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Volumn 37, Issue 6, 2012, Pages 1277-1295

Classic 18.5- and 21.5-kDa myelin basic protein isoforms associate with cytoskeletal and SH3-domain proteins in the immortalized N19-oligodendroglial cell line stimulated by phorbol ester and IGF-1

Author keywords

Confocal microscopy; Cytoskeleton; Focal adhesion contacts; IGF 1; Laminin 2; Live cell imaging; Membrane ruffling; Myelination; Phorbol ester; TIRF microscopy

Indexed keywords

ACTIN; CORTACTIN; MEROSIN; MYELIN BASIC PROTEIN; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN ZO1; RECOMBINANT PROTEIN; SOMATOMEDIN C; THREONINE; TUBULIN;

EID: 84862851788     PISSN: 03643190     EISSN: 15736903     Source Type: Journal    
DOI: 10.1007/s11064-011-0700-2     Document Type: Article
Times cited : (29)

References (93)
  • 1
    • 0035066639 scopus 로고    scopus 로고
    • Biology of oligodendrocyte and myelin in the mammalian central nervous system
    • Baumann N, Pham-Dinh D (2001) Biology of oligodendrocyte and myelin in the mammalian central nervous system. Physiol Rev 81:871-927 (Pubitemid 32267079)
    • (2001) Physiological Reviews , vol.81 , Issue.2 , pp. 871-927
    • Baumann, N.1    Pham-Dinh, D.2
  • 2
    • 25144469422 scopus 로고    scopus 로고
    • Mechanisms of axon ensheathment and myelin growth
    • DOI 10.1038/nrn1743, PII NRN1743
    • Sherman DL, Brophy PJ (2005) Mechanisms of axon ensheathment and myelin growth. Nat Rev Neurosci 6:683-690 (Pubitemid 43160317)
    • (2005) Nature Reviews Neuroscience , vol.6 , Issue.9 , pp. 683-690
    • Sherman, D.L.1    Brophy, P.J.2
  • 3
    • 77649192930 scopus 로고    scopus 로고
    • Oligodendrocytes: Biology and pathology
    • Bradl M, Lassmann H (2010) Oligodendrocytes: biology and pathology. Acta Neuropathol 119:37-53
    • (2010) Acta Neuropathol , vol.119 , pp. 37-53
    • Bradl, M.1    Lassmann, H.2
  • 4
    • 78650177929 scopus 로고    scopus 로고
    • Cells of the oligodendroglial lineage, myelination, and remyelination
    • Miron VE, Kuhlmann T, Antel JP (2011) Cells of the oligodendroglial lineage, myelination, and remyelination. Biochim Biophys Acta 1812:184-193
    • (2011) Biochim Biophys Acta , vol.1812 , pp. 184-193
    • Miron, V.E.1    Kuhlmann, T.2    Antel, J.P.3
  • 5
    • 80053571190 scopus 로고    scopus 로고
    • CNS live imaging reveals a new mechanism of myelination: The liquid croissant model
    • doi:10.1002/glia.21228
    • Sobottka B, Ziegler U, Kaech A, Becher B, Goebels N (2011) CNS live imaging reveals a new mechanism of myelination: the liquid croissant model. Glia 59:1841-1849. doi:10.1002/glia.21228
    • (2011) Glia , vol.59 , pp. 1841-1849
    • Sobottka, B.1    Ziegler, U.2    Kaech, A.3    Becher, B.4    Goebels, N.5
  • 6
    • 80053109845 scopus 로고    scopus 로고
    • Central nervous system myelin: Structure, synthesis and assembly
    • Aggarwal S, Yurlova L, Simons M (2011) Central nervous system myelin: structure, synthesis and assembly. Trends Cell Biol 21:585-593
    • (2011) Trends Cell Biol , vol.21 , pp. 585-593
    • Aggarwal, S.1    Yurlova, L.2    Simons, M.3
  • 7
    • 77952886177 scopus 로고    scopus 로고
    • The multiple roles of myelin protein genes during the development of the oligodendrocyte
    • Fulton D, Paez PM, Campagnoni AT (2010) The multiple roles of myelin protein genes during the development of the oligodendrocyte. ASN Neuro 2:e00027
    • (2010) ASN Neuro , vol.2
    • Fulton, D.1    Paez, P.M.2    Campagnoni, A.T.3
  • 8
    • 33748487414 scopus 로고    scopus 로고
    • Myelin basic protein: A multifunctional protein
    • DOI 10.1007/s00018-006-6094-7
    • Boggs JM (2006) Myelin basic protein: a multifunctional protein. Cell Mol Life Sci 63:1945-1961 (Pubitemid 44359737)
    • (2006) Cellular and Molecular Life Sciences , vol.63 , Issue.17 , pp. 1945-1961
    • Boggs, J.M.1
  • 9
    • 33750436896 scopus 로고    scopus 로고
    • Myelin basic protein-dependent plasma membrane reorganization in the formation of myelin
    • DOI 10.1038/sj.emboj.7601376, PII 7601376
    • Fitzner D, Schneider A, Kippert A, Mobius W, Willig KI, Hell SW, Bunt G, Gaus K, Simons M (2006) Myelin basic proteindependent plasma membrane reorganization in the formation of myelin. EMBO J 25:5037-5048 (Pubitemid 44658522)
    • (2006) EMBO Journal , vol.25 , Issue.21 , pp. 5037-5048
