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Volumn 5, Issue 2, 1998, Pages 116-121

Function of p55 and its nonerythroid homologues

Author keywords

[No Author keywords available]

Indexed keywords

CYTOSKELETON PROTEIN; ERYTHROCYTE BAND 4.1 PROTEIN; GLYCOPHORIN C; GUANYLATE KINASE; MEMBRANE PROTEIN; PHOSPHOPROTEIN; POLYPEPTIDE;

EID: 0031921349     PISSN: 10656251     EISSN: None     Source Type: Journal    
DOI: 10.1097/00062752-199803000-00006     Document Type: Review
Times cited : (37)

References (43)
  • 1
    • 0025941465 scopus 로고
    • The discs large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions
    • Woods DF, Brayant PJ: The discs large tumor suppressor gene of Drosophila encodes a guanylate kinase homolog localized at septate junctions. Cell 1991, 66:451-464.
    • (1991) Cell , vol.66 , pp. 451-464
    • Woods, D.F.1    Brayant, P.J.2
  • 2
    • 0025994663 scopus 로고
    • Molecular identification of a major palmitoylated erythrocyte membrane protein containing the src homology 3 motif
    • Ruff P, Speicher DW, Chishti AH: Molecular identification of a major palmitoylated erythrocyte membrane protein containing the src homology 3 motif. Proc Natl Acad Sci U S A 1991, 88:6595-6599.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 6595-6599
    • Ruff, P.1    Speicher, D.W.2    Chishti, A.H.3
  • 3
    • 0025098170 scopus 로고
    • Fatty acid acylation of membrane skeletal proteins in human erythrocytes
    • Maretzki D, Mariani M, Lutz HU: Fatty acid acylation of membrane skeletal proteins in human erythrocytes. FEBS Lett 1990, 259:305-310.
    • (1990) FEBS Lett , vol.259 , pp. 305-310
    • Maretzki, D.1    Mariani, M.2    Lutz, H.U.3
  • 4
    • 0026639316 scopus 로고
    • Fatty acid acylation of a 55 kDa membrane protein of human erythrocytes
    • Das AK, Kundu M, Chakrabarti P, Basu J: Fatty acid acylation of a 55 kDa membrane protein of human erythrocytes. Biochem Biophys Acta 1992, 1108:128-132.
    • (1992) Biochem Biophys Acta , vol.1108 , pp. 128-132
    • Das, A.K.1    Kundu, M.2    Chakrabarti, P.3    Basu, J.4
  • 5
    • 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, Venezia ND, Rana A, Andrabi K, Texier P, Gilsanz F, Cartron JP, Delaunay J, Chishti AH: Evidence that red blood cell protein p55 may participate in the skeleton-membrane linkage that involves protein 4.1 and glycophorin C. Blood 1993, 82:1323-1327.
    • (1993) Blood , vol.82 , pp. 1323-1327
    • Alloisio, N.1    Venezia, N.D.2    Rana, A.3    Andrabi, K.4    Texier, P.5    Gilsanz, F.6    Cartron, J.P.7    Delaunay, J.8    Chishti, A.H.9
  • 6
    • 0029915248 scopus 로고    scopus 로고
    • Reduced invasion and growth of Plasmodium falciparum into elliptocytic red blood cells with a combined deficiency of protein 4.1, glycophorin C, and p55
    • Chishti AH, Palek J, Fisher D, Maalouf GJ, Liu S-C: Reduced invasion and growth of Plasmodium falciparum into elliptocytic red blood cells with a combined deficiency of protein 4.1, glycophorin C, and p55. Blood 1996, 87:3462-3469.
    • (1996) Blood , vol.87 , pp. 3462-3469
    • Chishti, A.H.1    Palek, J.2    Fisher, D.3    Maalouf, G.J.4    Liu, S.-C.5
  • 7
    • 0026801368 scopus 로고
    • Red blood cell glycophorins
    • Chasis JA, Mohandas N: Red blood cell glycophorins. Blood 1992, 80:1869-1879.
