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Volumn 77, Issue , 2016, Pages 143-184

An Adaptable Spectrin/Ankyrin-Based Mechanism for Long-Range Organization of Plasma Membranes in Vertebrate Tissues

Author keywords

ANK repeat; Ankyrin; Axon; Axon initial segment; Costamere; Evolution; Intrinsically unstructured protein; Membrane spanning protein; Node of Ranvier; Palmitoylation; Plasma membrane; Spectrin

Indexed keywords

ANKYRIN; SPECTRIN;

EID: 84948846007     PISSN: 10635823     EISSN: None     Source Type: Book Series    
DOI: 10.1016/bs.ctm.2015.10.001     Document Type: Article
Times cited : (68)

References (185)
  • 1
    • 39449083242 scopus 로고    scopus 로고
    • Adducin promotes micrometer-scale organization of beta2-spectrin in lateral membranes of bronchial epithelial cells
    • Abdi, K.M., Bennett, V., Adducin promotes micrometer-scale organization of beta2-spectrin in lateral membranes of bronchial epithelial cells. Molecular Biology of the Cell 19:2 (2008), 536–545.
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.2 , pp. 536-545
    • Abdi, K.M.1    Bennett, V.2
  • 2
    • 33646830169 scopus 로고    scopus 로고
    • Isoform specificity of ankyrin-B: a site in the divergent C-terminal domain is required for intramolecular association
    • Abdi, K.M., Mohler, P.J., Davis, J.Q., Bennett, V., Isoform specificity of ankyrin-B: a site in the divergent C-terminal domain is required for intramolecular association. Journal of Biological Chemistry 281:9 (2006), 5741–5749.
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.9 , pp. 5741-5749
    • Abdi, K.M.1    Mohler, P.J.2    Davis, J.Q.3    Bennett, V.4
  • 3
    • 0021914750 scopus 로고
    • Partial deficiency of erythrocyte spectrin in hereditary spherocytosis
    • Agre, P., Casella, J.F., Zinkham, W.H., McMillan, C., Bennett, V., Partial deficiency of erythrocyte spectrin in hereditary spherocytosis. Nature 314:6009 (1985), 380–383.
    • (1985) Nature , vol.314 , Issue.6009 , pp. 380-383
    • Agre, P.1    Casella, J.F.2    Zinkham, W.H.3    McMillan, C.4    Bennett, V.5
  • 4
    • 0020083327 scopus 로고
    • Deficient red-cell spectrin in severe, recessively inherited spherocytosis
    • Agre, P., Orringer, E.P., Bennett, V., Deficient red-cell spectrin in severe, recessively inherited spherocytosis. The New England Journal of Medicine 306:19 (1982), 1155–1161.
    • (1982) The New England Journal of Medicine , vol.306 , Issue.19 , pp. 1155-1161
    • Agre, P.1    Orringer, E.P.2    Bennett, V.3
  • 6
    • 57649234553 scopus 로고    scopus 로고
    • An ankyrin-based mechanism for functional organization of dystrophin and dystroglycan
    • Ayalon, G., Davis, J.Q., Scotland, P.B., Bennett, V., An ankyrin-based mechanism for functional organization of dystrophin and dystroglycan. Cell 135:7 (2008), 1189–1200.
    • (2008) Cell , vol.135 , Issue.7 , pp. 1189-1200
    • Ayalon, G.1    Davis, J.Q.2    Scotland, P.B.3    Bennett, V.4
  • 7
    • 79953192175 scopus 로고    scopus 로고
    • Ankyrin-B interactions with spectrin and dynactin-4 are required for dystrophin-based protection of skeletal muscle from exercise injury
    • Ayalon, G., Hostettler, J.D., Hoffman, J., Kizhatil, K., Davis, J.Q., Bennett, V., Ankyrin-B interactions with spectrin and dynactin-4 are required for dystrophin-based protection of skeletal muscle from exercise injury. Journal of Biological Chemistry 286:9 (2011), 7370–7378.
    • (2011) Journal of Biological Chemistry , vol.286 , Issue.9 , pp. 7370-7378
    • Ayalon, G.1    Hostettler, J.D.2    Hoffman, J.3    Kizhatil, K.4    Davis, J.Q.5    Bennett, V.6
  • 8
    • 77955769377 scopus 로고    scopus 로고
    • The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life
    • Baines, A.J., The spectrin-ankyrin-4.1-adducin membrane skeleton: adapting eukaryotic cells to the demands of animal life. Protoplasma 244 (2010), 99–131.
    • (2010) Protoplasma , vol.244 , pp. 99-131
    • Baines, A.J.1
  • 9
    • 84892158141 scopus 로고    scopus 로고
    • The Protein 4.1 family: hub proteins in animals for organizing membrane proteins
    • February
    • Baines, A.J., Lu, H.C., Bennett, P.M., The Protein 4.1 family: hub proteins in animals for organizing membrane proteins. Biochimica et Biophysica Acta 1838:2 (February 2014), 605–619.
    • (2014) Biochimica et Biophysica Acta , vol.1838 , Issue.2 , pp. 605-619
    • Baines, A.J.1    Lu, H.C.2    Bennett, P.M.3
  • 10
    • 0032533444 scopus 로고    scopus 로고
    • Structural comparisons of calponin homology domains: implications for actin binding
    • Banuelos, S., Saraste, M., Carugo, K.D., Structural comparisons of calponin homology domains: implications for actin binding. Structure 6 (1998), 1419–1431.
    • (1998) Structure , vol.6 , pp. 1419-1431
    • Banuelos, S.1    Saraste, M.2    Carugo, K.D.3
  • 11
    • 0033832265 scopus 로고    scopus 로고
    • Amelioration of severe hereditary spherocytosis in nonablated adult mice by marrow transplantation
    • Barker, J.E., Deveau, S., Wandersee, N.J., Amelioration of severe hereditary spherocytosis in nonablated adult mice by marrow transplantation. Experimental Hematology 28:8 (2000), 985–992.
    • (2000) Experimental Hematology , vol.28 , Issue.8 , pp. 985-992
    • Barker, J.E.1    Deveau, S.2    Wandersee, N.J.3
  • 13
    • 0035140976 scopus 로고    scopus 로고
    • Ankyrins and cellular targeting of diverse membrane proteins to physiological sites
    • Bennett, V., Chen, L., Ankyrins and cellular targeting of diverse membrane proteins to physiological sites. Current Opinion in Cell Biology 13:1 (2001), 61–67.
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.1 , pp. 61-67
    • Bennett, V.1    Chen, L.2
  • 14
    • 0019971525 scopus 로고
    • Brain spectrin, a membrane-associated protein related in structure and function to erythrocyte spectrin
    • Bennett, V., Davis, J., Fowler, W.E., Brain spectrin, a membrane-associated protein related in structure and function to erythrocyte spectrin. Nature 299:5879 (1982), 126–131.
    • (1982) Nature , vol.299 , Issue.5879 , pp. 126-131
    • Bennett, V.1    Davis, J.2    Fowler, W.E.3
  • 15
    • 0023880432 scopus 로고
    • Brain adducin: a protein kinase C substrate that may mediate site-directed assembly at the spectrin-actin junction
    • Bennett, V., Gardner, K., Steiner, J.P., Brain adducin: a protein kinase C substrate that may mediate site-directed assembly at the spectrin-actin junction. Journal of Biological Chemistry 263:12 (1988), 5860–5869.
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.12 , pp. 5860-5869
    • Bennett, V.1    Gardner, K.2    Steiner, J.P.3
  • 16
    • 77955882462 scopus 로고    scopus 로고
    • Membrane domains based on ankyrin and spectrin associated with cell–cell interactions
    • Bennett, V., Healy, J., Membrane domains based on ankyrin and spectrin associated with cell–cell interactions. Cold Spring Harbor Perspectives in Biology, 1(6), 2009, a003012.
    • (2009) Cold Spring Harbor Perspectives in Biology , vol.1 , Issue.6 , pp. a003012
    • Bennett, V.1    Healy, J.2
  • 17
    • 84887196254 scopus 로고    scopus 로고
    • Spectrin- and ankyrin-based membrane domains and the evolution of vertebrates
    • Bennett, V., Lorenzo, D.N., Spectrin- and ankyrin-based membrane domains and the evolution of vertebrates. Current Topics in Membranes 72 (2013), 1–37.
    • (2013) Current Topics in Membranes , vol.72 , pp. 1-37
    • Bennett, V.1    Lorenzo, D.N.2
  • 18
    • 0018759538 scopus 로고
    • The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes
    • Bennett, V., Stenbuck, P.J., The membrane attachment protein for spectrin is associated with band 3 in human erythrocyte membranes. Nature 280:5722 (1979), 468–473.
    • (1979) Nature , vol.280 , Issue.5722 , pp. 468-473
    • Bennett, V.1    Stenbuck, P.J.2
  • 19
    • 0018397366 scopus 로고
    • Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin
    • April 10
    • Bennett, V., Stenbuck, P.J., Identification and partial purification of ankyrin, the high affinity membrane attachment site for human erythrocyte spectrin. Journal of Biological Chemistry 254:7 (April 10, 1979), 2533–2541.
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.7 , pp. 2533-2541
    • Bennett, V.1    Stenbuck, P.J.2
  • 20
    • 0019321291 scopus 로고
    • Association between ankyrin and the cytoplasmic domain of band 3 isolated from the human erythrocyte membrane
    • Bennett, V., Stenbuck, P.J., Association between ankyrin and the cytoplasmic domain of band 3 isolated from the human erythrocyte membrane. Journal of Biological Chemistry 255:13 (1980), 6424–6432.
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.13 , pp. 6424-6432
    • Bennett, V.1    Stenbuck, P.J.2
  • 21
    • 0019309226 scopus 로고
    • Human erythrocyte ankyrin. Purification and properties
    • Bennett, V., Stenbuck, P.J., Human erythrocyte ankyrin. Purification and properties. Journal of Biological Chemistry 255 (1980), 2540–2548.
