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Volumn 23, Issue 14, 2014, Pages 3875-3882

β-III spectrinunderpins ankyrin R function in purkinje cell dendritic trees: Protein complex critical for sodium channel activity is impaired by SCA5-associated mutations

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ANKYRIN; ANKYRIN R; BETA III SPECTRIN; NUCLEIC ACID BINDING PROTEIN; SODIUM CHANNEL NAV1.1; SODIUM CHANNEL NAV1.6; SPECTRIN; SPINOCEREBELLAR ATAXIA TYPE 5 PROTEIN; UNCLASSIFIED DRUG; VOLTAGE GATED SODIUM CHANNEL; SODIUM CHANNEL; SPTBN2 PROTEIN, MOUSE;

EID: 84902991843     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddu103     Document Type: Article
Times cited : (27)

References (37)
  • 1
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • De Matteis, M.A. and Morrow, J.S. (2000) Spectrin tethers and mesh in the biosynthetic pathway. J. Cell Sci. 113, 2331-2343.
    • (2000) J. Cell Sci. , vol.113 , pp. 2331-2343
    • De Matteis, M.A.1    Morrow, J.S.2
  • 2
    • 0034958883 scopus 로고    scopus 로고
    • Spectrin and ankyrin-based pathways:metazoan inventions for integrating cells into tissues
    • Bennett, V. and Baines, A.J. (2001) Spectrin and ankyrin-based pathways:metazoan inventions for integrating cells into tissues. Physiol. Rev., 81, 1353-1392.
    • (2001) Physiol. Rev. , vol.81 , pp. 1353-1392
    • Bennett, V.1    Baines, A.J.2
  • 3
    • 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. and Bennett, V. (1984) Brain ankyrin. A membrane-associated protein with binding sites for spectrin, tubulin, and the cytoplasmic domain of the erythrocyte anion channel. J. Biol. Chem., 259, 13550-13559.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13550-13559
    • Davis, J.Q.1    Bennett, V.2
  • 4
    • 0025995618 scopus 로고
    • Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin
    • Kennedy, S.P., Warren, S.L., Forget, B.G. and Morrow, J.S. (1991) Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin. J. Cell Biol., 115, 267-277.
    • (1991) J. Cell Biol. , vol.115 , pp. 267-277
    • Kennedy, S.P.1    Warren, S.L.2    Forget, B.G.3    Morrow, J.S.4
  • 5
    • 0026806912 scopus 로고
    • Ankyrins. Adaptors between diverse plasma membrane proteins and the cytoplasm
    • Bennett, V. (1992) Ankyrins. Adaptors between diverse plasma membrane proteins and the cytoplasm. J. Biol. Chem., 267, 8703-8706.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8703-8706
    • Bennett, V.1
  • 6
  • 7
    • 4544252325 scopus 로고    scopus 로고
    • Ankyrin-B targets b2-spectrin to an intracellular compartment in neonatal cardiomyocytes
    • Mohler, P.J., Yoon, W. and Bennett, V. (2004) Ankyrin-B targets b2-spectrin to an intracellular compartment in neonatal cardiomyocytes. J. Biol. Chem., 279, 40185-40193.
    • (2004) J. Biol. Chem. , vol.279 , pp. 40185-40193
    • Mohler, P.J.1    Yoon, W.2    Bennett, V.3
  • 8
    • 45449118896 scopus 로고    scopus 로고
    • The 22.5 kDa spectrin-binding domain of ankyrinR binds spectrin with high affinity and changes the spectrin distribution in cells in vivo
    • Kolondra, A., Grzybek, M., Chorzalska, A. and Sikorski, A.F. (2008) The 22.5 kDa spectrin-binding domain of ankyrinR binds spectrin with high affinity and changes the spectrin distribution in cells in vivo. Protein Expr. Purif., 60, 157-164.
    • (2008) Protein Expr. Purif. , vol.60 , pp. 157-164
    • Kolondra, A.1    Grzybek, M.2    Chorzalska, A.3    Sikorski, A.F.4
  • 9
    • 47249140034 scopus 로고    scopus 로고
    • Molecular epitopes of the ankyrin-spectrin interaction
    • Ipsaro, J.J., Huang, L., Gutierrez, L. and MacDonald, R.I. (2008) Molecular epitopes of the ankyrin-spectrin interaction. Biochemistry, 47, 7452-7464.
    • (2008) Biochemistry , vol.47 , pp. 7452-7464
    • Ipsaro, J.J.1    Huang, L.2    Gutierrez, L.3    MacDonald, R.I.4
  • 10
    • 1942509531 scopus 로고    scopus 로고
    • Hereditary spherocytosis-defects in proteins that connect the membrane skeleton to the lipid bilayer
    • Eber, S.W. and Lux, S.E. (2004) Hereditary spherocytosis-defects in proteins that connect the membrane skeleton to the lipid bilayer. Semin. Hematol., 41, 118-141.
