    Mohandas, N.4
  • 9
    • 0022494195 scopus 로고
    • Molecular basis of hereditary elliptocytosis due to protein 4.1 deficiency
    • Conboy J, Mohandas N, Tchernia G, Kan YW (1986b) Molecular basis of hereditary elliptocytosis due to protein 4.1 deficiency. N Engl J Med 315:680-685.
    • (1986) N Engl J Med , vol.315 , pp. 680-685
    • Conboy, J.1    Mohandas, N.2    Tchernia, G.3    Kan, Y.W.4
  • 10
    • 0007170020 scopus 로고
    • Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells
    • Conboy JG, Chan J, Mohandas N, Kan YW (1988) Multiple protein 4.1 isoforms produced by alternative splicing in human erythroid cells. Proc Natl Acad Sci USA 85:9062-9065.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 9062-9065
    • Conboy, J.G.1    Chan, J.2    Mohandas, N.3    Kan, Y.W.4
  • 11
    • 0025787256 scopus 로고
    • Tissue- and development-specific alternative RNA splicing regulates expression of multiple isoforms of erythroid membrane protein 4.1
    • Conboy JG, Chan JY, Chasis JA, Kan YW, Mohandas N (1991) Tissue- and development-specific alternative RNA splicing regulates expression of multiple isoforms of erythroid membrane protein 4.1. J Biol Chem 266:8273-8280.
    • (1991) J Biol Chem , vol.266 , pp. 8273-8280
    • Conboy, J.G.1    Chan, J.Y.2    Chasis, J.A.3    Kan, Y.W.4    Mohandas, N.5
  • 12
    • 0022815261 scopus 로고
    • Immunological detection of an analogue of the erythroid protein 4.1 in endothelial cells
    • Constantinescu E, Heltianu C, Simionescu M (1986) Immunological detection of an analogue of the erythroid protein 4.1 in endothelial cells. Cell Biol Int Rep 10:861-868.
    • (1986) Cell Biol Int Rep , vol.10 , pp. 861-868
    • Constantinescu, E.1    Heltianu, C.2    Simionescu, M.3
  • 13
    • 0022998571 scopus 로고
    • Identification of the functional site of erythrocyte protein 4.1 involved in spectrin-actin associations
    • Correas I, Leto TL, Speicher DW, Marchesi VT (1986) Identification of the functional site of erythrocyte protein 4.1 involved in spectrin-actin associations. J Biol Chem 261:3310-3315.
    • (1986) J Biol Chem , vol.261 , pp. 3310-3315
    • Correas, I.1    Leto, T.L.2    Speicher, D.W.3    Marchesi, V.T.4
  • 14
    • 0027273473 scopus 로고
    • The distribution of glutamate receptors in cultured rat hippocampal neurons: Postsynaptic clustering of AMPA-selective subunits
    • Craig A, Blackstone C, Huganir R, Banker G (1993) The distribution of glutamate receptors in cultured rat hippocampal neurons: postsynaptic clustering of AMPA-selective subunits. Neuron 10:1055-1068.
    • (1993) Neuron , vol.10 , pp. 1055-1068
    • Craig, A.1    Blackstone, C.2    Huganir, R.3    Banker, G.4
  • 15
    • 0025320809 scopus 로고
    • Selective modulation of band 4.1 binding to erythrocyte membranes by protein kinase
    • Danilov YN, Fennell R, Ling E, Cohen CM (1990) Selective modulation of band 4.1 binding to erythrocyte membranes by protein kinase C. J Biol Chem 265:2556-2562.
    • (1990) C. J Biol Chem , vol.265 , pp. 2556-2562
    • Danilov, Y.N.1    Fennell, R.2    Ling, E.3    Cohen, C.M.4
  • 16
    • 0024530060 scopus 로고
    • Distribution of analogues of spectrin, fodrin and protein 4.1 in rat spermatogenic cells
    • De Cesaris P, Filippini A, Ziparo E, Russo MA, Stefanini M (1989) Distribution of analogues of spectrin, fodrin and protein 4.1 in rat spermatogenic cells. Prog Clin Biol Res 296:149-152.