    • (1980) Journal of Biological Chemistry , vol.255 , pp. 2540-2548
    • Bennett, V.1    Stenbuck, P.J.2
  • 22
    • 84926308183 scopus 로고    scopus 로고
    • Evolution in action: giant ankyrins awake
    • Bennett, V., Walder, K., Evolution in action: giant ankyrins awake. Developmental Cell 33:1 (2015), 1–2.
    • (2015) Developmental Cell , vol.33 , Issue.1 , pp. 1-2
    • Bennett, V.1    Walder, K.2
  • 23
    • 0034722147 scopus 로고    scopus 로고
    • βIV spectrin, a new spectrin localized at axon initial segments and nodes of ranvier in the central and peripheral nervous system
    • Berghs, S., Aggujaro, D., Dirkx, R. Jr., Maksimova, E., Stabach, P., Hermel, J.M., et al. βIV spectrin, a new spectrin localized at axon initial segments and nodes of ranvier in the central and peripheral nervous system. Journal of Cell Biology 151 (2000), 985–1002.
    • (2000) Journal of Cell Biology , vol.151 , pp. 985-1002
    • Berghs, S.1    Aggujaro, D.2    Dirkx, R.3    Maksimova, E.4    Stabach, P.5    Hermel, J.M.6
  • 24
    • 0021704597 scopus 로고
    • Spectrin deficient inherited hemolytic anemias in the mouse: characterization by spectrin synthesis and mRNA activity in reticulocytes
    • Bodine, D.M. 4th, Birkenmeier, C.S., Barker, J.E., Spectrin deficient inherited hemolytic anemias in the mouse: characterization by spectrin synthesis and mRNA activity in reticulocytes. Cell 37:3 (1984), 721–729.
    • (1984) Cell , vol.37 , Issue.3 , pp. 721-729
    • Bodine, D.M.1    Birkenmeier, C.S.2    Barker, J.E.3
  • 27
    • 33244457068 scopus 로고    scopus 로고
    • Molecular evolution of the ankyrin gene family
    • March
    • Cai, X., Zhang, Y., Molecular evolution of the ankyrin gene family. Molecular Biology and Evolution 23:3 (March 2006), 550–558.
    • (2006) Molecular Biology and Evolution , vol.23 , Issue.3 , pp. 550-558
    • Cai, X.1    Zhang, Y.2
  • 29
    • 0027729564 scopus 로고
    • 440-kD ankyrinB: structure of the major developmentally regulated domain and selective localization in unmyelinated axons
    • Chan, W., Kordeli, E., Bennett, V., 440-kD ankyrinB: structure of the major developmentally regulated domain and selective localization in unmyelinated axons. Journal of Cell Biology 123 (1993), 1463–1473.
    • (1993) Journal of Cell Biology , vol.123 , pp. 1463-1473
    • Chan, W.1    Kordeli, E.2    Bennett, V.3
  • 31
    • 0037470168 scopus 로고    scopus 로고
    • Identification of a critical ankyrin-binding loop on the cytoplasmic domain of erythrocyte membrane band 3 by crystal structure analysis and site-directed mutagenesis
    • Chang, S.H., Low, P.S., Identification of a critical ankyrin-binding loop on the cytoplasmic domain of erythrocyte membrane band 3 by crystal structure analysis and site-directed mutagenesis. Journal of Biological Chemistry 278 (2003), 6879–6884.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 6879-6884
    • Chang, S.H.1    Low, P.S.2
  • 32
    • 0035921416 scopus 로고    scopus 로고
    • LAD-1, the Caenorhabditis elegans L1CAM homologue, participates in embryonic and gonadal morphogenesis and is a substrate for fibroblast growth factor receptor pathway-dependent phosphotyrosine-based signaling
    • Chen, L., Ong, B., Bennett, V., LAD-1, the Caenorhabditis elegans L1CAM homologue, participates in embryonic and gonadal morphogenesis and is a substrate for fibroblast growth factor receptor pathway-dependent phosphotyrosine-based signaling. Journal of Cell Biology 154 (2001), 841–855.
    • (2001) Journal of Cell Biology , vol.154 , pp. 841-855
    • Chen, L.1    Ong, B.2    Bennett, V.3
  • 33
    • 55649115607 scopus 로고    scopus 로고
    • Exon organization and novel alternative splicing of the human ANK2 gene: implications for cardiac function and human cardiac disease
    • Cunha, S.R., Le Scouarnec, S., Schott, J.J., Mohler, P.J., Exon organization and novel alternative splicing of the human ANK2 gene: implications for cardiac function and human cardiac disease. Journal of Molecular and Cellular Cardiology 45 (2008), 724–734.
    • (2008) Journal of Molecular and Cellular Cardiology , vol.45 , pp. 724-734
    • Cunha, S.R.1    Le Scouarnec, S.2    Schott, J.J.3    Mohler, P.J.4
  • 34
    • 57649129419 scopus 로고    scopus 로고
    • Obscurin targets ankyrin-B and protein phosphatase 2A to the cardiac M-line
    • Cunha, S.R., Mohler, P.J., Obscurin targets ankyrin-B and protein phosphatase 2A to the cardiac M-line. Journal of Biological Chemistry 283 (2008), 31968–31980.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 31968-31980
    • Cunha, S.R.1    Mohler, P.J.2
  • 35
    • 84903131157 scopus 로고    scopus 로고
    • EHD3-dependent endosome pathway regulates cardiac membrane excitability and physiology
    • Curran, J., Makara, M.A., Little, S.C., Musa, H., Liu, B., Wu, X., et al. EHD3-dependent endosome pathway regulates cardiac membrane excitability and physiology. Circulation Research 115:1 (2014), 68–78.
    • (2014) Circulation Research , vol.115 , Issue.1 , pp. 68-78
    • Curran, J.1    Makara, M.A.2    Little, S.C.3    Musa, H.4    Liu, B.5    Wu, X.6
  • 36
    • 45549099883 scopus 로고    scopus 로고
    • Unexpected complexity in the mechanisms that target assembly of the spectrin cytoskeleton
    • Das, A., Base, C., Manna, D., Cho, W., Dubreuil, R.R., Unexpected complexity in the mechanisms that target assembly of the spectrin cytoskeleton. Journal of Biological Chemistry 283:18 (2008), 12643–12653.
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.18 , pp. 12643-12653
    • Das, A.1    Base, C.2    Manna, D.3    Cho, W.4    Dubreuil, R.R.5
  • 37
    • 35349007899 scopus 로고    scopus 로고
    • Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling
    • Daumke, O., Lundmark, R., Vallis, Y., Martens, S., Butler, P.J., McMahon, H.T., Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling. Nature 449 (2007), 923–927.
    • (2007) Nature , vol.449 , pp. 923-927
    • Daumke, O.1    Lundmark, R.2    Vallis, Y.3    Martens, S.4    Butler, P.J.5    McMahon, H.T.6
  • 38
    • 0020555463 scopus 로고
    • Brain spectrin. Isolation of subunits and formation of hybrids with erythrocyte spectrin subunits
    • Davis, J., Bennett, V., Brain spectrin. Isolation of subunits and formation of hybrids with erythrocyte spectrin subunits. Journal of Biological Chemistry 258 (1983), 7757–7766.
    • (1983) Journal of Biological Chemistry , vol.258 , pp. 7757-7766
    • Davis, J.1    Bennett, V.2
  • 39
    • 0021689392 scopus 로고
    • Brain ankyrin. A membrane-associated protein with binding sites for spectrin, tubulin, and the cytoplasmic domain of the erythrocyte anion channel
    • Davis, J.Q., Bennett, V., Brain ankyrin. A membrane-associated protein with binding sites for spectrin, tubulin, and the cytoplasmic domain of the erythrocyte anion channel. Journal of Biological Chemistry 259 (1984), 13550–13559.
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 13550-13559
    • Davis, J.Q.1    Bennett, V.2
  • 40
    • 0030443956 scopus 로고    scopus 로고
    • Molecular composition of the node of Ranvier: identification of ankyrin-binding cell adhesion molecules neurofascin (mucin+/third FNIII domain−) and NrCAM at nodal axon segments
    • Davis, J.Q., Lambert, S., Bennett, V., Molecular composition of the node of Ranvier: identification of ankyrin-binding cell adhesion molecules neurofascin (mucin+/third FNIII domain−) and NrCAM at nodal axon segments. Journal of Cell Biology 135 (1996), 1355–1367.
    • (1996) Journal of Cell Biology , vol.135 , pp. 1355-1367
    • Davis, J.Q.1    Lambert, S.2    Bennett, V.3
  • 42
    • 0026722207 scopus 로고
    • Ankyrin regulation: an alternatively spliced segment of the regulatory domain functions as an intramolecular modulator
    • Davis, L.H., Davis, J.Q., Bennett, V., Ankyrin regulation: an alternatively spliced segment of the regulatory domain functions as an intramolecular modulator. Journal of Biological Chemistry 267 (1992), 18966–18972.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 18966-18972
    • Davis, L.H.1    Davis, J.Q.2    Bennett, V.3
  • 43
    • 0030480422 scopus 로고    scopus 로고
    • Alpha-spectrin is required for germline cell division and differentiation in the Drosophila ovary
    • De Cuevas, M., Lee, J.K., Spradling, A.C., Alpha-spectrin is required for germline cell division and differentiation in the Drosophila ovary. Development 122 (1996), 3959–3968.
    • (1996) Development , vol.122 , pp. 3959-3968
    • De Cuevas, M.1    Lee, J.K.2    Spradling, A.C.3
  • 44
    • 84912144889 scopus 로고    scopus 로고
    • Synaptic, transcriptional and chromatin genes disrupted in autism
    • De Rubeis, S., He, X., Goldberg, A.P., Poultney, C.S., Samocha, K., Cicek, A.E., et al. Synaptic, transcriptional and chromatin genes disrupted in autism. Nature 515:7526 (2014), 209–215.
    • (2014) Nature , vol.515 , Issue.7526 , pp. 209-215
    • De Rubeis, S.1    He, X.2    Goldberg, A.P.3    Poultney, C.S.4    Samocha, K.5    Cicek, A.E.6
  • 45
    • 0033588277 scopus 로고    scopus 로고
    • Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments
    • Djinovic-Carugo, K., Young, P., Gautel, M., Saraste, M., Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments. Cell 98 (1999), 537–546.