    • (1992) Blood , vol.80 , pp. 1869-1879
    • Chasis, J.A.1    Mohandas, N.2
  • 8
    • 0027391114 scopus 로고
    • An isoform-specific mutation in the protein 4.1 gene results in hereditary elliptocytosis and complete deficiency of protein 4.1 in erythrocytes but not in nonerythroid cells
    • Conboy JG, Chasis JA, Winardi R, Tchernia G, Kan YW, Mohandas N: An isoform-specific mutation in the protein 4.1 gene results in hereditary elliptocytosis and complete deficiency of protein 4.1 in erythrocytes but not in nonerythroid cells. J Clin Invest 1993, 91:77-82.
    • (1993) J Clin Invest , vol.91 , pp. 77-82
    • Conboy, J.G.1    Chasis, J.A.2    Winardi, R.3    Tchernia, G.4    Kan, Y.W.5    Mohandas, N.6
  • 10
    • 0030006958 scopus 로고    scopus 로고
    • Differential use of protein 4.1 translation initiation sites during erythropoiesis: Implications for a mutation-induced stage-specific deficiency of protein 4.1 during erythroid development
    • Chasis JA, Coulombel L, McGee S, Lee G, Tchernia G, Conboy J, Mohandas N: Differential use of protein 4.1 translation initiation sites during erythropoiesis: implications for a mutation-induced stage-specific deficiency of protein 4.1 during erythroid development. Blood 1996, 87:5324-5331.
    • (1996) Blood , vol.87 , pp. 5324-5331
    • Chasis, J.A.1    Coulombel, L.2    McGee, S.3    Lee, G.4    Tchernia, G.5    Conboy, J.6    Mohandas, N.7
  • 11
    • 0028944110 scopus 로고
    • Identification of the membrane attachment sites for protein 4.1 in the human erythrocyte
    • Hemming NJ, Anstee DJ, Staricoff MA, Tanner MJA, Mohandas N: Identification of the membrane attachment sites for protein 4.1 in the human erythrocyte. J Biol Chem 1995, 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.A.4    Mohandas, N.5
  • 12
    • 0028013757 scopus 로고
    • Membraneactin microfilament connections: An increasing diversity of players related to band 4.1
    • Arpin M, Algrain M, Louvard D: Membraneactin microfilament connections: an increasing diversity of players related to band 4.1. Curr Opin Cell Biol 1994, 16:136-141.
    • (1994) Curr Opin Cell Biol , vol.16 , pp. 136-141
    • Arpin, M.1    Algrain, M.2    Louvard, D.3
  • 13
    • 0028325048 scopus 로고
    • A Drosophila homologue of membrane-skeleton protein 4.1 is associated with septate junctions and is encoded by the coracle gene
    • Fehon RG, Dawson IA, Artavanis-Tsakonas S: A Drosophila homologue of membrane-skeleton protein 4.1 is associated with septate junctions and is encoded by the coracle gene. Development 1994, 120:545-557.
    • (1994) Development , vol.120 , pp. 545-557
    • Fehon, R.G.1    Dawson, I.A.2    Artavanis-Tsakonas, S.3
  • 15
    • 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 SM, Lue RA, Branton D, Chishti AH: 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 1995, 270:715-719.