    • Fitzner, D.1    Schneider, A.2    Kippert, A.3    Mobius, W.4    Willig, K.I.5    Hell, S.W.6    Bunt, G.7    Gaus, K.8    Simons, M.9
  • 10
    • 64849102424 scopus 로고    scopus 로고
    • Nova Science Publishers, Hauppauge, NY
    • Boggs JM (2008) Myelin basic protein. Nova Science Publishers, Hauppauge, NY
    • (2008) Myelin Basic Protein
    • Boggs, J.M.1
  • 11
    • 69249131573 scopus 로고    scopus 로고
    • The classic basic protein of myelin - Conserved structural motifs and the dynamic molecular barcode involved in membrane adhesion and protein-protein interactions
    • Harauz G, Libich DS (2009) The classic basic protein of myelin - conserved structural motifs and the dynamic molecular barcode involved in membrane adhesion and protein-protein interactions. Current Protein and Peptide Science 10:196-215
    • (2009) Current Protein and Peptide Science , vol.10 , pp. 196-215
    • Harauz, G.1    Libich, D.S.2
  • 12
    • 69249091013 scopus 로고    scopus 로고
    • Structural polymorphism and multifunctionality of myelin basic protein
    • Harauz G, Ladizhansky V, Boggs JM (2009) Structural polymorphism and multifunctionality of myelin basic protein. Biochemistry 48:8094-8104
    • (2009) Biochemistry , vol.48 , pp. 8094-8104
    • Harauz, G.1    Ladizhansky, V.2    Boggs, J.M.3
  • 14
    • 0035889536 scopus 로고    scopus 로고
    • Expression and regulation of golli products of myelin basic protein gene during in vitro development of oligodendrocytes
    • DOI 10.1002/jnr.10031
    • Givogri MI, Bongarzone ER, Schonmann V, Campagnoni AT (2001) Expression and regulation of golli products of myelin basic protein gene during in vitro development of oligodendrocytes. J Neurosci Res 66:679-690 (Pubitemid 33032337)
    • (2001) Journal of Neuroscience Research , vol.66 , Issue.4 , pp. 679-690
    • Givogri, M.I.1    Bongarzone, E.R.2    Schonmann, V.3    Campagnoni, A.T.4
  • 15
    • 3042553626 scopus 로고    scopus 로고
    • Myelin basic protein - Diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis
    • DOI 10.1016/j.micron.2004.04.005, PII S0968432804000964
    • Harauz G, Ishiyama N, Hill CMD, Bates IR, Libich DS, Farès C (2004) Myelin basic protein - diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis. Micron 35:503-542 (Pubitemid 38836830)
    • (2004) Micron , vol.35 , Issue.7 , pp. 503-542
    • Harauz, G.1    Ishiyama, N.2    Hill, C.M.D.3    Bates, I.R.4    Libich, D.S.5    Fares, C.6
  • 16
    • 37849026077 scopus 로고    scopus 로고
    • Binding of the proline-rich segment of myelin basic protein to SH3-domains - Spectroscopic, microarray, and modelling studies of ligand conformation and effects of post-translational modifications
    • Polverini E, Rangaraj G, Libich DS, Boggs JM, Harauz G (2008) Binding of the proline-rich segment of myelin basic protein to SH3-domains - spectroscopic, microarray, and modelling studies of ligand conformation and effects of post-translational modifications. Biochemistry 47:267-282
    • (2008) Biochemistry , vol.47 , pp. 267-282
    • Polverini, E.1    Rangaraj, G.2    Libich, D.S.3    Boggs, J.M.4    Harauz, G.5
  • 17
    • 77955586355 scopus 로고    scopus 로고
    • Interaction of myelin basic protein with actin in the presence of dodecylphosphocholine micelles
    • Bamm VV, Ahmed MA, Harauz G (2010) Interaction of myelin basic protein with actin in the presence of dodecylphosphocholine micelles. Biochemistry 49:6903-6915
    • (2010) Biochemistry , vol.49 , pp. 6903-6915
    • Bamm, V.V.1    Ahmed, M.A.2    Harauz, G.3
  • 18
    • 80052461749 scopus 로고    scopus 로고
    • Structured functional domains of myelin basic protein: Cross talk between actin polymerization and Ca(2+)-dependent calmodulin interaction
    • Bamm VV, De Avila M, Smith GST, Ahmed MA, Harauz G (2011) Structured functional domains of myelin basic protein: cross talk between actin polymerization and Ca(2+)-dependent calmodulin interaction. Biophys J 101:1248-1256
    • (2011) Biophys J , vol.101 , pp. 1248-1256
    • Bamm, V.V.1    De Avila, M.2    Gst, S.3    Ahmed, M.A.4    Harauz, G.5
  • 20
    • 2942627583 scopus 로고    scopus 로고
    • Connexin47, connexin29 and connexin32 co-expression in oligodendrocytes and Cx47 association with zonula occludens-1 (ZO-1) in mouse brain
    • DOI 10.1016/j.neuroscience.2004.03.063, PII S0306452204002490