    • (1999) Cell , vol.98 , pp. 537-546
    • Djinovic-Carugo, K.1    Young, P.2    Gautel, M.3    Saraste, M.4
  • 46
  • 47
    • 34249896927 scopus 로고    scopus 로고
    • Nodes of Ranvier and axon initial segments are ankyrin G-dependent domains that assemble by distinct mechanisms
    • Dzhashiashvili, Y., Zhang, Y., Galinska, J., Lam, I., Grumet, M., Salzer, J.L., Nodes of Ranvier and axon initial segments are ankyrin G-dependent domains that assemble by distinct mechanisms. Journal of Cell Biology 177 (2007), 857–870.
    • (2007) Journal of Cell Biology , vol.177 , pp. 857-870
    • Dzhashiashvili, Y.1    Zhang, Y.2    Galinska, J.3    Lam, I.4    Grumet, M.5    Salzer, J.L.6
  • 48
    • 1942509531 scopus 로고    scopus 로고
    • Hereditary spherocytosis–defects in proteins that connect the membrane skeleton to the lipid bilayer
    • Eber, S., Lux, S.E., Hereditary spherocytosis–defects in proteins that connect the membrane skeleton to the lipid bilayer. Seminars in Hematology 41 (2004), 118–141.
    • (2004) Seminars in Hematology , vol.41 , pp. 118-141
    • Eber, S.1    Lux, S.E.2
  • 49
    • 84877000448 scopus 로고    scopus 로고
    • Transsynaptic coordination of synaptic growth, function, and stability by the L1-type CAM Neuroglian
    • Enneking, E.M., Kudumala, S.R., Moreno, E., Stephan, R., Boerner, J., Godenschwege, T.A., et al. Transsynaptic coordination of synaptic growth, function, and stability by the L1-type CAM Neuroglian. PLoS Biology, 11, 2013, e1001537.
    • (2013) PLoS Biology , vol.11 , pp. e1001537
    • Enneking, E.M.1    Kudumala, S.R.2    Moreno, E.3    Stephan, R.4    Boerner, J.5    Godenschwege, T.A.6
  • 50
    • 0024708031 scopus 로고
    • + channels and ankyrin in neuromuscular junctions is complementary to that of acetylcholine receptors and the 43 kd protein
    • + channels and ankyrin in neuromuscular junctions is complementary to that of acetylcholine receptors and the 43 kd protein. Neuron 3:2 (1989), 163–175.
    • (1989) Neuron , vol.3 , Issue.2 , pp. 163-175
    • Flucher, B.E.1    Daniels, M.P.2
  • 51
    • 84887185966 scopus 로고    scopus 로고
    • The human erythrocyte plasma membrane: a Rosetta Stone for decoding membrane-cytoskeleton structure
    • Fowler, V.M., The human erythrocyte plasma membrane: a Rosetta Stone for decoding membrane-cytoskeleton structure. Current Topics in Membranes 72 (2013), 39–88.
    • (2013) Current Topics in Membranes , vol.72 , pp. 39-88
    • Fowler, V.M.1
  • 52
    • 0018085699 scopus 로고
    • Association of spectrin with its membrane attachment site restricts lateral mobility of human erythrocyte integral membrane proteins
    • Fowler, V.M., Bennett, V., Association of spectrin with its membrane attachment site restricts lateral mobility of human erythrocyte integral membrane proteins. Journal of Supramolecular Structure 8 (1978), 215–221.
    • (1978) Journal of Supramolecular Structure , vol.8 , pp. 215-221
    • Fowler, V.M.1    Bennett, V.2
  • 54
    • 0035801351 scopus 로고    scopus 로고
    • Invertebrate connectin spans as much as 3.5 μm in the giant sarcomeres of crayfish claw muscle
    • Fukuzawa, A., Shimamura, J., Takemori, S., Kanzawa, N., Yamaguchi, M., Sun, P., et al. Invertebrate connectin spans as much as 3.5 μm in the giant sarcomeres of crayfish claw muscle. EMBO Journal 20:17 (2001), 4826–4835.
    • (2001) EMBO Journal , vol.20 , Issue.17 , pp. 4826-4835
    • Fukuzawa, A.1    Shimamura, J.2    Takemori, S.3    Kanzawa, N.4    Yamaguchi, M.5    Sun, P.6
  • 55
    • 77953543377 scopus 로고    scopus 로고
    • The Beclin 1-VPS34 complex–at the crossroads of autophagy and beyond
    • Funderburk, S.F., Wang, Q.J., Yue, Z., The Beclin 1-VPS34 complex–at the crossroads of autophagy and beyond. Trends in Cell Biology 20:6 (2010), 355–362.
    • (2010) Trends in Cell Biology , vol.20 , Issue.6 , pp. 355-362
    • Funderburk, S.F.1    Wang, Q.J.2    Yue, Z.3
  • 56
    • 81255195587 scopus 로고    scopus 로고
    • β-III spectrin is critical for development of purkinje cell dendritic tree and spine morphogenesis
    • Gao, Y., Perkins, E.M., Clarkson, Y.L., Tobia, S., Lyndon, A.R., Jackson, M., et al. β-III spectrin is critical for development of purkinje cell dendritic tree and spine morphogenesis. Journal of Neuroscience 31 (2011), 16581–16590.
    • (2011) Journal of Neuroscience , vol.31 , pp. 16581-16590
    • Gao, Y.1    Perkins, E.M.2    Clarkson, Y.L.3    Tobia, S.4    Lyndon, A.R.5    Jackson, M.6
  • 58
    • 0023245565 scopus 로고
    • Modulation of spectrin-actin assembly by erythrocyte adducin
    • Gardner, K., Bennett, V., Modulation of spectrin-actin assembly by erythrocyte adducin. Nature 328:6128 (1987), 359–362.
    • (1987) Nature , vol.328 , Issue.6128 , pp. 359-362
    • Gardner, K.1    Bennett, V.2
  • 59
    • 0038270765 scopus 로고    scopus 로고
    • A targeting motif involved in sodium channel clustering at the axonal initial segment
    • Garrido, J.J., Giraud, P., Carlier, E., Fernandes, F., Moussif, A., Fache, M.P., et al. A targeting motif involved in sodium channel clustering at the axonal initial segment. Science 300:5628 (2003), 2091–2094.
    • (2003) Science , vol.300 , Issue.5628 , pp. 2091-2094
    • Garrido, J.J.1    Giraud, P.2    Carlier, E.3    Fernandes, F.4    Moussif, A.5    Fache, M.P.6
  • 60
    • 84924873138 scopus 로고    scopus 로고
    • Evidence of a structural and functional ammonium transporter RhBG/anion exchanger 1/ankyrin-G complex in kidney epithelial cells
    • Genetet, S., Ripoche, P., Le Van Kim, C., Colin, Y., Lopez, C., Evidence of a structural and functional ammonium transporter RhBG/anion exchanger 1/ankyrin-G complex in kidney epithelial cells. Journal of Biological Chemistry 290:11 (2015), 6925–6936.
    • (2015) Journal of Biological Chemistry , vol.290 , Issue.11 , pp. 6925-6936
    • Genetet, S.1    Ripoche, P.2    Le Van Kim, C.3    Colin, Y.4    Lopez, C.5
  • 62
    • 0019190475 scopus 로고
    • Lateral mobility of band 3 in the human erythrocyte membrane studied by fluorescence photobleaching recovery: evidence for control by cytoskeletal interactions
    • Golan, D.E., Veatch, W., Lateral mobility of band 3 in the human erythrocyte membrane studied by fluorescence photobleaching recovery: evidence for control by cytoskeletal interactions. Proceedings of the National Academy of Sciences of the United States of America 77:5 (1980), 2537–2541.
    • (1980) Proceedings of the National Academy of Sciences of the United States of America , vol.77 , Issue.5 , pp. 2537-2541
    • Golan, D.E.1    Veatch, W.2
  • 63
    • 84867546627 scopus 로고    scopus 로고
    • Identification of contact sites between ankyrin and band 3 in the human erythrocyte membrane
    • Grey, J.L., Kodippili, G.C., Simon, K., Low, P.S., Identification of contact sites between ankyrin and band 3 in the human erythrocyte membrane. Biochemistry 51 (2012), 6838–6846.
    • (2012) Biochemistry , vol.51 , pp. 6838-6846
    • Grey, J.L.1    Kodippili, G.C.2    Simon, K.3    Low, P.S.4
  • 66
    • 0023196746 scopus 로고
    • Regulatory domains of erythrocyte ankyrin
    • Hall, T.G., Bennett, V., Regulatory domains of erythrocyte ankyrin. Journal of Biological Chemistry 262 (1987), 10537–10545.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 10537-10545
    • Hall, T.G.1    Bennett, V.2
  • 68
    • 0034130363 scopus 로고    scopus 로고
    • Identification of a novel C-terminal variant of beta II spectrin: two isoforms of beta II spectrin have distinct intracellular locations and activities
    • Hayes, N.V., Scott, C., Heerkens, E., Ohanian, V., Maggs, A.M., Pinder, J.C., et al. Identification of a novel C-terminal variant of beta II spectrin: two isoforms of beta II spectrin have distinct intracellular locations and activities. Journal of Cell Science J113 (2000), 2023–2034.
    • (2000) Journal of Cell Science , vol.J113 , pp. 2023-2034
    • Hayes, N.V.1    Scott, C.2    Heerkens, E.3    Ohanian, V.4    Maggs, A.M.5    Pinder, J.C.6
  • 69
    • 84904645592 scopus 로고    scopus 로고
    • Ankyrin-G palmitoylation and βII-spectrin binding to phosphoinositide lipids drive lateral membrane assembly
    • July 21
    • He, M., Abdi, K.M., Bennett, V., Ankyrin-G palmitoylation and βII-spectrin binding to phosphoinositide lipids drive lateral membrane assembly. Journal of Cell Biology 206:2 (July 21, 2014), 273–288.