    • (1995) J Biol Chem , vol.270 , pp. 715-719
    • Marfatia, S.M.1    Lue, R.A.2    Branton, D.3    Chishti, A.H.4
  • 16
    • 0028237630 scopus 로고
    • In vitro binding studies suggest a membrane-associated complex between erythroid p55, protein 4.1, and glycophorin
    • Marfatia SM, Lue RA, Branton D, Chishti AH: In vitro binding studies suggest a membrane-associated complex between erythroid p55, protein 4.1, and glycophorin. J Biol Chem 1994, 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
    • 0028096801 scopus 로고
    • Cloning and characterization of hDlg: The human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1
    • Lue RA, Marfatia SM, Branton D, Chishti AH: Cloning and characterization of hDlg: the human homologue of the Drosophila discs large tumor suppressor binds to protein 4.1. Proc Natl Acad Sci U S A 1994, 91:9818-9822.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 9818-9822
    • Lue, R.A.1    Marfatia, S.M.2    Branton, D.3    Chishti, A.H.4
  • 18
    • 15444341493 scopus 로고    scopus 로고
    • Organizing a junctional complex requires specific domains of the Drosophila MAGUK Dlg
    • Woods DF, Hough CD, Bryant PJ: Organizing a junctional complex requires specific domains of the Drosophila MAGUK Dlg[abstract]. Mol Biol Cell 1997, 8:412. Using transgenic flies expressing mutant Dlg proteins, the authors show that the PDZ2 and HOOK (4.1 binding) domain are necessary to target Dlg to the septate junctions. Similarly, PDZ2 and PDZ3 domains are necessary for growth regulation but not junctional structure, whereas the SH3 and HOOK domains are required for both functions.
    • (1997) Mol Biol Cell , vol.8 , pp. 412
    • Woods, D.F.1    Hough, C.D.2    Bryant, P.J.3
  • 19
    • 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 SM, Cabral JHM, Kim AC, Byron O, Chishti AH: 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 1997, 272:24191-24197. The PDZ domain of p55 binds to the cytoplasmic domain of glycophorin C; the last three residues (YFI) of glycophorin C are critical for this binding.
    • (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    Chishti, A.H.5
  • 21
    • 0026492629 scopus 로고
    • The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs large tumor suppressor protein
    • Cho KO, Hunt CA, Kennedy MB: The rat brain postsynaptic density fraction contains a homolog of the Drosophila discs large tumor suppressor protein. Neuron 1992, 9:929-942.
    • (1992) Neuron , vol.9 , pp. 929-942
    • Cho, K.O.1    Hunt, C.A.2    Kennedy, M.B.3
  • 22
    • 0028902098 scopus 로고
    • DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins
    • Ponting CP, Phillips C: DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins. Trends Biochem Sci 1995, 20:102-103.
    • (1995) Trends Biochem Sci , vol.20 , pp. 102-103
    • Ponting, C.P.1    Phillips, C.2
  • 23
    • 0029066512 scopus 로고
    • FAP-1: A protein tyrosine phosphatase that associates with Fas
    • Sato T, Irie S, Kitada S, Reed JC: FAP-1: a protein tyrosine phosphatase that associates with Fas. Science 1995, 268:411-415.
    • (1995) Science , vol.268 , pp. 411-415
    • Sato, T.1    Irie, S.2    Kitada, S.3    Reed, J.C.4
  • 24
    • 0029098659 scopus 로고
    • Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95
    • Kornau H-C, Schenker LT, Kennedy MB, Seeburg PH: Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95. Science 1995, 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
  • 25
    • 0028882810 scopus 로고
    • Clustering of Shaker-type K+ channels by direct interaction with the PSD-95/SAP90 family of membrane-associated guanylate kinases
    • Kim E, Niethammer AR, Rothschild AY, Jan N, Sheng M: Clustering of Shaker-type K+ channels by direct interaction with the PSD-95/SAP90 family of membrane-associated guanylate kinases. Nature 1995, 378:85-88.
    • (1995) Nature , vol.378 , pp. 85-88
    • Kim, E.1    Niethammer, A.R.2    Rothschild, A.Y.3    Jan, N.4    Sheng, M.5
  • 28
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle DA, Lee A, Lewis J, Kim E, Sheng M, MacKinnon R: Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell 1996, 85:1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    MacKinnon, R.6
  • 29
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T: Protein modules and signalling networks. Nature 1995, 373:573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 30
    • 0029819449 scopus 로고    scopus 로고
    • Dlg protein is required for junction structure, cell polarity, and proliferation control in Drosophila epithelia
    • Woods DF, Hough C, Peel D, Callaini G, Bryant PJ: Dlg protein is required for junction structure, cell polarity, and proliferation control in Drosophila epithelia. J Cell Biol 1996, 134:1469-1482.