    • Li X, Ionescu AV, Lynn BD, Lu S, Kamasawa N, Morita M, Davidson KG, Yasumura T, Rash JE, Nagy JI (2004) Connexin47, connexin29 and connexin32 co-expression in oligodendrocytes and Cx47 association with zonula occludens-1 (ZO-1) in mouse brain. Neuroscience 126:611-630 (Pubitemid 38759255)
    • (2004) Neuroscience , vol.126 , Issue.3 , pp. 611-630
    • Li, X.1    Ionescu, A.V.2    Lynn, B.D.3    Lu, S.4    Kamasawa, N.5    Morita, M.6    Davidson, K.G.V.7    Yasumura, T.8    Rash, J.E.9    Nagy, J.I.10
  • 21
    • 23244464404 scopus 로고    scopus 로고
    • Expression of zonula occludens-1 (ZO-1) and the transcription factor ZO-1-associated nucleic acid-binding protein (ZONAB)-MsY3 in glial cells and colocalization at oligodendrocyte and astrocyte gap junctions in mouse brain
    • DOI 10.1111/j.1460-9568.2005.04225.x
    • Penes MC, Li X, Nagy JI (2005) Expression of zonula occludens-1 (ZO-1) and the transcription factor ZO-1-associated nucleic acid-binding protein (ZONAB)-MsY3 in glial cells and colocalization at oligodendrocyte and astrocyte gap junctions in mouse brain. Eur J Neurosci 22:404-418 (Pubitemid 41097614)
    • (2005) European Journal of Neuroscience , vol.22 , Issue.2 , pp. 404-418
    • Penes, M.C.1    Li, X.2    Nagy, J.I.3
  • 23
    • 13844269553 scopus 로고    scopus 로고
    • Effect of arginine loss in myelin basic protein, as occurs in its deiminated charge isoform, on mediation of actin polymerization and actin binding to a lipid membrane in vitro
    • DOI 10.1021/bi0473760
    • Boggs JM, Rangaraj G, Hill CMD, Bates IR, Heng YM, Harauz G (2005) Effect of arginine loss in myelin basic protein, as occurs in its deiminated charge isoform, on mediation of actin polymerization and actin binding to a lipid membrane in vitro. Biochemistry 44:3524-3534 (Pubitemid 40322022)
    • (2005) Biochemistry , vol.44 , Issue.9 , pp. 3524-3534
    • Boggs, J.M.1    Rangaraj, G.2    Hill, C.M.D.3    Bates, I.R.4    Heng, Y.-M.5    Harauz, G.6
  • 24
    • 13844298216 scopus 로고    scopus 로고
    • Charge effects modulate actin assembly by classic myelin basic protein isoforms
    • DOI 10.1016/j.bbrc.2005.01.151
    • Hill CMD, Harauz G (2005) Charge effects modulate actin assembly by classic myelin basic protein isoforms. Biochem Biophys Res Commun 329:362-369 (Pubitemid 40255462)
    • (2005) Biochemical and Biophysical Research Communications , vol.329 , Issue.1 , pp. 362-369
    • Hill, C.M.D.1    Harauz, G.2
  • 25
    • 0034604261 scopus 로고    scopus 로고
    • Interaction of lipid-bound myelin basic protein with actin filaments and calmodulin
    • DOI 10.1021/bi0002129
    • Boggs JM, Rangaraj G (2000) Interaction of lipid-bound myelin basic protein with actin filaments and calmodulin. Biochemistry 39:7799-7806 (Pubitemid 30439608)
    • (2000) Biochemistry , vol.39 , Issue.26 , pp. 7799-7806
    • Boggs, J.M.1    Rangaraj, G.2
  • 26
    • 78651262578 scopus 로고    scopus 로고
    • Myelin basic protein binds microtubules to a membrane surface and to actin filaments in vitro: Effect of phosphorylation and deimination
    • Boggs JM, Rangaraj G, Heng YM, Liu Y, Harauz G (2011) Myelin basic protein binds microtubules to a membrane surface and to actin filaments in vitro: effect of phosphorylation and deimination. Biochim Biophys Acta 1808:761-773
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 761-773
    • Boggs, J.M.1    Rangaraj, G.2    Heng, Y.M.3    Liu, Y.4    Harauz, G.5
  • 27
    • 29244451550 scopus 로고    scopus 로고
    • Assembly of tubulin by classic myelin basic protein isoforms and regulation by post-translational modification
    • DOI 10.1021/bi050646+
    • Hill CMD, Libich DS, Harauz G (2005) Assembly of tubulin by classic myelin basic protein isoforms and regulation by posttranslational modification. Biochemistry 44:16672-16683 (Pubitemid 41832047)
    • (2005) Biochemistry , vol.44 , Issue.50 , pp. 16672-16683
    • Hill, C.M.D.1    Libich, D.S.2    Harauz, G.3
  • 28
    • 0026655772 scopus 로고
    • Ca(2+)-calmodulin regulated effectors of microtubule stability in bovine brain
    • Pirollet F, Derancourt J, Haiech J, Job D, Margolis RL (1992) Ca(2+)-calmodulin regulated effectors of microtubule stability in bovine brain. Biochemistry 31:8849-8855
    • (1992) Biochemistry , vol.31 , pp. 8849-8855
    • Pirollet, F.1    Derancourt, J.2    Haiech, J.3    Job, D.4    Margolis, R.L.5
  • 31
    • 0035869417 scopus 로고    scopus 로고