    • (2014) Journal of Cell Biology , vol.206 , Issue.2 , pp. 273-288
    • He, M.1    Abdi, K.M.2    Bennett, V.3
  • 70
    • 84871565497 scopus 로고    scopus 로고
    • Cysteine 70 of ankyrin-G is S-palmitoylated and is required for function of ankyrin-G in membrane domain assembly
    • He, M., Jenkins, P., Bennett, V., Cysteine 70 of ankyrin-G is S-palmitoylated and is required for function of ankyrin-G in membrane domain assembly. Journal of Biological Chemistry 287:52 (2012), 43995–44005.
    • (2012) Journal of Biological Chemistry , vol.287 , Issue.52 , pp. 43995-44005
    • He, M.1    Jenkins, P.2    Bennett, V.3
  • 71
    • 84878214874 scopus 로고    scopus 로고
    • A single divergent exon inhibits ankyrin-B association with the plasma membrane
    • He, M., Tseng, W.C., Bennett, V., A single divergent exon inhibits ankyrin-B association with the plasma membrane. Journal of Biological Chemistry 288:21 (2013), 14769–14779.
    • (2013) Journal of Biological Chemistry , vol.288 , Issue.21 , pp. 14769-14779
    • He, M.1    Tseng, W.C.2    Bennett, V.3
  • 72
    • 58149185390 scopus 로고    scopus 로고
    • AnkyrinG is required for maintenance of the axon initial segment and neuronal polarity
    • Hedstrom, K.L., Ogawa, Y., Rasband, M.N., AnkyrinG is required for maintenance of the axon initial segment and neuronal polarity. Journal of Cell Biology 183 (2008), 635–640.
    • (2008) Journal of Cell Biology , vol.183 , pp. 635-640
    • Hedstrom, K.L.1    Ogawa, Y.2    Rasband, M.N.3
  • 73
    • 58149144729 scopus 로고    scopus 로고
    • Ion channel clustering at the axon initial segment and node of Ranvier evolved sequentially in early chordates
    • Hill, A.S., Nishino, A., Nakajo, K., Zhang, G., Fineman, J.R., Selzer, M.E., et al. Ion channel clustering at the axon initial segment and node of Ranvier evolved sequentially in early chordates. PLoS Genetics, 4(12), 2008, e1000317.
    • (2008) PLoS Genetics , vol.4 , Issue.12 , pp. e1000317
    • Hill, A.S.1    Nishino, A.2    Nakajo, K.3    Zhang, G.4    Fineman, J.R.5    Selzer, M.E.6
  • 74
    • 0030968027 scopus 로고    scopus 로고
    • Isoforms of ankyrin-3 that lack the NH2-terminal repeats associate with mouse macrophage lysosomes
    • Hoock, T.C., Peters, L.L., Lux, S.E., Isoforms of ankyrin-3 that lack the NH2-terminal repeats associate with mouse macrophage lysosomes. Journal of Cell Biology 136 (1997), 1059–1070.
    • (1997) Journal of Cell Biology , vol.136 , pp. 1059-1070
    • Hoock, T.C.1    Peters, L.L.2    Lux, S.E.3
  • 75
    • 28944446876 scopus 로고    scopus 로고
    • Molecular evolution of ankyrin: gain of function in vertebrates by acquisition of an obscurin/titin-binding-related domain
    • Hopitzan, A.A., Baines, A.J., Kordeli, E., Molecular evolution of ankyrin: gain of function in vertebrates by acquisition of an obscurin/titin-binding-related domain. Molecular Biology and Evolution 23 (2006), 46–55.
    • (2006) Molecular Biology and Evolution , vol.23 , pp. 46-55
    • Hopitzan, A.A.1    Baines, A.J.2    Kordeli, E.3
  • 76
    • 23944454910 scopus 로고    scopus 로고
    • Ankyrin-G in skeletal muscle: tissue-specific alternative splicing contributes to the complexity of the sarcolemmal cytoskeleton
    • Hopitzan, A.A., Baines, A.J., Ludosky, M.A., Recouvreur, M., Kordeli, E., Ankyrin-G in skeletal muscle: tissue-specific alternative splicing contributes to the complexity of the sarcolemmal cytoskeleton. Experimental Cell Research S309 (2005), 86–98.
    • (2005) Experimental Cell Research , vol.S309 , pp. 86-98
    • Hopitzan, A.A.1    Baines, A.J.2    Ludosky, M.A.3    Recouvreur, M.4    Kordeli, E.5
  • 77
    • 58949098197 scopus 로고    scopus 로고
    • The interaction between L1-type proteins and ankyrins–a master switch for L1-type CAM function
    • Hortsch, M., Nagaraj, K., Godenschwege, T.A., The interaction between L1-type proteins and ankyrins–a master switch for L1-type CAM function. Cellular and Molecular Biology Letters 14 (2009), 57–69.
    • (2009) Cellular and Molecular Biology Letters , vol.14 , pp. 57-69
    • Hortsch, M.1    Nagaraj, K.2    Godenschwege, T.A.3
  • 78
    • 0026732691 scopus 로고
    • Characterization of human brain cDNA encoding the general isoform of beta-spectrin
    • Hu, R.J., Watanabe, M., Bennett, V., Characterization of human brain cDNA encoding the general isoform of beta-spectrin. Journal of Biological Chemistry 267 (1992), 18715–18722.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 18715-18722
    • Hu, R.J.1    Watanabe, M.2    Bennett, V.3
  • 79
    • 0035853847 scopus 로고    scopus 로고
    • The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover
    • Huber, A.H., Stewart, D.B., Laurents, D.V., Nelson, W.J., Weis, W.I., The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover. Journal of Biological Chemistry 276 (2001), 12301–12309.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 12301-12309
    • Huber, A.H.1    Stewart, D.B.2    Laurents, D.V.3    Nelson, W.J.4    Weis, W.I.5
  • 80
    • 77957838101 scopus 로고    scopus 로고
    • A β(IV)-spectrin/CaMKII signaling complex is essential for membrane excitability in mice
    • Hund, T.J., Koval, O.M., Li, J., Wright, P.J., Qian, L., Snyder, J.S., et al. A β(IV)-spectrin/CaMKII signaling complex is essential for membrane excitability in mice. Journal of Clinical Investigation 120 (2010), 3508–3519.
    • (2010) Journal of Clinical Investigation , vol.120 , pp. 3508-3519
    • Hund, T.J.1    Koval, O.M.2    Li, J.3    Wright, P.J.4    Qian, L.5    Snyder, J.S.6
  • 81
  • 84
    • 84912101541 scopus 로고    scopus 로고
    • The contribution of de novo coding mutations to autism spectrum disorder
    • Iossifov, I., O'Roak, B.J., Sanders, S.J., Ronemus, M., Krumm, N., Levy, D., et al. The contribution of de novo coding mutations to autism spectrum disorder. Nature 515:7526 (2014), 216–221.
    • (2014) Nature , vol.515 , Issue.7526 , pp. 216-221
    • Iossifov, I.1    O'Roak, B.J.2    Sanders, S.J.3    Ronemus, M.4    Krumm, N.5    Levy, D.6
  • 85
    • 77954699179 scopus 로고    scopus 로고
    • Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex
    • Ipsaro, J.J., Harper, S.L., Messick, T.E., Marmorstein, R., Mondragón, A., Speicher, D.W., Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex. Blood 115 (2010), 4843–4852.
    • (2010) Blood , vol.115 , pp. 4843-4852
    • Ipsaro, J.J.1    Harper, S.L.2    Messick, T.E.3    Marmorstein, R.4    Mondragón, A.5    Speicher, D.W.6
  • 86
    • 62549129569 scopus 로고    scopus 로고
    • Structures of the spectrin-ankyrin interaction binding domains
    • Ipsaro, J.J., Huang, L., Mondragón, A., Structures of the spectrin-ankyrin interaction binding domains. Blood 113 (2009), 5385–5393.
    • (2009) Blood , vol.113 , pp. 5385-5393
    • Ipsaro, J.J.1    Huang, L.2    Mondragón, A.3
  • 87
    • 77953239491 scopus 로고    scopus 로고
    • Structural basis for spectrin recognition by ankyrin
    • Ipsaro, J.J., Mondragón, A., Structural basis for spectrin recognition by ankyrin. Blood 115 (2010), 4093–4101.
    • (2010) Blood , vol.115 , pp. 4093-4101
    • Ipsaro, J.J.1    Mondragón, A.2
  • 88
    • 84877045763 scopus 로고    scopus 로고
    • Homozygous and heterozygous disruptions of ANK3: at the crossroads of neurodevelopmental and psychiatric disorders
    • Iqbal, Z., Vandeweyer, G., van der Voet, M., Waryah, A.M., Zahoor, M.Y., Besseling, J.A., et al. Homozygous and heterozygous disruptions of ANK3: at the crossroads of neurodevelopmental and psychiatric disorders. Human Molecular Genetics 22 (2013), 1960–1970.
    • (2013) Human Molecular Genetics , vol.22 , pp. 1960-1970
    • Iqbal, Z.1    Vandeweyer, G.2    van der Voet, M.3    Waryah, A.M.4    Zahoor, M.Y.5    Besseling, J.A.6
  • 89
    • 84954110832 scopus 로고    scopus 로고
    • Motile spectrin/ankyrin-G microdomains promote lateral membrane assembly by opposing endocytosis
    • Sep 11
    • Jenkins, P.M., He, M., Bennett, V., Motile spectrin/ankyrin-G microdomains promote lateral membrane assembly by opposing endocytosis. Sci Adv, 1(8), Sep 11, 2015, e1500301.
    • (2015) Sci Adv , vol.1 , Issue.8 , pp. e1500301
    • Jenkins, P.M.1    He, M.2    Bennett, V.3
  • 91
    • 84877911596 scopus 로고    scopus 로고
    • E-cadherin polarity is determined by a multifunction motif mediating lateral membrane retention through ankyrin-G and apical-lateral transcytosis through clathrin
    • Jenkins, P.M., Vasavda, C., Hostettler, J., Davis, J.Q., Abdi, K., Bennett, V., E-cadherin polarity is determined by a multifunction motif mediating lateral membrane retention through ankyrin-G and apical-lateral transcytosis through clathrin. Journal of Biological Chemistry 288:20 (2013), 14018–14031.