    • (1996) J Cell Biol , vol.134 , pp. 1469-1482
    • Woods, D.F.1    Hough, C.2    Peel, D.3    Callaini, G.4    Bryant, P.J.5
  • 31
    • 0026572318 scopus 로고
    • Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src
    • Seidel-Dugan C, Meyer BE, Thomas SM, Brugge, JS: Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src. Mol Cell Biol 1992, 12:1835-1845.
    • (1992) Mol Cell Biol , vol.12 , pp. 1835-1845
    • Seidel-Dugan, C.1    Meyer, B.E.2    Thomas, S.M.3    Brugge, J.S.4
  • 32
    • 0024461553 scopus 로고
    • Deletion of an N-terminal regulatory domain of the c-abl tyrosine kinase activates its oncogenic potential
    • Franz WM, Berger P, Wang JYJ: Deletion of an N-terminal regulatory domain of the c-abl tyrosine kinase activates its oncogenic potential. EMBO J 1989, 8:137-147.
    • (1989) EMBO J , vol.8 , pp. 137-147
    • Franz, W.M.1    Berger, P.2    Wang, J.Y.J.3
  • 33
    • 0031052970 scopus 로고    scopus 로고
    • GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules
    • Kim E, Naisbitt S, Hsueh YP, Rao A, Rothschild A, Craig AM, Sheng M: GKAP, a novel synaptic protein that interacts with the guanylate kinase-like domain of the PSD-95/SAP90 family of channel clustering molecules. J Cell Biol 1997, 136:669-678.
    • (1997) J Cell Biol , vol.136 , pp. 669-678
    • Kim, E.1    Naisbitt, S.2    Hsueh, Y.P.3    Rao, A.4    Rothschild, A.5    Craig, A.M.6    Sheng, M.7
  • 34
    • 0030957966 scopus 로고    scopus 로고
    • SAPAPs: A family of PSD-95/SAP90-associated proteins localized at postsynaptic density
    • Takeuchi M, Hata Y, Hirao K, Toyoda A, Irie M, Takai Y: SAPAPs: a family of PSD-95/SAP90-associated proteins localized at postsynaptic density. J Biol Chem 1997, 272:11943-11951.
    • (1997) J Biol Chem , vol.272 , pp. 11943-11951
    • Takeuchi, M.1    Hata, Y.2    Hirao, K.3    Toyoda, A.4    Irie, M.5    Takai, Y.6
  • 35
    • 0030067804 scopus 로고    scopus 로고
    • The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins
    • Hoskins R, Hajnal AF, Harp SA, Kim SA.: The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK family of cell junction proteins. Development 1996, 122:97-111.
    • (1996) Development , vol.122 , pp. 97-111
    • Hoskins, R.1    Hajnal, A.F.2    Harp, S.A.3    Kim, S.A.4
  • 36
    • 0028906288 scopus 로고
    • Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs large tumor suppressor protein
    • Muller BM, Kistner U, Veh RW, Cases-Langhoff C, Becker B, Gundelfinger ED, Garner CC: Molecular characterization and spatial distribution of SAP97, a novel presynaptic protein homologous to SAP90 and the Drosophila discs large tumor suppressor protein. J Neuroscience 1995, 15:2354-2366.
    • (1995) J Neuroscience , vol.15 , pp. 2354-2366
    • Muller, B.M.1    Kistner, U.2    Veh, R.W.3    Cases-Langhoff, C.4    Becker, B.5    Gundelfinger, E.D.6    Garner, C.C.7
  • 37
    • 0030776844 scopus 로고    scopus 로고
    • Human homologue of the Drosophila discs large tumor suppressor binds to p56lck tyrosine kinase and Shaker type Kv1.3 potassium channel in T lymphocytes
    • lck tyrosine kinase is demonstrated. This paper also shows in vivo association between hDlg and Kv1.3 channel, and it suggests a novel mechanism in coupling tyrosine kinase and voltage-gated potassium channel in T lymphocytes.