    • (1989) Prog Clin Biol Res , vol.296 , pp. 149-152
    • De Cesaris, P.1    Filippini, A.2    Ziparo, E.3    Russo, M.A.4    Stefanini, M.5
  • 17
    • 0030296378 scopus 로고    scopus 로고
    • Synaptic proteins and the assembly of synaptic junctions
    • Garner CC, Kindler S (1996) Synaptic proteins and the assembly of synaptic junctions. Trends Cell Biol 6:429-433.
    • (1996) Trends Cell Biol , vol.6 , pp. 429-433
    • Garner, C.C.1    Kindler, S.2
  • 19
    • 0028330166 scopus 로고
    • Dendritic spines: Cellular specializations imparting both stability and flexibility to synaptic function
    • Harris KM, Kater SB (1994) Dendritic spines: cellular specializations imparting both stability and flexibility to synaptic function. Annu Rev Neurosci 17:341-371.
    • (1994) Annu Rev Neurosci , vol.17 , pp. 341-371
    • Harris, K.M.1    Kater, S.B.2
  • 20
    • 0026732691 scopus 로고
    • Characterization of human brain cDNA encoding the general isoform of beta-spectrin
    • Hu RJ, Watanabe M, Bennett V (1992) Characterization of human brain cDNA encoding the general isoform of beta-spectrin. J Biol Chem 267:18715-18722.
    • (1992) J Biol Chem , vol.267 , pp. 18715-18722
    • Hu, R.J.1    Watanabe, M.2    Bennett, V.3
  • 21
    • 0027401499 scopus 로고
    • Genomic structure of the locus encoding protein 4.1. Structural basis for complex combinational patterns of tissue-specific alternative RNA splicing
    • Huang JP, Tang CJ, Kou GH, Marchesi VT, Benz Jr EJ, Tang TK (1993) Genomic structure of the locus encoding protein 4.1. Structural basis for complex combinational patterns of tissue-specific alternative RNA splicing. J Biol Chem 268:3758-3766.
    • (1993) J Biol Chem , vol.268 , pp. 3758-3766
    • Huang, J.P.1    Tang, C.J.2    Kou, G.H.3    Marchesi, V.T.4    Benz E.J., Jr.5    Tang, T.K.6
  • 22
    • 0032053865 scopus 로고    scopus 로고
    • Radiation hybrid mapping of EPB41L1, a novel protein 4.1 homologue, to human chromosome 20q11.2-q12
    • Kim AC, Van Huffel C, Lutchman M, Chishti AH (1998) Radiation hybrid mapping of EPB41L1, a novel protein 4.1 homologue, to human chromosome 20q11.2-q12. Genomics 49:165-166.
    • (1998) Genomics , vol.49 , pp. 165-166
    • Kim, A.C.1    Van Huffel, C.2    Lutchman, M.3    Chishti, A.H.4
  • 23
    • 0028985712 scopus 로고
    • AnkyrinG: A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier
    • Kordeli E, Lamber S, Bennett V (1995) AnkyrinG: a new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier. J Biol Chem 270:2352-2359.
    • (1995) J Biol Chem , vol.270 , pp. 2352-2359
    • Kordeli, E.1    Lamber, S.2    Bennett, V.3
  • 24
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau HC, Schenker LT, Kennedy MB, Seeburg PH (1995) Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 269:1737-1740.
    • (1995) Science , vol.269 , pp. 1737-1740
    • Kornau, H.C.1    Schenker, L.T.2    Kennedy, M.B.3    Seeburg, P.H.4
  • 27
    • 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 binding interface by in vitro mutagenesis
    • Marfatia SM, Cabral JHM, Kim AC, Byron O, Chrishti AH (1997) The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C: analysis of 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    Cabral, J.H.M.2    Kim, A.C.3    Byron, O.4    Chrishti, A.H.5
  • 28
    • 25344462463 scopus 로고    scopus 로고
    • Phosphorylation of the MARCKS-related domain of adducin occurs in dendritic spines of hippocampal neurons and modulates its actin-capping and spectrin-recruiting activities
    • Matsuoka Y, Li X, Bennett GV (1997) Phosphorylation of the MARCKS-related domain of adducin occurs in dendritic spines of hippocampal neurons and modulates its actin-capping and spectrin-recruiting activities. Mol Biol Cell [Suppl] 8:275a.