    • (2013) Journal of Biological Chemistry , vol.288 , Issue.20 , pp. 14018-14031
    • Jenkins, P.M.1    Vasavda, C.2    Hostettler, J.3    Davis, J.Q.4    Abdi, K.5    Bennett, V.6
  • 92
    • 0035956420 scopus 로고    scopus 로고
    • Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs at Purkinje neuron initial segments
    • Jenkins, S.M., Bennett, V., Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs at Purkinje neuron initial segments. Journal of Cell Biology 155 (2001), 739–746.
    • (2001) Journal of Cell Biology , vol.155 , pp. 739-746
    • Jenkins, S.M.1    Bennett, V.2
  • 93
    • 84901649742 scopus 로고    scopus 로고
    • Axon initial segment cytoskeleton comprises a multiprotein submembranous coat containing sparse actin filaments
    • Jones, S.L., Korobova, F., Svitkina, T., Axon initial segment cytoskeleton comprises a multiprotein submembranous coat containing sparse actin filaments. Journal of Cell Biology 205:1 (2014), 67–81.
    • (2014) Journal of Cell Biology , vol.205 , Issue.1 , pp. 67-81
    • Jones, S.L.1    Korobova, F.2    Svitkina, T.3
  • 94
    • 62849099990 scopus 로고    scopus 로고
    • Ankyrin-G promotes cyclic nucleotide-gated channel transport to rod photoreceptor sensory cilia
    • Kizhatil, K., Baker, S.A., Arshavsky, V.Y., Bennett, V., Ankyrin-G promotes cyclic nucleotide-gated channel transport to rod photoreceptor sensory cilia. Science 323 (2009), 1614–1617.
    • (2009) Science , vol.323 , pp. 1614-1617
    • Kizhatil, K.1    Baker, S.A.2    Arshavsky, V.Y.3    Bennett, V.4
  • 95
    • 1942533405 scopus 로고    scopus 로고
    • Lateral membrane biogenesis in human bronchial epithelial cells requires 190 kDa Ankyrin-G
    • Kizhatil, K., Bennett, V., Lateral membrane biogenesis in human bronchial epithelial cells requires 190 kDa Ankyrin-G. Journal of Biological Chemistry 279 (2004), 16706–16714.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 16706-16714
    • Kizhatil, K.1    Bennett, V.2
  • 97
    • 57649130788 scopus 로고    scopus 로고
    • Ankyrin-B is required for coordinated expression of beta-2 spectrin, the Na/K ATPase and the Na/Ca exchanger in the inner segment of rod photoreceptors
    • Kizhatil, K., Sandhu, N., Peachy, N.S., Bennett, V., Ankyrin-B is required for coordinated expression of beta-2 spectrin, the Na/K ATPase and the Na/Ca exchanger in the inner segment of rod photoreceptors. Experimental Eye Research 88 (2009), 59–64.
    • (2009) Experimental Eye Research , vol.88 , pp. 59-64
    • Kizhatil, K.1    Sandhu, N.2    Peachy, N.S.3    Bennett, V.4
  • 98
    • 33847314248 scopus 로고    scopus 로고
    • Ankyrin-G and beta2-spectrin collaborate in biogenesis of lateral membrane of human bronchial epithelial cells
    • Kizhatil, K., Yoon, W., Mohler, P.J., Davis, L.H., Hoffman, J.A., Bennett, V., Ankyrin-G and beta2-spectrin collaborate in biogenesis of lateral membrane of human bronchial epithelial cells. Journal of Biological Chemistry 282 (2007), 2029–2037.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 2029-2037
    • Kizhatil, K.1    Yoon, W.2    Mohler, P.J.3    Davis, L.H.4    Hoffman, J.A.5    Bennett, V.6
  • 101
    • 0037148526 scopus 로고    scopus 로고
    • βIV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier
    • January 21
    • Komada, M., Soriano, P., βIV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier. Journal of Cell Biology 156:2 (January 21, 2002), 337–348.
    • (2002) Journal of Cell Biology , vol.156 , Issue.2 , pp. 337-348
    • Komada, M.1    Soriano, P.2
  • 102
    • 0028985712 scopus 로고
    • AnkyrinG. A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier
    • Kordeli, E., Lambert, S., Bennett, V., AnkyrinG. A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier. Journal of Biological Chemistry 270 (1995), 2352–2359.
    • (1995) Journal of Biological Chemistry , vol.270 , pp. 2352-2359
    • Kordeli, E.1    Lambert, S.2    Bennett, V.3
  • 103
    • 0031711226 scopus 로고    scopus 로고
    • AnkyrinG is associated with the postsynaptic membrane and the sarcoplasmic reticulum in the skeletal muscle fiber
    • Kordeli, E., Ludosky, M.A., Deprette, C., Frappier, T., Cartaud, J., AnkyrinG is associated with the postsynaptic membrane and the sarcoplasmic reticulum in the skeletal muscle fiber. Journal of Cell Science 111:Pt 15 (1998), 2197–2207.
    • (1998) Journal of Cell Science , vol.111 , pp. 2197-2207
    • Kordeli, E.1    Ludosky, M.A.2    Deprette, C.3    Frappier, T.4    Cartaud, J.5
  • 105
    • 0030005249 scopus 로고    scopus 로고
    • A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments
    • Kuhlman, P.A., Hughes, C.A., Bennett, V., Fowler, V.M., A new function for adducin. Calcium/calmodulin-regulated capping of the barbed ends of actin filaments. Journal of Biological Chemistry 271:14 (1996), 7986–7991.
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.14 , pp. 7986-7991
    • Kuhlman, P.A.1    Hughes, C.A.2    Bennett, V.3    Fowler, V.M.4
  • 106
    • 80053578949 scopus 로고    scopus 로고
    • A pathway for the control of anoikis sensitivity by E-cadherin and epithelial-to-mesenchymal transition
    • October
    • Kumar, S., Park, S.H., Cieply, B., Schupp, J., Killiam, E., Zhang, F., et al. A pathway for the control of anoikis sensitivity by E-cadherin and epithelial-to-mesenchymal transition. Molecular and Cellular Biology 31:19 (October 2011), 4036–4051.
    • (2011) Molecular and Cellular Biology , vol.31 , Issue.19 , pp. 4036-4051
    • Kumar, S.1    Park, S.H.2    Cieply, B.3    Schupp, J.4    Killiam, E.5    Zhang, F.6
  • 107
    • 0029558546 scopus 로고
    • A neuron-specific isoform of brain ankyrin, 440-kD ankyrinB, is targeted to the axons of rat cerebellar neurons
    • Kunimoto, M., A neuron-specific isoform of brain ankyrin, 440-kD ankyrinB, is targeted to the axons of rat cerebellar neurons. Journal of Cell Biology 131 (1995), 1821–1829.
    • (1995) Journal of Cell Biology , vol.131 , pp. 1821-1829
    • Kunimoto, M.1
  • 108
    • 0025840276 scopus 로고
    • A new 440-kD isoform is the major ankyrin in neonatal rat brain
    • Kunimoto, M., Otto, E., Bennett, V., A new 440-kD isoform is the major ankyrin in neonatal rat brain. Journal of Cell Biology 115 (1991), 1319–1331.
    • (1991) Journal of Cell Biology , vol.115 , pp. 1319-1331
    • Kunimoto, M.1    Otto, E.2    Bennett, V.3
  • 109
    • 84870188756 scopus 로고    scopus 로고
    • Dynamic organizing principles of the plasma membrane that regulate signal transduction: commemorating the fortieth anniversary of Singer and Nicolson's fluid-mosaic model
    • Kusumi, A., Fujiwara, T.K., Chadda, R., Xie, M., Tsunoyama, T.A., Kalay, Z., et al. Dynamic organizing principles of the plasma membrane that regulate signal transduction: commemorating the fortieth anniversary of Singer and Nicolson's fluid-mosaic model. Annual Review of Cell and Developmental Biology 28 (2012), 215–250.
    • (2012) Annual Review of Cell and Developmental Biology , vol.28 , pp. 215-250
    • Kusumi, A.1    Fujiwara, T.K.2    Chadda, R.3    Xie, M.4    Tsunoyama, T.A.5    Kalay, Z.6
  • 111
    • 0041345748 scopus 로고    scopus 로고
    • Identification of a conserved ankyrin-binding motif in the family of sodium channel alpha subunits
    • Lemaillet, G., Walker, B., Lambert, S., Identification of a conserved ankyrin-binding motif in the family of sodium channel alpha subunits. Journal of Biological Chemistry 278:30 (2003), 27333–27339.
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.30 , pp. 27333-27339
    • Lemaillet, G.1    Walker, B.2    Lambert, S.3
  • 113
    • 33845934490 scopus 로고    scopus 로고
    • Ankyrin repeat: a unique motif mediating protein-protein interactions
    • Li, J., Mahajan, A., Tsai, M.D., Ankyrin repeat: a unique motif mediating protein-protein interactions. Biochemistry 45:51 (2006), 15168–15178.
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15168-15178
    • Li, J.1    Mahajan, A.2    Tsai, M.D.3
  • 114
    • 0032563088 scopus 로고    scopus 로고
    • Adducin preferentially recruits spectrin to the fast growing ends of actin filaments in a complex requiring the MARCKS-related domain and a newly defined oligomerization domain
    • Li, X., Matsuoka, Y., Bennett, V., Adducin preferentially recruits spectrin to the fast growing ends of actin filaments in a complex requiring the MARCKS-related domain and a newly defined oligomerization domain. Journal of Biological Chemistry 273:30 (1998), 19329–19338.
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.30 , pp. 19329-19338
    • Li, X.1    Matsuoka, Y.2    Bennett, V.3
  • 115
    • 42649106474 scopus 로고    scopus 로고
    • New components of the Drosophila fusome suggest it plays novel roles in signaling and transport
    • Lighthouse, D.V., Buszczak, M., Spradling, A.C., New components of the Drosophila fusome suggest it plays novel roles in signaling and transport. Developmental Biology 317 (2008), 59–71.