    • Organization and functional roles of the cytoskeleton in oligodendrocytes
    • DOI 10.1002/jemt.1047
    • Richter-Landsberg C (2001) Organization and functional roles of the cytoskeleton in oligodendrocytes. Microsc Res Tech 52:628-636 (Pubitemid 32222190)
    • (2001) Microscopy Research and Technique , vol.52 , Issue.6 , pp. 628-636
    • Richter-Landsberg, C.1
  • 32
    • 45949106557 scopus 로고    scopus 로고
    • The cytoskeleton in oligodendrocytes: Microtubule dynamics in health and disease
    • Richter-Landsberg C (2008) The cytoskeleton in oligodendrocytes: microtubule dynamics in health and disease. J Mol Neurosci 35:55-63
    • (2008) J Mol Neurosci , vol.35 , pp. 55-63
    • Richter-Landsberg, C.1
  • 33
    • 71249151075 scopus 로고    scopus 로고
    • Role of the oligodendroglial cytoskeleton in differentiation and myelination
    • Bauer NG, Richter-Landsberg C, Ffrench-Constant C (2009) Role of the oligodendroglial cytoskeleton in differentiation and myelination. Glia 57:1691-1705
    • (2009) Glia , vol.57 , pp. 1691-1705
    • Bauer, N.G.1    Richter-Landsberg, C.2    Ffrench-Constant, C.3
  • 34
    • 64849090288 scopus 로고    scopus 로고
    • Influence of membrane surface charge and post-translational modifications to myelin basic protein on its ability to tether the Fyn-SH3 domain to a membrane in vitro
    • Homchaudhuri L, Polverini E, Gao W, Harauz G, Boggs JM (2009) Influence of membrane surface charge and post-translational modifications to myelin basic protein on its ability to tether the Fyn-SH3 domain to a membrane in vitro. Biochemistry 48:2385-2393
    • (2009) Biochemistry , vol.48 , pp. 2385-2393
    • Homchaudhuri, L.1    Polverini, E.2    Gao, W.3    Harauz, G.4    Boggs, J.M.5
  • 35
    • 80052434381 scopus 로고    scopus 로고
    • Proline substitutions and threonine pseudophosphorylation of the SH3 ligand of 18.5-kDa myelin basic protein decrease its affinity for the Fyn-SH3 domain and alter process development and protein localization in oligodendrocytes
    • Smith GS, De AM, Paez PM, Spreuer V, Wills MK, Jones N, Boggs JM, Harauz G (2012) Proline substitutions and threonine pseudophosphorylation of the SH3 ligand of 18.5-kDa myelin basic protein decrease its affinity for the Fyn-SH3 domain and alter process development and protein localization in oligodendrocytes. J Neurosci Res 90:28-47
    • (2012) J Neurosci Res , vol.90 , pp. 28-47
    • Smith, G.S.1    De Am Paez, P.M.2    Spreuer, V.3    Wills, M.K.4    Jones, N.5    Boggs, J.M.6    Harauz, G.7
  • 37
    • 0036025305 scopus 로고    scopus 로고
    • An Arg/Lys → Gln mutant of recombinant murine myelin basic protein as a mimic of the deiminated form implicated in multiple sclerosis
    • DOI 10.1016/S1046-5928(02)00017-7, PII S1046592802000177
    • Bates IR, Libich DS, Wood DD, Moscarello MA, Harauz G (2002) An Arg/Lys → Gln mutant of recombinant murine myelin basic protein as a mimic of the deiminated form implicated in multiple sclerosis. Protein Expr Purif 25:330-341 (Pubitemid 35307518)
    • (2002) Protein Expression and Purification , vol.25 , Issue.2 , pp. 330-341
    • Bates, I.R.1    Libich, D.S.2    Wood, D.D.3    Moscarello, M.A.4    Harauz, G.5
  • 38
    • 79751472668 scopus 로고    scopus 로고
    • Classical 18.5- and 21.5-kDa isoforms of myelin basic protein inhibit calcium influx into oligodendroglial cells, in contrast to golli isoforms
    • Smith GST, Paez PM, Spreuer V, Campagnoni CW, Boggs JM, Campagnoni AT, Harauz G (2011) Classical 18.5- and 21.5-kDa isoforms of myelin basic protein inhibit calcium influx into oligodendroglial cells, in contrast to golli isoforms. J Neurosci Res 89:467-480
    • (2011) J Neurosci Res , vol.89 , pp. 467-480
    • Smith, G.S.T.1    Paez, P.M.2    Spreuer, V.3    Campagnoni, C.W.4    Boggs, J.M.5    Campagnoni, A.T.6    Harauz, G.7
  • 39
    • 0036367467 scopus 로고    scopus 로고
    • A ZO1-GFP fusion protein to study the dynamics of tight junctions in living cells
    • DOI 10.1007/s00418-002-0398-y
    • Riesen FK, Rothen-Rutishauser B, Wunderli-Allenspach H (2002) A ZO1-GFP fusion protein to study the dynamics of tight junctions in living cells. Histochem Cell Biol 117:307-315 (Pubitemid 34985036)
    • (2002) Histochemistry and Cell Biology , vol.117 , Issue.4 , pp. 307-315
    • Riesen, F.K.1    Rothen-Rutishauser, B.2    Wunderli-Allenspach, H.3
  • 41