    • (1997) Mol Biol Cell [Suppl] , vol.8
    • Matsuoka, Y.1    Li, X.2    Bennett, G.V.3
  • 29
  • 33
    • 85087575156 scopus 로고    scopus 로고
    • 2+-dependent and -independent calmodulin binding sites on protein 4.1: Implications in regulation of 4.1 interactions with transmembrane proteins
    • 2+-dependent and -independent calmodulin binding sites on protein 4.1: implications in regulation of 4.1 interactions with transmembrane proteins. Mol Biol Cell [Suppl] 8:176a.
    • (1997) Mol Biol Cell [Suppl] , vol.8
    • Nunomura, W.1    Takakuwa, Y.2    Parra, M.3    Conboy, J.4    Mohandas, N.5
  • 35
    • 0025874185 scopus 로고
    • Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively spliced genes
    • Otto E, Kunimoto M, McLaughlin T, Bennett V (1991) Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively spliced genes. J Cell Biol 114:241-253.
    • (1991) J Cell Biol , vol.114 , pp. 241-253
    • Otto, E.1    Kunimoto, M.2    McLaughlin, T.3    Bennett, V.4
  • 36
    • 0020788331 scopus 로고
    • Red cell membrane skeletal defects in hereditary and acquired hemolytic anemias
    • Palek J, Lux SE (1983) Red cell membrane skeletal defects in hereditary and acquired hemolytic anemias. Semin Hematol 20:189.
    • (1983) Semin Hematol , vol.20 , pp. 189
    • Palek, J.1    Lux, S.E.2
  • 37
    • 0000104067 scopus 로고    scopus 로고
    • Cloning and characterization of 4.1G (EPB41L2), a new member of the skeletal protein 4.1 (EPB41) gene family
    • Parra M, Gascard P, Walensky LD, Snyder SH, Mohandas N, Conboy JG (1998a) Cloning and characterization of 4.1G (EPB41L2), a new member of the skeletal protein 4.1 (EPB41) gene family. Genomics 49:298-306.
    • (1998) Genomics , vol.49 , pp. 298-306
    • Parra, M.1    Gascard, P.2    Walensky, L.D.3    Snyder, S.H.4    Mohandas, N.5    Conboy, J.G.6
  • 38
    • 25344441654 scopus 로고    scopus 로고
    • Characterization of protein 4.1B, a novel member of the protein 4.1 family with high level, focal expression in brain
    • Parra M, Walensky LD, Chan N, Snyder S, Mohandas N, Conboy J (1998b) Characterization of protein 4.1B, a novel member of the protein 4.1 family with high level, focal expression in brain. Mol Biol Cell [Suppl] 9:265a.
    • (1998) Mol Biol Cell [Suppl] , vol.9
    • Parra, M.1    Walensky, L.D.2    Chan, N.3    Snyder, S.4    Mohandas, N.5    Conboy, J.6
  • 39
    • 0021940465 scopus 로고
    • Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton
    • Pasternack GR, Anderson RA, Leto TL, Marchesi VT (1985) Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton. J Biol Chem 260:3676-3683.
    • (1985) J Biol Chem , vol.260 , pp. 3676-3683
    • Pasternack, G.R.1    Anderson, R.A.2    Leto, T.L.3    Marchesi, V.T.4
  • 41
    • 0024809783 scopus 로고
    • Functional role for glycophorin c and its interaction with the human red cell membrane skeletal component, protein 4.1
    • discussion 572-573
    • Reid ME, Takakuwa Y, Tchernia G, Jensen RH, Chasis JA, Mohandas N (1989) Functional role for glycophorin C and its interaction with the human red cell membrane skeletal component, protein 4.1. Prog Clin Biol Res 319:553-571; discussion 572-573.
    • (1989) Prog Clin Biol Res , vol.319 , pp. 553-571
    • Reid, M.E.1    Takakuwa, Y.2    Tchernia, G.3    Jensen, R.H.4    Chasis, J.A.5    Mohandas, N.6
  • 42
    • 0025354418 scopus 로고
    • Glycophorin C content of human erythrocyte membrane is regulated by protein 4.1
    • Reid ME, Takakuwa Y, Conboy J, Tchernia G, Mohandas N (1990) Glycophorin C content of human erythrocyte membrane is regulated by protein 4.1. Blood 75:2229-2234.