    • (2008) Developmental Biology , vol.317 , pp. 59-71
    • Lighthouse, D.V.1    Buszczak, M.2    Spradling, A.C.3
  • 116
    • 0028214601 scopus 로고
    • The Drosophila fusome, a germline-specific organelle, contains membrane skeletal proteins and functions in cyst formation
    • Lin, H., Yue, L., Spradling, A.C., The Drosophila fusome, a germline-specific organelle, contains membrane skeletal proteins and functions in cyst formation. Development 120 (1994), 947–956.
    • (1994) Development , vol.120 , pp. 947-956
    • Lin, H.1    Yue, L.2    Spradling, A.C.3
  • 117
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood, D., Simons, K., Lipid rafts as a membrane-organizing principle. Science 327:5961 (2010), 46–50.
    • (2010) Science , vol.327 , Issue.5961 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 118
    • 84872021463 scopus 로고    scopus 로고
    • Recessive mutations in SPTBN2 implicate β-III spectrin in both cognitive and motor development
    • Lise, S., Clarkson, Y., Perkins, E., Kwasniewska, A., Sadighi Akha, E., Schnekenberg, R.P., et al. Recessive mutations in SPTBN2 implicate β-III spectrin in both cognitive and motor development. PLoS Genetics, 8(12), 2012, e1003074.
    • (2012) PLoS Genetics , vol.8 , Issue.12 , pp. e1003074
    • Lise, S.1    Clarkson, Y.2    Perkins, E.3    Kwasniewska, A.4    Sadighi Akha, E.5    Schnekenberg, R.P.6
  • 119
    • 20044369520 scopus 로고    scopus 로고
    • The ammonium transporter RhBG requirement of a tyrosine-based signal and ankyrin-G for basolateral targeting and membrane anchorage in polarized kidney epithelial cells
    • Lopez, C., Metral, S., Eladari, D., Drevensek, S., Gane, P., Chambrey, R., et al. The ammonium transporter RhBG requirement of a tyrosine-based signal and ankyrin-G for basolateral targeting and membrane anchorage in polarized kidney epithelial cells. Journal of Biological Chemistry 280 (2005), 8221–8228.
    • (2005) Journal of Biological Chemistry , vol.280 , pp. 8221-8228
    • Lopez, C.1    Metral, S.2    Eladari, D.3    Drevensek, S.4    Gane, P.5    Chambrey, R.6
  • 120
    • 84930441800 scopus 로고    scopus 로고
    • A PIK3C3-ankyrin-B-dynactin pathway promotes axonal growth and multiorganelle transport
    • Lorenzo, D.N., Badea, A., Davis, J., Hostettler, J., He, J., Zhong, G., et al. A PIK3C3-ankyrin-B-dynactin pathway promotes axonal growth and multiorganelle transport. Journal of Cell Biology 207:6 (2014), 735–752.
    • (2014) Journal of Cell Biology , vol.207 , Issue.6 , pp. 735-752
    • Lorenzo, D.N.1    Badea, A.2    Davis, J.3    Hostettler, J.4    He, J.5    Zhong, G.6
  • 121
    • 77950564431 scopus 로고    scopus 로고
    • Spectrin mutations that cause spinocerebellar ataxia type 5 impair axonal transport and induce neurodegeneration in Drosophila
    • Lorenzo, D.N., Li, M.G., Mische, S.E., Armbrust, K.R., Ranum, L.P., Hays, T.S., Spectrin mutations that cause spinocerebellar ataxia type 5 impair axonal transport and induce neurodegeneration in Drosophila. Journal of Cell Biology 189 (2010), 143–158.
    • (2010) Journal of Cell Biology , vol.189 , pp. 143-158
    • Lorenzo, D.N.1    Li, M.G.2    Mische, S.E.3    Armbrust, K.R.4    Ranum, L.P.5    Hays, T.S.6
  • 122
    • 38349080944 scopus 로고    scopus 로고
    • Voltage-gated Nav channel targeting in the heart requires an ankyrin-G dependent cellular pathway
    • Lowe, J.S., Palygin, O., Bhasin, N., Hund, T.J., Boyden, P.A., Shibata, E., et al. Voltage-gated Nav channel targeting in the heart requires an ankyrin-G dependent cellular pathway. Journal of Cell Biology 180:1 (2008), 173–186.
    • (2008) Journal of Cell Biology , vol.180 , Issue.1 , pp. 173-186
    • Lowe, J.S.1    Palygin, O.2    Bhasin, N.3    Hund, T.J.4    Boyden, P.A.5    Shibata, E.6
  • 123
    • 0025117790 scopus 로고
    • Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue- differentiation and cell cycle control proteins
    • Lux, S.E., John, K.M., Bennett, V., Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue- differentiation and cell cycle control proteins. Nature 344 (1990), 36–42.
    • (1990) Nature , vol.344 , pp. 36-42
    • Lux, S.E.1    John, K.M.2    Bennett, V.3
  • 125
    • 84922392783 scopus 로고    scopus 로고
    • Ankyrin-G coordinates intercalated disc signaling platform to regulate cardiac excitability in vivo
    • Makara, M.A., Curran, J., Little, S.C., Musa, H., Polina, I., Smith, S.A., et al. Ankyrin-G coordinates intercalated disc signaling platform to regulate cardiac excitability in vivo. Circulation Research 115:11 (2014), 929–938.
    • (2014) Circulation Research , vol.115 , Issue.11 , pp. 929-938
    • Makara, M.A.1    Curran, J.2    Little, S.C.3    Musa, H.4    Polina, I.5    Smith, S.A.6
  • 127
    • 84655167160 scopus 로고    scopus 로고
    • UNC-33 (CRMP) and ankyrin organize microtubules and localize kinesin to polarize axon-dendrite sorting
    • Maniar, T.A., Kaplan, M., Wang, G.J., Shen, K., Wei, L., Shaw, J.E., et al. UNC-33 (CRMP) and ankyrin organize microtubules and localize kinesin to polarize axon-dendrite sorting. Nature Neuroscience 15:1 (2011), 48–56.
    • (2011) Nature Neuroscience , vol.15 , Issue.1 , pp. 48-56
    • Maniar, T.A.1    Kaplan, M.2    Wang, G.J.3    Shen, K.4    Wei, L.5    Shaw, J.E.6
  • 128
    • 0034607695 scopus 로고    scopus 로고
    • Age of Neoproterozoic bilatarian body and trace fossils, White Sea, Russia: implications for metazoan evolution
    • Martin, M.W., Grazhdankin, D.V., Bowring, S.A., Evans, D.A., Fedonkin, M.A., Kirschvink, J.L., Age of Neoproterozoic bilatarian body and trace fossils, White Sea, Russia: implications for metazoan evolution. Science 288 (2000), 841–845.
    • (2000) Science , vol.288 , pp. 841-845
    • Martin, M.W.1    Grazhdankin, D.V.2    Bowring, S.A.3    Evans, D.A.4    Fedonkin, M.A.5    Kirschvink, J.L.6
  • 129
    • 33846270032 scopus 로고    scopus 로고
    • PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42
    • Martin-Belmonte, F., Gassama, A., Datta, A., Yu, W., Rescher, U., Gerke, V., et al. PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42. Cell 128 (2007), 383–397.
    • (2007) Cell , vol.128 , pp. 383-397
    • Martin-Belmonte, F.1    Gassama, A.2    Datta, A.3    Yu, W.4    Rescher, U.5    Gerke, V.6
  • 131
    • 77951994713 scopus 로고    scopus 로고
    • Crystal structure of the nonerythroid alpha-spectrin tetramerization site reveals differences between erythroid and nonerythroid spectrin tetramer formation
    • Mehboob, S., Song, Y., Witek, M., Long, F., Santarsiero, B.D., Johnson, M.E., et al. Crystal structure of the nonerythroid alpha-spectrin tetramerization site reveals differences between erythroid and nonerythroid spectrin tetramer formation. Journal of Biological Chemistry 285 (2010), 14572–14584.
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 14572-14584
    • Mehboob, S.1    Song, Y.2    Witek, M.3    Long, F.4    Santarsiero, B.D.5    Johnson, M.E.6
  • 132
    • 0037011104 scopus 로고    scopus 로고
    • Crystal structure of a 12 ANK repeat stack from human ankyrinR
    • Michaely, P., Tomchick, D.R., Machius, M., Anderson, R.G., Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO Journal 21 (2002), 6387–6396.
    • (2002) EMBO Journal , vol.21 , pp. 6387-6396
    • Michaely, P.1    Tomchick, D.R.2    Machius, M.3    Anderson, R.G.4
  • 134
    • 0037155903 scopus 로고    scopus 로고
    • The ankyrin-B C-terminal domain determines activity of ankyrin-B/G chimeras in rescue of abnormal inositol 1,4,5-trisphosphate and ryanodine receptor distribution in ankyrin-B (−/−) neonatal cardiomyocytes
    • Mohler, P.J., Gramolini, A.O., Bennett, V., The ankyrin-B C-terminal domain determines activity of ankyrin-B/G chimeras in rescue of abnormal inositol 1,4,5-trisphosphate and ryanodine receptor distribution in ankyrin-B (−/−) neonatal cardiomyocytes. Journal of Biological Chemistry 277 (2002), 10599–10607.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 10599-10607
    • Mohler, P.J.1    Gramolini, A.O.2    Bennett, V.3
  • 136
    • 0242464931 scopus 로고    scopus 로고
    • Ankyrin-B mutation causes type 4 long-QT cardiac arrhythmia and sudden cardiac death
    • Mohler, P.J., Schott, J.J., Gramolini, A.O., Dilly, K.W., Guatimosim, S., duBell, W.H., et al. Ankyrin-B mutation causes type 4 long-QT cardiac arrhythmia and sudden cardiac death. Nature 421 (2003), 634–639.