    • (1997) J Biol Chem , vol.272 , pp. 26899-26904
    • Hanada, T.1    Lin, L.2    Chandy, K.G.3    Oh, S.S.4    Chishti, A.H.5
  • 38
    • 0029851093 scopus 로고    scopus 로고
    • Modular organization of the PDZ domains in the human discs large protein suggests a mechanism for coupling PDZ domain binding proteins to ATP and the membrane cytoskeleton
    • Marfatia SM, Morais-Cabral JH, Lin L, Hough C, Bryant PJ, Stolz L, Chishti AH: Modular organization of the PDZ domains in the human discs large protein suggests a mechanism for coupling PDZ domain binding proteins to ATP and the membrane cytoskeleton. J Cell Biol 1996, 135:753-766.
    • (1996) J Cell Biol , vol.135 , pp. 753-766
    • Marfatia, S.M.1    Morais-Cabral, J.H.2    Lin, L.3    Hough, C.4    Bryant, P.J.5    Stolz, L.6    Chishti, A.H.7
  • 39
    • 0029846832 scopus 로고    scopus 로고
    • Two independent domains of hDlg are sufficient for subcellular targeting: The PDZ1-2 conformational unit and an alternatively spliced domain
    • Lue RA, Brandin E, Chan EP, Branton D: Two independent domains of hDlg are sufficient for subcellular targeting: the PDZ1-2 conformational unit and an alternatively spliced domain. J Cell Biol 1996, 135:1125-1137.
    • (1996) J Cell Biol , vol.135 , pp. 1125-1137
    • Lue, R.A.1    Brandin, E.2    Chan, E.P.3    Branton, D.4
  • 41
    • 0030950410 scopus 로고    scopus 로고
    • Binding of human virus oncoproteins to hDlg/SAP97, a mammalian homolog of the Drosophila discs large tumor suppressor protein
    • Lee SS, Weiss RS, Javier RT: Binding of human virus oncoproteins to hDlg/SAP97, a mammalian homolog of the Drosophila discs large tumor suppressor protein. Proc Natl Acad Sci U S A 1997, 94:6670-6675. PDZ domain-mediated binding of hDlg with several viral oncoproteins is demonstrated. The viral proteins include adenovirus E4 oncoprotein, HTLV-1 tax protein, and human papillomavirus-18 E6 protein. These findings suggested that interactions with the hDlg may contribute to the tumorigenic potentials of several different human virus oncoproteins.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 6670-6675
    • Lee, S.S.1    Weiss, R.S.2    Javier, R.T.3
  • 42
    • 0026864937 scopus 로고
    • The gene encoding the palmitoylated erythrocyte membrane protein, p55, originates at the CpG island 3' to the factor VIII gene
    • Metzenberg AB, Gitschier J: The gene encoding the palmitoylated erythrocyte membrane protein, p55, originates at the CpG island 3' to the factor VIII gene. Hum Mol Genet 1992, 1:97-101.
    • (1992) Hum Mol Genet , vol.1 , pp. 97-101
    • Metzenberg, A.B.1    Gitschier, J.2
  • 43
    • 0030046846 scopus 로고    scopus 로고
    • Complete genomic organization of the human erythroid p55 gene (MPP1), a membrane-associated guanylate kinase homologue
    • Kim AC, Metzenberg AB, Sahr KE, Marfatia SM, Chishti AH: Complete genomic organization of the human erythroid p55 gene (MPP1), a membrane-associated guanylate kinase homologue. Genomics 1996, 31:223-229.
    • (1996) Genomics , vol.31 , pp. 223-229
    • Kim, A.C.1    Metzenberg, A.B.2    Sahr, K.E.3    Marfatia, S.M.4    Chishti, A.H.5


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