    • (1990) Blood , vol.75 , pp. 2229-2234
    • Reid, M.E.1    Takakuwa, Y.2    Conboy, J.3    Tchernia, G.4    Mohandas, N.5
  • 43
    • 0022454882 scopus 로고
    • Brain spectrin(240/235) and brain spectrin(240/235E): Two distinct spectrin subtypes with different locations within mammalian neural cells
    • Riederer BM, Zagon IS, Goodman SR (1986) Brain spectrin(240/235) and brain spectrin(240/235E): two distinct spectrin subtypes with different locations within mammalian neural cells. J Cell Biol 102:2088-2096.
    • (1986) J Cell Biol , vol.102 , pp. 2088-2096
    • Riederer, B.M.1    Zagon, I.S.2    Goodman, S.R.3
  • 46
    • 0028093239 scopus 로고
    • Evidence for the association of protein 4.1 immunoreactive forms with neurofibrillary tangles in Alzheimer's disease brains
    • Sihag RK, Wang LW, Cataldo AM, Hamlin M, Cohen CM, Nixon RA (1994) Evidence for the association of protein 4.1 immunoreactive forms with neurofibrillary tangles in Alzheimer's disease brains. Brain Res 656:14-26.
    • (1994) Brain Res , vol.656 , pp. 14-26
    • Sihag, R.K.1    Wang, L.W.2    Cataldo, A.M.3    Hamlin, M.4    Cohen, C.M.5    Nixon, R.A.6
  • 47
    • 0023132974 scopus 로고
    • Ontogeny, compartmentation, and turnover of spectrin isoforms in rat central neurons
    • Siman R, Ahdoot M, Lynch G (1987) Ontogeny, compartmentation, and turnover of spectrin isoforms in rat central neurons. J Neurosci 7:55-64.
    • (1987) J Neurosci , vol.7 , pp. 55-64
    • Siman, R.1    Ahdoot, M.2    Lynch, G.3
  • 49
    • 0021175072 scopus 로고
    • An analogue of the erythroid membrane skeletal protein 4.1 in nonerythroid cells
    • Spiegel JE, Beardsley DS, Southwick FS, Lux SE (1984) An analogue of the erythroid membrane skeletal protein 4.1 in nonerythroid cells. J Cell Biol 99:886-893.
    • (1984) J Cell Biol , vol.99 , pp. 886-893
    • Spiegel, J.E.1    Beardsley, D.S.2    Southwick, F.S.3    Lux, S.E.4
  • 50
    • 0025268929 scopus 로고
    • Heterogeneity of mRNA and protein products arising from the protein 4.1 gene in erythroid and nonerythroid tissues
    • Tang TK, Qin Z, Leto T, Marchesi VT, Benz Jr EJ (1990) Heterogeneity of mRNA and protein products arising from the protein 4.1 gene in erythroid and nonerythroid tissues. J Cell Biol 110:617-624.
    • (1990) J Cell Biol , vol.110 , pp. 617-624
    • Tang, T.K.1    Qin, Z.2    Leto, T.3    Marchesi, V.T.4    Benz E.J., Jr.5
  • 52
    • 0027328684 scopus 로고
    • Spatial segregation of odorant receptor expression in the mammalian olfactory epithelium
    • Vassar R, Ngai J, Axel R (1993) Spatial segregation of odorant receptor expression in the mammalian olfactory epithelium. Cell 74:309-318.
    • (1993) Cell , vol.74 , pp. 309-318
    • Vassar, R.1    Ngai, J.2    Axel, R.3
  • 53
    • 0032489868 scopus 로고    scopus 로고
    • The 13 kDa FK506 binding protein, FKBP13, interacts with a novel homologue of the erythrocyte membrane cytoskeletal protein 4.1
    • Walensky LD, Gascard P, Fields ME, Blackshaw S, Conboy JG, Mohandas N, Snyder SH (1998a) The 13 kDa FK506 binding protein, FKBP13, interacts with a novel homologue of the erythrocyte membrane cytoskeletal protein 4.1. J Cell Biol 141:143-153.
    • (1998) J Cell Biol , vol.141 , pp. 143-153
    • Walensky, L.D.1    Gascard, P.2    Fields, M.E.3    Blackshaw, S.4    Conboy, J.G.5    Mohandas, N.6    Snyder, S.H.7


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