    • (2003) Nature , vol.421 , pp. 634-639
    • Mohler, P.J.1    Schott, J.J.2    Gramolini, A.O.3    Dilly, K.W.4    Guatimosim, S.5    duBell, W.H.6
  • 137
    • 4544252325 scopus 로고    scopus 로고
    • Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes
    • Mohler, P.J., Yoon, W., Bennett, V., Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes. Journal of Biological Chemistry 279 (2004), 40185–40193.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 40185-40193
    • Mohler, P.J.1    Yoon, W.2    Bennett, V.3
  • 138
    • 0024554715 scopus 로고
    • +-ATPase, ankyrin, and fodrin in Madin-Darby canine kidney (MDCK) cells: implications for the biogenesis of epithelial cell polarity
    • +-ATPase, ankyrin, and fodrin in Madin-Darby canine kidney (MDCK) cells: implications for the biogenesis of epithelial cell polarity. Journal of Cell Biology 108:3 (1989), 893–902.
    • (1989) Journal of Cell Biology , vol.108 , Issue.3 , pp. 893-902
    • Nelson, W.J.1    Hammerton, R.W.2
  • 139
    • 0025125799 scopus 로고
    • Identification of a membrane-cytoskeletal complex containing the cell adhesion molecule uvomorulin (E-cadherin), ankyrin, and fodrin in Madin-Darby canine kidney epithelial cells
    • February
    • Nelson, W.J., Shore, E.M., Wang, A.Z., Hammerton, R.W., Identification of a membrane-cytoskeletal complex containing the cell adhesion molecule uvomorulin (E-cadherin), ankyrin, and fodrin in Madin-Darby canine kidney epithelial cells. Journal of Cell Biology 110:2 (February 1990), 349–357.
    • (1990) Journal of Cell Biology , vol.110 , Issue.2 , pp. 349-357
    • Nelson, W.J.1    Shore, E.M.2    Wang, A.Z.3    Hammerton, R.W.4
  • 140
    • 84922348019 scopus 로고    scopus 로고
    • Flexible stoichiometry and asymmetry of the PIDDosome core complex by heteronuclear NMR spectroscopy and mass spectrometry
    • Nematollahi, L.A., Garza-Garcia, A., Bechara, C., Esposito, D., Morgner, N., Robinson, C.V., et al. Flexible stoichiometry and asymmetry of the PIDDosome core complex by heteronuclear NMR spectroscopy and mass spectrometry. Journal of Molecular Biology 427:4 (2015), 737–752.
    • (2015) Journal of Molecular Biology , vol.427 , Issue.4 , pp. 737-752
    • Nematollahi, L.A.1    Garza-Garcia, A.2    Bechara, C.3    Esposito, D.4    Morgner, N.5    Robinson, C.V.6
  • 142
    • 0029074731 scopus 로고
    • An ankyrin-related gene (unc-44) is necessary for proper axonal guidance in Caenorhabditis elegans
    • Otsuka, A.J., Franco, R., Yang, B., Shim, K.H., Tang, L.Z., Zhang, Y.Y., et al. An ankyrin-related gene (unc-44) is necessary for proper axonal guidance in Caenorhabditis elegans. Journal of Cell Biology 129 (1995), 1081–1092.
    • (1995) Journal of Cell Biology , vol.129 , pp. 1081-1092
    • Otsuka, A.J.1    Franco, R.2    Yang, B.3    Shim, K.H.4    Tang, L.Z.5    Zhang, Y.Y.6
  • 143
    • 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., Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively-spliced genes. Journal of Cell Biology 114 (1991), 241–253.
    • (1991) Journal of Cell Biology , vol.114 , pp. 241-253
    • Otto, E.1    Kunimoto, M.2    McLaughlin, T.3    Bennett, V.4
  • 144
    • 33644819526 scopus 로고    scopus 로고
    • A common ankyrin-G-based mechanism retains KCNQ and NaV channels at electrically active domains of the axon
    • Pan, Z., Kao, T., Horvath, Z., Lemos, J., Sul, J.Y., Cranstoun, S.D., et al. A common ankyrin-G-based mechanism retains KCNQ and NaV channels at electrically active domains of the axon. Journal of Neuroscience 26:10 (2006), 2599–2613.
    • (2006) Journal of Neuroscience , vol.26 , Issue.10 , pp. 2599-2613
    • Pan, Z.1    Kao, T.2    Horvath, Z.3    Lemos, J.4    Sul, J.Y.5    Cranstoun, S.D.6
  • 146
    • 0032885169 scopus 로고    scopus 로고
    • Genome evolution and the evolution of exon-shuffling–a review
    • Patthy, L., Genome evolution and the evolution of exon-shuffling–a review. Gene 238:1 (1999), 103–114.
    • (1999) Gene , vol.238 , Issue.1 , pp. 103-114
    • Patthy, L.1
  • 147
    • 77950618122 scopus 로고    scopus 로고
    • Loss of beta-III spectrin leads to Purkinje cell dysfunction recapitulating the behavior and neuropathology of spinocerebellar ataxia type 5 in humans
    • Perkins, E.M., Clarkson, Y.L., Sabatier, N., Longhurst, D.M., Millward, C.P., Jack, J., et al. Loss of beta-III spectrin leads to Purkinje cell dysfunction recapitulating the behavior and neuropathology of spinocerebellar ataxia type 5 in humans. Journal of Neuroscience 30 (2010), 4857–4867.
    • (2010) Journal of Neuroscience , vol.30 , pp. 4857-4867
    • Perkins, E.M.1    Clarkson, Y.L.2    Sabatier, N.3    Longhurst, D.M.4    Millward, C.P.5    Jack, J.6
  • 148
    • 0029047129 scopus 로고
    • Ank3 (epithelial ankyrin), a widely distributed new member of the ankyrin gene family and the major ankyrin in kidney, is expressed in alternatively spliced forms, including forms that lack the repeat domain
    • Peters, L.L., John, K.M., Lu, F.M., Eicher, E.M., Higgins, A., Yialamas, M., et al. Ank3 (epithelial ankyrin), a widely distributed new member of the ankyrin gene family and the major ankyrin in kidney, is expressed in alternatively spliced forms, including forms that lack the repeat domain. Journal of Cell Biology 130 (1995), 313–330.
    • (1995) Journal of Cell Biology , vol.130 , pp. 313-330
    • Peters, L.L.1    John, K.M.2    Lu, F.M.3    Eicher, E.M.4    Higgins, A.5    Yialamas, M.6
  • 149
    • 42149171410 scopus 로고    scopus 로고
    • A presynaptic giant ankyrin stabilizes the NMJ through regulation of presynaptic microtubules and transsynaptic cell adhesion
    • Pielage, J., Cheng, L., Fetter, R.D., Carlton, P.M., Sedat, J.W., Davis, G.W., A presynaptic giant ankyrin stabilizes the NMJ through regulation of presynaptic microtubules and transsynaptic cell adhesion. Neuron 58:2 (2008), 195–209.
    • (2008) Neuron , vol.58 , Issue.2 , pp. 195-209
    • Pielage, J.1    Cheng, L.2    Fetter, R.D.3    Carlton, P.M.4    Sedat, J.W.5    Davis, G.W.6
  • 150
    • 20144380700 scopus 로고    scopus 로고
    • Presynaptic spectrin is essential for synapse stabilization
    • Pielage, J., Fetter, R.D., Davis, G.W., Presynaptic spectrin is essential for synapse stabilization. Current Biology 15:10 (2005), 918–928.
    • (2005) Current Biology , vol.15 , Issue.10 , pp. 918-928
    • Pielage, J.1    Fetter, R.D.2    Davis, G.W.3
  • 151
    • 84920848625 scopus 로고    scopus 로고
    • Designed ankyrin repeat proteins (DARPins): binding proteins for research, diagnostics, and therapy
    • Plückthun, A., Designed ankyrin repeat proteins (DARPins): binding proteins for research, diagnostics, and therapy. Annual Review of Pharmacology and Toxicology 55 (2015), 489–511.
    • (2015) Annual Review of Pharmacology and Toxicology , vol.55 , pp. 489-511
    • Plückthun, A.1
  • 152
    • 37349028655 scopus 로고    scopus 로고
    • Functional dissection of the C. elegans cell adhesion molecule SAX-7, a homologue of human L1
    • Pocock, R., Bénard, C.Y., Shapiro, L., Hobert, O., Functional dissection of the C. elegans cell adhesion molecule SAX-7, a homologue of human L1. Molecular and Cellular Neurosciences 37 (2008), 56–68.
    • (2008) Molecular and Cellular Neurosciences , vol.37 , pp. 56-68
    • Pocock, R.1    Bénard, C.Y.2    Shapiro, L.3    Hobert, O.4
  • 153
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles
    • Rief, M., Pascual, J., Saraste, M., Gaub, H.E., Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. Journal of Molecular Biology 286 (1999), 553–561.
    • (1999) Journal of Molecular Biology , vol.286 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 156
    • 0032583202 scopus 로고    scopus 로고
    • Nervous system defects of ankyrin-B (−/−) mice suggest functional overlap between the cell adhesion molecule L1 and 440 kD ankyrin-B in premyelinated axons
    • Scotland, P., Zhou, D., Benveniste, H., Bennett, V., Nervous system defects of ankyrin-B (−/−) mice suggest functional overlap between the cell adhesion molecule L1 and 440 kD ankyrin-B in premyelinated axons. Journal of Cell Biology 143 (1998), 1305–1315.
    • (1998) Journal of Cell Biology , vol.143 , pp. 1305-1315
    • Scotland, P.1    Zhou, D.2    Benveniste, H.3    Bennett, V.4
  • 157
    • 0019304034 scopus 로고
    • Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes
    • Sheetz, M.P., Schindler, M., Koppel, D.E., Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes. Nature 285:5765 (1980), 510–511.
    • (1980) Nature , vol.285 , Issue.5765 , pp. 510-511
    • Sheetz, M.P.1    Schindler, M.2    Koppel, D.E.3
  • 159
    • 0018742616 scopus 로고
    • The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies
    • Shotton, D.M., Burke, B.E., Branton, D., The molecular structure of human erythrocyte spectrin. Biophysical and electron microscopic studies. Journal of Molecular Biology 131:2 (1979), 303–329.