    • 0028298724 scopus 로고
    • Volume and surface area measurement of viable chondrocytes in situ using geometric modelling of serial confocal sections
    • Guilak F (1994) Volume and surface area measurement of viable chondrocytes in situ using geometric modelling of serial confocal sections. J Microsc 173:245-256 (Pubitemid 24173203)
    • (1994) Journal of Microscopy , vol.173 , Issue.3 , pp. 245-256
    • Guilak, F.1
  • 43
    • 78649432637 scopus 로고    scopus 로고
    • Dystroglycan modulates the ability of insulin-like growth factor-1 to promote oligodendrocyte differentiation
    • Galvin J, Eyermann C, Colognato H (2010) Dystroglycan modulates the ability of insulin-like growth factor-1 to promote oligodendrocyte differentiation. J Neurosci Res 88:3295-3307
    • (2010) J Neurosci Res , vol.88 , pp. 3295-3307
    • Galvin, J.1    Eyermann, C.2    Colognato, H.3
  • 44
    • 0027509316 scopus 로고
    • Expression of myelin protein genes and other myelin components in an oligodendrocytic cell line conditionally immortalized with a temperature- sensitive retrovirus
    • DOI 10.1111/j.1471-4159.1993.tb03188.x
    • Verity AN, Bredesen D, Vonderscher C, Handley VW, Campagnoni AT (1993) Expression of myelin protein genes and other myelin components in an oligodendrocytic cell line conditionally immortalized with a temperature-sensitive retrovirus. J Neurochem 60:577-587 (Pubitemid 23030954)
    • (1993) Journal of Neurochemistry , vol.60 , Issue.2 , pp. 577-587
    • Verity, A.N.1    Bredesen, D.2    Vonderscher, C.3    Handley, V.W.4    Campagnoni, A.T.5
  • 45
    • 0027761083 scopus 로고
    • Generation and analysis of normal and shiverer temperature-sensitive immortalized cell lines exhibiting phenotypic characteristics of oligodendrocytes at several stages of differentiation
    • Foster LM, Phan T, Verity AN, Bredesen D, Campagnoni AT (1993) Generation and analysis of normal and shiverer temperature-sensitive immortalized cell lines exhibiting phenotypic characteristics of oligodendrocytes at several stages of differentiation. Dev Neurosci 15:100-109 (Pubitemid 24053211)
    • (1993) Developmental Neuroscience , vol.15 , Issue.2 , pp. 100-109
    • Foster, L.M.1    Phan, T.2    Verity, A.N.3    Bredesen, D.4    Campagnoni, A.T.5
  • 46
    • 36248949702 scopus 로고    scopus 로고
    • Increased expression of golli myelin basic proteins enhances calcium influx into oligodendroglial cells
    • DOI 10.1523/JNEUROSCI.2381-07.2007
    • Paez PM, Spreuer V, Handley V, Feng JM, Campagnoni C, Campagnoni AT (2007) Increased expression of golli myelin basic proteins enhances calcium influx into oligodendroglial cells. J Neurosci 27:12690-12699 (Pubitemid 350127809)
    • (2007) Journal of Neuroscience , vol.27 , Issue.46 , pp. 12690-12699
    • Paez, P.M.1    Spreuer, V.2    Handley, V.3    Feng, J.-M.4    Campagnoni, C.5    Campagnoni, A.T.6
  • 48
    • 70449435949 scopus 로고    scopus 로고
    • Fyn kinase is involved in oligodendroglial cell differentiation induced by apotransferrin
    • Perez MJ, Ortiz EH, Roffe M, Soto EF, Pasquini JM (2009) Fyn kinase is involved in oligodendroglial cell differentiation induced by apotransferrin. J Neurosci Res 87:3378-3389
    • (2009) J Neurosci Res , vol.87 , pp. 3378-3389
    • Perez, M.J.1    Ortiz, E.H.2    Roffe, M.3    Soto, E.F.4    Pasquini, J.M.5
  • 51
    • 0030946002 scopus 로고    scopus 로고
    • The active transport of myelin basic protein into the nucleus suggests a regulatory role in myelination
    • Pedraza L, Fidler L, Staugaitis SM, Colman DR (1997) The active transport of myelin basic protein into the nucleus suggests a regulatory role in myelination. Neuron 18:579-589 (Pubitemid 27194638)
    • (1997) Neuron , vol.18 , Issue.4 , pp. 579-589
    • Pedraza, L.1    Fidler, L.2    Staugaitis, S.M.3    Colman, D.R.4
  • 52
    • 0030853075 scopus 로고    scopus 로고
    • Nuclear transport of myelin basic protein
    • DOI 10.1002/(SICI)1097-4547(19971015)50:2<258::AID-JNR14>3.0.CO;2-4
    • Pedraza L (1997) Nuclear transport of myelin basic protein. J Neurosci Res 50:258-264 (Pubitemid 27473641)
    • (1997) Journal of Neuroscience Research , vol.50 , Issue.2 , pp. 258-264
    • Pedraza, L.1
  • 53
    • 0036297398 scopus 로고    scopus 로고
    • Phorbol myristate acetate induces ruffling of the acrosome of human sperm
    • DOI 10.1016/S0015-0282(02)03166-7, PII S0015028202031667