    • (2004) Semin. Hematol. , vol.41 , pp. 118-141
    • Eber, S.W.1    Lux, S.E.2
  • 11
    • 27744595523 scopus 로고    scopus 로고
    • Hematologically important mutations: ankyrin variants in hereditary spherocytosis
    • Gallagher, P.G. (2005) Hematologically important mutations: ankyrin variants in hereditary spherocytosis. Blood Cells Mol. Dis., 35, 345-347.
    • (2005) Blood Cells Mol. Dis. , vol.35 , pp. 345-347
    • Gallagher, P.G.1
  • 12
    • 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. and 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    Lambert, S.2    Bennett, V.3
  • 13
    • 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. and Bennett, V. (2001) Ankyrin-G coordinates assembly of the spectrin-based membrane skeleton, voltage-gated sodium channels, and L1 CAMs at Purkinje neuron initial segments. J. Cell Biol., 155, 739-746.
    • (2001) J. Cell Biol. , vol.155 , pp. 739-746
    • Jenkins, S.M.1    Bennett, V.2
  • 14
    • 0037148526 scopus 로고    scopus 로고
    • bIV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier
    • Komada, M. and Soriano, P. (2002) bIV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier. J. Cell Biol., 156, 337-348.
    • (2002) J. Cell Biol. , vol.156 , pp. 337-348
    • Komada, M.1    Soriano, P.2
  • 16
    • 81255195587 scopus 로고    scopus 로고
    • β 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. and Rothstein, J.D. (2011) β spectrin is critical for development of Purkinje cell dendritic tree and spine morphogenesis. J. Neurosci., 31, 16581-16590.
    • (2011) J. Neurosci. , 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    Rothstein, J.D.7
  • 19
    • 0021704597 scopus 로고
    • Spectrin deficient inherited haemolytic anemias in the mouse: characterization by spectrin synthesis and mRNA activity in reticulocytes
    • Bodine, D.M. IV, Birkenmeier, C.S. and Barker, J.E. (1984) Spectrin deficient inherited haemolytic anemias in the mouse: characterization by spectrin synthesis and mRNA activity in reticulocytes. Cell, 37, 721-729.
    • (1984) Cell , vol.37 , pp. 721-729
    • Bodine, D.M.1    Birkenmeier, C.S.2    Barker, J.E.3
  • 21
    • 0026077783 scopus 로고
    • Distinct ankyrin isoforms at neuron cell bodies and nodes of ranvier resolved using erythrocyte ankyrin-deficient mice
    • Kordeli, E. and Bennett, V. (1991) Distinct ankyrin isoforms at neuron cell bodies and nodes of ranvier resolved using erythrocyte ankyrin-deficient mice. J. Cell Biol., 114, 1243-1259.
    • (1991) J. Cell Biol. , vol.114 , pp. 1243-1259
    • Kordeli, E.1    Bennett, V.2
  • 22
    • 33750334569 scopus 로고    scopus 로고
    • Spectrin functions upstream of ankyrin in a spectrin cytoskeleton assembly pathway
    • Das, A., Base, C., Dhulipala, S. and Dubreuil, R. (2006) Spectrin functions upstream of ankyrin in a spectrin cytoskeleton assembly pathway. J. Cell Biol., 175, 325-335.
    • (2006) J. Cell Biol. , vol.175 , pp. 325-335
    • Das, A.1    Base, C.2    Dhulipala, S.3    Dubreuil, R.4
  • 23
    • 0034808728 scopus 로고    scopus 로고
    • A novel isoform of beta-spectrin II localizes to cerebellar Purkinje-cell bodies and interacts with neurofibromatosis type 2 gene product schwannomin
    • Chen, Y., Yu, P., Lu, D., Tagle, D.A. and Cai, T. (2001) A novel isoform of beta-spectrin II localizes to cerebellar Purkinje-cell bodies and interacts with neurofibromatosis type 2 gene product schwannomin. J. Mol. Neurosci., 17, 59-70.
    • (2001) J. Mol. Neurosci. , vol.17 , pp. 59-70
    • Chen, Y.1    Yu, P.2    Lu, D.3    Tagle, D.A.4    Cai, T.5
  • 24
    • 0032582909 scopus 로고    scopus 로고
    • AnkyrinG is required for clustering of voltage-gated Na channels at axon initial segments and for normal action potential firing
    • Zhou, D.,Lambert,S.,Malen,P.L.,Carpenter,S., Boland,L.M.andBennett,V. (1998) AnkyrinG is required for clustering of voltage-gated Na channels at axon initial segments and for normal action potential firing. J. Cell Biol., 143, 1295-1304.
    • (1998) J. Cell Biol. , vol.143 , pp. 1295-1304
    • Zhou, D.1    Lambert, S.2    Malen, P.L.3    Carpenter, S.4    Boland, L.M.5    Bennett, V.6
  • 26
    • 0034686371 scopus 로고    scopus 로고