    • (1979) Journal of Molecular Biology , vol.131 , Issue.2 , pp. 303-329
    • Shotton, D.M.1    Burke, B.E.2    Branton, D.3
  • 160
    • 84928242229 scopus 로고    scopus 로고
    • L1CAM/Neuroglian controls the axon-axon interactions establishing layered and lobular mushroom body architecture
    • Siegenthaler, D., Enneking, E.M., Moreno, E., Pielage, J., L1CAM/Neuroglian controls the axon-axon interactions establishing layered and lobular mushroom body architecture. Journal of Cell Biology 208:7 (2015), 1003–1018.
    • (2015) Journal of Cell Biology , vol.208 , Issue.7 , pp. 1003-1018
    • Siegenthaler, D.1    Enneking, E.M.2    Moreno, E.3    Pielage, J.4
  • 161
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer, S.J., Nicolson, G.L., The fluid mosaic model of the structure of cell membranes. Science 175:4023 (1972), 720–731.
    • (1972) Science , vol.175 , Issue.4023 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 162
    • 84908223216 scopus 로고    scopus 로고
    • Psychiatric risk factor ANK3/ankyrin-G nanodomains regulate the structure and function of glutamatergic synapses
    • Smith, K.R., Kopeikina, K.J., Fawcett-Patel, J.M., Leaderbrand, K., Gao, R., Schürmann, B., et al. Psychiatric risk factor ANK3/ankyrin-G nanodomains regulate the structure and function of glutamatergic synapses. Neuron 84:2 (2014), 399–415.
    • (2014) Neuron , vol.84 , Issue.2 , pp. 399-415
    • Smith, K.R.1    Kopeikina, K.J.2    Fawcett-Patel, J.M.3    Leaderbrand, K.4    Gao, R.5    Schürmann, B.6
  • 164
    • 67049164963 scopus 로고    scopus 로고
    • The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties
    • Stabach, P.R., Simonović, I., Ranieri, M.A., Aboodi, M.S., Steitz, T.A., Simonović, M., et al. The structure of the ankyrin-binding site of beta-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties. Blood 113 (2009), 5377–5384.
    • (2009) Blood , vol.113 , pp. 5377-5384
    • Stabach, P.R.1    Simonović, I.2    Ranieri, M.A.3    Aboodi, M.S.4    Steitz, T.A.5    Simonović, M.6
  • 166
    • 0023394457 scopus 로고
    • Ankyrin-bound fatty acid turns over rapidly at the erythrocyte plasma membrane
    • Staufenbiel, M., Ankyrin-bound fatty acid turns over rapidly at the erythrocyte plasma membrane. Molecular and Cellular Biology 7 (1987), 2981–2984.
    • (1987) Molecular and Cellular Biology , vol.7 , pp. 2981-2984
    • Staufenbiel, M.1
  • 167
    • 84926322108 scopus 로고    scopus 로고
    • Hierarchical microtubule organization controls axon caliber and transport and determines synaptic structure and stability
    • Stephan, R., Goellner, B., Moreno, E., Frank, C.A., Hugenschmidt, T., Genoud, C., et al. Hierarchical microtubule organization controls axon caliber and transport and determines synaptic structure and stability. Developmental Cell 33:1 (2015), 5–21.
    • (2015) Developmental Cell , vol.33 , Issue.1 , pp. 5-21
    • Stephan, R.1    Goellner, B.2    Moreno, E.3    Frank, C.A.4    Hugenschmidt, T.5    Genoud, C.6
  • 169
    • 0037462502 scopus 로고    scopus 로고
    • Disruption of transforming growth factor-beta signaling in ELF beta-spectrin-deficient mice
    • Tang, Y., Katuri, V., Dillner, A., Mishra, B., Deng, C.X., Mishra, L., Disruption of transforming growth factor-beta signaling in ELF beta-spectrin-deficient mice. Science 299 (2003), 574–777.
    • (2003) Science , vol.299 , pp. 574-777
    • Tang, Y.1    Katuri, V.2    Dillner, A.3    Mishra, B.4    Deng, C.X.5    Mishra, L.6
  • 170
    • 79960680557 scopus 로고    scopus 로고
    • Cdk5 regulates the size of an axon initial segment-like compartment in mushroom body neurons of the Drosophila central brain
    • Trunova, S., Baek, B., Giniger, E., Cdk5 regulates the size of an axon initial segment-like compartment in mushroom body neurons of the Drosophila central brain. Journal of Neuroscience 31:29 (2011), 10451–10462.
    • (2011) Journal of Neuroscience , vol.31 , Issue.29 , pp. 10451-10462
    • Trunova, S.1    Baek, B.2    Giniger, E.3
  • 172
    • 34250314110 scopus 로고    scopus 로고
    • Specific role of the truncated betaIV-spectrin Sigma6 in sodium channel clustering at axon initial segments and nodes of Ranvier
    • Uemoto, Y., Suzuki, S., Terada, N., Ohno, N., Ohno, S., Yamanaka, S., et al. Specific role of the truncated betaIV-spectrin Sigma6 in sodium channel clustering at axon initial segments and nodes of Ranvier. Journal of Biological Chemistry 282 (2007), 6548–6555.
    • (2007) Journal of Biological Chemistry , vol.282 , pp. 6548-6555
    • Uemoto, Y.1    Suzuki, S.2    Terada, N.3    Ohno, N.4    Ohno, S.5    Yamanaka, S.6
  • 173
    • 33646900710 scopus 로고    scopus 로고
    • O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry
    • Vosseller, K., Trinidad, J.C., Chalkley, R.J., Specht, C.G., Thalhammer, A., Lynn, A.J., et al. O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry. Molecular and Cellular Proteomics 5 (2006), 923–934.
    • (2006) Molecular and Cellular Proteomics , vol.5 , pp. 923-934
    • Vosseller, K.1    Trinidad, J.C.2    Chalkley, R.J.3    Specht, C.G.4    Thalhammer, A.5    Lynn, A.J.6
  • 174
    • 84936163230 scopus 로고    scopus 로고
    • Structural basis of diverse membrane target recognitions by ankyrins
    • Nov 10
    • Wang, C., Wei, Z., Chen, K., Ye, F., Yu, C., Bennett, V., et al. Structural basis of diverse membrane target recognitions by ankyrins. Elife, 3, Nov 10, 2014, 10.7554/eLife.04353.
    • (2014) Elife , vol.3
    • Wang, C.1    Wei, Z.2    Chen, K.3    Ye, F.4    Yu, C.5    Bennett, V.6
  • 178
    • 0025250561 scopus 로고
    • Beta spectrin in human skeletal muscle. Tissue-specific differential processing of 3' beta spectrin pre-mRNA generates a beta spectrin isoform with a unique carboxyl terminus
    • Winkelmann, J.C., Costa, F.F., Linzie, B.L., Forget, B.G., Beta spectrin in human skeletal muscle. Tissue-specific differential processing of 3' beta spectrin pre-mRNA generates a beta spectrin isoform with a unique carboxyl terminus. Journal of Biological Chemistry 265 (1990), 20449–20454.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 20449-20454
    • Winkelmann, J.C.1    Costa, F.F.2    Linzie, B.L.3    Forget, B.G.4
  • 179
    • 0032498588 scopus 로고    scopus 로고
    • β-Spectrin is colocalized with both voltage-gated sodium channels and ankyrinG at the adult rat neuromuscular junction
    • February 9
    • Wood, S.J., Slater, C.R., β-Spectrin is colocalized with both voltage-gated sodium channels and ankyrinG at the adult rat neuromuscular junction. Journal of Cell Biology 140:3 (February 9, 1998), 675–684.
    • (1998) Journal of Cell Biology , vol.140 , Issue.3 , pp. 675-684
    • Wood, S.J.1    Slater, C.R.2
  • 180
    • 84872796017 scopus 로고    scopus 로고
    • Actin, spectrin, and associated proteins form a periodic cytoskeletal structure in axons
    • Xu, K., Zhong, G., Zhuang, X., Actin, spectrin, and associated proteins form a periodic cytoskeletal structure in axons. Science 339:6118 (2013), 452–456.
    • (2013) Science , vol.339 , Issue.6118 , pp. 452-456
    • Xu, K.1    Zhong, G.2    Zhuang, X.3
  • 182
    • 0029969728 scopus 로고    scopus 로고
    • Identification of O-linked N-acetyl glucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier
    • Zhang, X., Bennett, V., Identification of O-linked N-acetyl glucosamine modification of ankyrinG isoforms targeted to nodes of Ranvier. Journal of Biological Chemistry 271 (1996), 31391–31398.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 31391-31398
    • Zhang, X.1    Bennett, V.2
  • 184
    • 77952672566 scopus 로고    scopus 로고
    • Characterization and expression of a heart-selective alternatively spliced variant of alpha II-spectrin, cardi+, during development in the rat
    • Zhang, Y., Resneck, W.G., Lee, P.C., Randall, W.R., Bloch, R.J., Ursitti, J.A., Characterization and expression of a heart-selective alternatively spliced variant of alpha II-spectrin, cardi+, during development in the rat. Journal of Molecular and Cellular Cardiology 48 (2010), 1050–1059.
    • (2010) Journal of Molecular and Cellular Cardiology , vol.48 , pp. 1050-1059
    • Zhang, Y.1    Resneck, W.G.2    Lee, P.C.3    Randall, W.R.4    Bloch, R.J.5    Ursitti, J.A.6
  • 185
    • 84996486097 scopus 로고    scopus 로고
    • Developmental mechanism of the periodic membrane skeleton in axons
    • Dec 23
    • Zhong, G., He, J., Zhou, R., Lorenzo, D., Babcock, H.P., Bennett, V., et al. Developmental mechanism of the periodic membrane skeleton in axons. Elife, 3, Dec 23, 2014, 10.7554/eLife.04581.
    • (2014) Elife , vol.3
    • Zhong, G.1    He, J.2    Zhou, R.3    Lorenzo, D.4    Babcock, H.P.5    Bennett, V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.