    • Liu DY, Martic M, Grkovic I, Garrett C, Dunlop ME, Baker HW (2002) Phorbol myristate acetate induces ruffling of the acrosome of human sperm. Fertil Steril 78:128-136 (Pubitemid 34722682)
    • (2002) Fertility and Sterility , vol.78 , Issue.1 , pp. 128-136
    • Liu, D.Y.1    Martic, M.2    Grkovic, I.3    Garrett, C.4    Dunlop, M.E.5    Baker H.W.Gordon6
  • 54
    • 0032773274 scopus 로고    scopus 로고
    • Morphological changes in the Golgi complex correlate with actin cytoskeleton rearrangements
    • DOI 10.1002/(SICI)1097-0169(1999)43:4<334::AID-CM6>3.0.CO;2-3
    • di Campli A, Valderrama F, Babia T, De Matteis MA, Luini A, Egea G (1999) Morphological changes in the Golgi complex correlate with actin cytoskeleton rearrangements. Cell Motil Cytoskelet 43:334-348 (Pubitemid 29368206)
    • (1999) Cell Motility and the Cytoskeleton , vol.43 , Issue.4 , pp. 334-348
    • Di Campli, A.1    Valderrama, F.2    Babia, T.3    De Matteis, M.A.4    Luini, A.5    Egea, G.6
  • 55
    • 0031034456 scopus 로고    scopus 로고
    • Role of extracellular signal-regulated protein kinases 1 and 2 in oligodendroglial process extension
    • Stariha RL, Kikuchi S, Siow YL, Pelech SL, Kim M, Kim SU (1997) Role of extracellular signal-regulated protein kinases 1 and 2 in oligodendroglial process extension. J Neurochem 68:945-953 (Pubitemid 27086198)
    • (1997) Journal of Neurochemistry , vol.68 , Issue.3 , pp. 945-953
    • Stariha, R.L.1    Kikuchi, S.2    Siow, Y.L.3    Pelech, S.L.4    Kim, M.5    Kim, S.U.6
  • 57
    • 0028176874 scopus 로고
    • Protein kinase FA/glycogen synthase kinase-3 predominantly phosphorylates the in vivo site Thr97-Pro in brain myelin basic protein: Evidence for Thr-Pro and Ser-Arg-X-X-Ser as consensus sequence motifs
    • Yu JS, Yang SD (1994) Protein kinase FA/glycogen synthase kinase-3 predominantly phosphorylates the in vivo site Thr97-Pro in brain myelin basic protein: evidence for Thr-Pro and Ser-Arg-X-X-Ser as consensus sequence motifs. J Neurochem 62: 1596-1603
    • (1994) J Neurochem , vol.62 , pp. 1596-1603
    • Yu, J.S.1    Yang, S.D.2
  • 58
    • 0030717725 scopus 로고    scopus 로고
    • Insulin-like growth factors regulate neuronal differentiation and survival
    • DOI 10.1006/nbdi.1997.0156
    • Feldman EL, Sullivan KA, Kim B, Russell JW (1997) Insulin-like growth factors regulate neuronal differentiation and survival. Neurobiol Dis 4:201-214 (Pubitemid 27465510)
    • (1997) Neurobiology of Disease , vol.4 , Issue.3-4 , pp. 201-214
    • Feldman, E.L.1    Sullivan, K.A.2    Kim, B.3    Russell, J.W.4
  • 59
    • 0034282454 scopus 로고    scopus 로고
    • GTPases and phosphatidylinositol 3-kinase are critical for insulin-like growth factor-I-mediated Schwann cell motility
    • Cheng HL, Steinway ML, Russell JW, Feldman EL (2000) GTPases and phosphatidylinositol 3-kinase are critical for insulin-like growth factor-I-mediated Schwann cell motility. J Biol Chem 275:27197-27204
    • (2000) J Biol Chem , vol.275 , pp. 27197-27204
    • Cheng, H.L.1    Steinway, M.L.2    Russell, J.W.3    Feldman, E.L.4
  • 60
    • 32144433831 scopus 로고    scopus 로고
    • Use of TIRF microscopy to visualize actin and microtubules in migrating cells
    • Manneville JB (2006) Use of TIRF microscopy to visualize actin and microtubules in migrating cells. Methods Enzymol 406: 520-532
    • (2006) Methods Enzymol , vol.406 , pp. 520-532
    • Manneville, J.B.1
  • 61
    • 77955596267 scopus 로고    scopus 로고
    • Microtubule dynamics at the cell cortex probed by TIRF microscopy
    • Grigoriev I, Akhmanova A (2010) Microtubule dynamics at the cell cortex probed by TIRF microscopy. Methods Cell Biol 97:91-109
    • (2010) Methods Cell Biol , vol.97 , pp. 91-109
    • Grigoriev, I.1    Akhmanova, A.2
  • 62
    • 70349305427 scopus 로고    scopus 로고
    • Using total internal reflection fluorescence (TIRF) microscopy to visualize cortical actin and microtubules in the drosophila syncytial embryo
    • Webb RL, Rozov O, Watkins SC, McCartney BM (2009) Using total internal reflection fluorescence (TIRF) microscopy to visualize cortical actin and microtubules in the drosophila syncytial embryo. Dev Dyn 238:2622-2632
    • (2009) Dev Dyn , vol.238 , pp. 2622-2632
    • Webb, R.L.1    Rozov, O.2    Watkins, S.C.3    McCartney, B.M.4
  • 63
    • 57949112733 scopus 로고    scopus 로고