    • Distribution of voltage-gated sodium channela-subunit and b-subunit mRNAs in human hippocampal formation, cortex, and cerebellum
    • Whitaker, W.R., Clare, J.J., Powell, A.J., Chen, Y.H., Faull, R.L.M. and Emson, P.C. (2000) Distribution of voltage-gated sodium channela-subunit and b-subunit mRNAs in human hippocampal formation, cortex, and cerebellum. J. Comp. Neurol., 422, 123-139.
    • (2000) J. Comp. Neurol. , vol.422 , pp. 123-139
    • Whitaker, W.R.1    Clare, J.J.2    Powell, A.J.3    Chen, Y.H.4    Faull, R.L.M.5    Emson, P.C.6
  • 27
    • 77953239491 scopus 로고    scopus 로고
    • Structural basis for spectrin recognition by ankyrin
    • Ipsaro, J.J. and Mondragon, A. (2010) Structural basis for spectrin recognition by ankyrin. Blood, 115, 4093-4101.
    • (2010) Blood , vol.115 , pp. 4093-4101
    • Ipsaro, J.J.1    Mondragon, A.2
  • 30
    • 0017067601 scopus 로고
    • Spinal cord disease in hereditary spherocytosis: report of two cases with a hypothesized common mechanism for neurologic and red cell abnormalities
    • McCann, S.R. and Jacob, H.S. (1976) Spinal cord disease in hereditary spherocytosis: report of two cases with a hypothesized common mechanism for neurologic and red cell abnormalities. Blood, 48, 259-263.
    • (1976) Blood , vol.48 , pp. 259-263
    • McCann, S.R.1    Jacob, H.S.2
  • 31
    • 0035128831 scopus 로고    scopus 로고
    • Propagation of action potentials in dendrites depends on dendritic morphology
    • Vetter, P., Roth, A. and Hausser, M. (2001) Propagation of action potentials in dendrites depends on dendritic morphology. J. Neurophysiol., 85, 926-937.
    • (2001) J. Neurophysiol. , vol.85 , pp. 926-937
    • Vetter, P.1    Roth, A.2    Hausser, M.3
  • 32
    • 33748943301 scopus 로고    scopus 로고
    • Non-conducting functions of voltage-gated ion channels
    • Kaczmarek, L.K. (2006) Non-conducting functions of voltage-gated ion channels. Nat. Rev. Neurosci., 7, 761-771.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 761-771
    • Kaczmarek, L.K.1
  • 33
    • 84869089377 scopus 로고    scopus 로고
    • Mutations of ANK3 identified by exome sequencing are associated with autism susceptibility
    • Bi, C., Wu, J., Jiang, T., Liu, Q., Cai, W., Yu, P., Cai, T., Zhao, M., Jiang, Y-H. and Sun, Z.S. (2012) Mutations of ANK3 identified by exome sequencing are associated with autism susceptibility. Human Mutation, 33, 1635-1638.
    • (2012) Human Mutation , vol.33 , pp. 1635-1638
    • Bi, C.1    Wu, J.2    Jiang, T.3    Liu, Q.4    Cai, W.5    Yu, P.6    Cai, T.7    Zhao, M.8    Jiang, Y.-H.9    Sun, Z.S.10
  • 35
    • 77956123201 scopus 로고    scopus 로고
    • Beta-III spectrin mutation L253P associated with spinocerebellar ataxia type 5 interferes with binding to Arp1 and protein trafficking from the Golgi
    • Clarkson, Y.L., Gillespie, T., Perkins, E.M., Lyndon, A.R. and Jackson, M. (2010) Beta-III spectrin mutation L253P associated with spinocerebellar ataxia type 5 interferes with binding to Arp1 and protein trafficking from the Golgi. Hum. Mol. Genet., 19, 3634-3641.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 3634-3641
    • Clarkson, Y.L.1    Gillespie, T.2    Perkins, E.M.3    Lyndon, A.R.4    Jackson, M.5
  • 36
    • 0031791601 scopus 로고    scopus 로고
    • An improved method for culturing cerebellar Purkinje cells with differentiated dendrites under a mixed monolayer setting
    • Furuya, S., Makino, A. and Hirabayashi, Y. (1998) An improved method for culturing cerebellar Purkinje cells with differentiated dendrites under a mixed monolayer setting. Brain Res. Protoc., 3, 192-198.
    • (1998) Brain Res. Protoc. , vol.3 , pp. 192-198
    • Furuya, S.1    Makino, A.2    Hirabayashi, Y.3
  • 37
    • 0024423656 scopus 로고
    • NMDA and non-NMDA receptors are co-localized at individual excitatory synapses in cultured rat hippocampus
    • Bekkers, J.M. and Stevens, C.F. (1989) NMDA and non-NMDA receptors are co-localized at individual excitatory synapses in cultured rat hippocampus. Nature, 341, 230-233.
    • (1989) Nature , vol.341 , pp. 230-233
    • Bekkers, J.M.1    Stevens, C.F.2


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