    • Chapter 7: Total internal reflection fluorescence microscopy
    • Axelrod D (2008) Chapter 7: total internal reflection fluorescence microscopy. Methods Cell Biol 89:169-221
    • (2008) Methods Cell Biol , vol.89 , pp. 169-221
    • Axelrod, D.1
  • 64
    • 50649090270 scopus 로고    scopus 로고
    • Cortactin branches out: Roles in regulating protrusive actin dynamics
    • Ammer AG, Weed SA (2008) Cortactin branches out: roles in regulating protrusive actin dynamics. Cell Motil Cytoskeleton 65:687-707
    • (2008) Cell Motil Cytoskeleton , vol.65 , pp. 687-707
    • Ammer, A.G.1    Weed, S.A.2
  • 65
    • 0035012459 scopus 로고    scopus 로고
    • Cytoskeletal reorganization during the formation of oligodendrocyte processes and branches
    • DOI 10.1006/mcne.2001.0974
    • Song J, Goetz BD, Baas PW, Duncan ID (2001) Cytoskeletal reorganization during the formation of oligodendrocyte processes and branches. Mol Cell Neurosci 17:624-636 (Pubitemid 32430039)
    • (2001) Molecular and Cellular Neuroscience , vol.17 , Issue.4 , pp. 624-636
    • Song, J.1    Goetz, B.D.2    Baas, P.W.3    Duncan, L.D.4
  • 66
    • 15744393174 scopus 로고    scopus 로고
    • Doublecortin association with actin filaments is regulated by neurabin II
    • DOI 10.1074/jbc.M405525200
    • Tsukada M, Prokscha A, Ungewickell E, Eichele G (2005) Doublecortin association with actin filaments is regulated by neurabin II. J Biol Chem 280:11361-11368 (Pubitemid 40418444)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11361-11368
    • Tsukada, M.1    Prokscha, A.2    Ungewickell, E.3    Eichele, G.4
  • 67
    • 0036469248 scopus 로고    scopus 로고
    • Process outgrowth of oligodendrocytes is promoted by interaction of Fyn kinase with the cytoskeletal protein Tau
    • Klein C, Kramer EM, Cardine AM, Schraven B, Brandt R, Trotter J (2002) Process outgrowth of oligodendrocytes is promoted by interaction of Fyn kinase with the cytoskeletal protein tau. J Neurosci 22:698-707 (Pubitemid 34141750)
    • (2002) Journal of Neuroscience , vol.22 , Issue.3 , pp. 698-707
    • Klein, C.1    Kramer, E.-M.2    Cardine, A.-M.3    Schraven, B.4    Brandt, R.5    Trotter, J.6
  • 68
    • 0024442564 scopus 로고
    • Organization of oligodendroglial membrane sheets. I: Association of myelin basic protein and 2',3'-cyclic nucleotide 3'-phosphohydrolase with cytoskeleton
    • Dyer CA, Benjamins JA (1989) Organization of oligodendroglial membrane sheets. I: association of myelin basic protein and 2′,3′-cyclic nucleotide 3′-phosphohydrolase with cytoskeleton. J Neurosci Res 24:201-211 (Pubitemid 19261871)
    • (1989) Journal of Neuroscience Research , vol.24 , Issue.2 , pp. 201-211
    • Dyer, C.A.1    Benjamins, J.A.2
  • 70
    • 24944525686 scopus 로고    scopus 로고
    • Two types of detergent-insoluble, glycosphingolipid/cholesterol-rich membrane domains from isolated myelin
    • DOI 10.1111/j.1471-4159.2005.03331.x
    • Arvanitis DN, Min W, Gong Y, Heng YM, Boggs JM (2005) Two types of detergent-insoluble, glycosphingolipid/cholesterol-rich membrane domains from isolated myelin. J Neurochem 94:1696-1710 (Pubitemid 41324650)
    • (2005) Journal of Neurochemistry , vol.94 , Issue.6 , pp. 1696-1710
    • Arvanitis, D.N.1    Min, W.2    Gong, Y.3    Heng, Y.M.4    Boggs, J.M.5
  • 72
    • 0033519348 scopus 로고    scopus 로고
    • Claudin-11/OSP-based tight junctions of myelin sheaths in brain and Sertoli cells in testis
    • DOI 10.1083/jcb.145.3.579
    • Morita K, Sasaki H, Fujimoto K, Furuse M, Tsukita S (1999) Claudin-11/OSP-based tight junctions of myelin sheaths in brain and Sertoli cells in testis. J Cell Biol 145:579-588 (Pubitemid 29215721)
    • (1999) Journal of Cell Biology , vol.145 , Issue.3 , pp. 579-588
    • Morita, K.1    Sasaki, H.2    Fujimoto, K.3    Furuse, M.4    Tsukita, S.5
  • 73
    • 33846926110 scopus 로고    scopus 로고
    • White matter rafting - Membrane microdomains in myelin
    • DOI 10.1007/s11064-006-9137-4
    • DeBruin LS, Harauz G (2007) White matter rafting - membrane microdomains in myelin. Neurochem Res 32:213-228 (Pubitemid 46238867)
    • (2007) Neurochemical Research , vol.32 , Issue.2 , pp. 213-228
    • DeBruin, L.S.1    Harauz, G.2
  • 74
    • 78650619555 scopus 로고    scopus 로고
    • Conformational choreography of a molecular switch region in myelin basic protein-molecular dynamics shows induced folding and secondary structure type conversion upon threonyl phosphorylation in both aqueous and membrane-associated environments
    • Polverini E, Coll EP, Tieleman DP, Harauz G (2011) Conformational choreography of a molecular switch region in myelin basic protein-molecular dynamics shows induced folding and secondary structure type conversion upon threonyl phosphorylation in both aqueous and membrane-associated environments. Biochim Biophys Acta 1808:674-683
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 674-683
    • Polverini, E.1    Coll, E.P.2    Tieleman, D.P.3    Harauz, G.4
  • 75
    • 77949629794 scopus 로고    scopus 로고
    • Misincorporation of the proline homologue Aze (azetidine-2-carboxylic acid) into recombinant myelin basic protein
    • Bessonov K, Bamm VV, Harauz G (2010) Misincorporation of the proline homologue Aze (azetidine-2-carboxylic acid) into recombinant myelin basic protein. Phytochemistry 71:502-507
    • (2010) Phytochemistry , vol.71 , pp. 502-507
    • Bessonov, K.1    Bamm, V.V.2    Harauz, G.3
  • 76
    • 0032840879 scopus 로고    scopus 로고
    • Regulation of myelin basic protein phosphorylation by mitogen-activated protein kinase during increased action potential firing in the hippocampus
    • DOI 10.1046/j.1471-4159.1999.0731090.x
    • Atkins CM, Yon M, Groome NP, Sweatt JD (1999) Regulation of myelin basic protein phosphorylation by mitogen-activated protein kinase during increased action potential firing in the hippocampus. J Neurochem 73:1090-1097 (Pubitemid 29395466)
    • (1999) Journal of Neurochemistry , vol.73 , Issue.3 , pp. 1090-1097
    • Atkins, C.M.1    Yon, M.2    Groome, N.P.3    Sweatt, J.D.4
  • 77
    • 0142234077 scopus 로고    scopus 로고
    • Multiple sclerosis: An important role for post-translational modifications of myelin basic protein in pathogenesis
    • Kim JK, Mastronardi FG, Wood DD, Lubman DM, Zand R, Moscarello MA (2003) Multiple sclerosis: an important role for post-translational modifications of myelin basic protein in pathogenesis. Mol Cell Proteomics 2:453-462
    • (2003) Mol Cell Proteomics , vol.2 , pp. 453-462
    • Kim, J.K.1    Mastronardi, F.G.2    Wood, D.D.3    Lubman, D.M.4    Zand, R.5    Moscarello, M.A.6
  • 78
    • 0023753477 scopus 로고
    • Endogenous phosphorylation of basic protein in myelin of varying degrees of compaction
    • Schulz P, Cruz TF, Moscarello MA (1988) Endogenous phosphorylation of basic protein in myelin of varying degrees of compaction. Biochemistry 27:7793-7799
    • (1988) Biochemistry , vol.27 , pp. 7793-7799
    • Schulz, P.1    Cruz, T.F.2    Moscarello, M.A.3
  • 79
    • 33947371742 scopus 로고    scopus 로고
    • Partitioning of myelin basic protein into membrane microdomains in a spontaneously demyelinating mouse model for multiple sclerosis
    • DOI 10.1139/O06-180
    • DeBruin LS, Haines JD, Bienzle D, Harauz G (2006) Partitioning of myelin basic protein into membrane microdomains in a spontaneously demyelinating mouse model for multiple sclerosis. Biochem Cell Biol 84:993-1005 (Pubitemid 46450698)
    • (2006) Biochemistry and Cell Biology , vol.84 , Issue.6 , pp. 993-1005
    • DeBruin, L.S.1    Haines, J.D.2    Bienzle, D.3    Harauz, G.4
  • 80
    • 30644473886 scopus 로고    scopus 로고
    • Myelin basic protein, an autoantigen in multiple sclerosis, is selectively processed by human trypsin 4
    • DOI 10.1016/j.febslet.2005.12.067, PII S0014579305015528
    • Medveczky P, Antal J, Patthy A, Kekesi K, Juhasz G, Szilagyi L, Graf L (2006) Myelin basic protein, an autoantigen in multiple sclerosis, is selectively processed by human trypsin 4. FEBS Lett 580:545-552 (Pubitemid 43089684)
    • (2006) FEBS Letters , vol.580 , Issue.2 , pp. 545-552
    • Medveczky, P.1    Antal, J.2    Patthy, A.3    Kekesi, K.4    Juhasz, G.5    Szilagyi, L.6    Graf, L.7
  • 82
    • 0024334338 scopus 로고
    • Secondary structure of charge isomers of myelin basic protein before and after phosphorylation
    • Ramwani JJ, Epand RM, Moscarello MA (1989) Secondary structure of charge isomers of myelin basic protein before and after phosphorylation. Biochemistry 28:6538-6543 (Pubitemid 19208302)
    • (1989) Biochemistry , vol.28 , Issue.16 , pp. 6538-6543
    • Ramwani, J.J.1    Epand, R.M.2    Moscarello, M.A.3
  • 83
    • 30744479193 scopus 로고    scopus 로고
    • Effect of phosphorylation of myelin basic protein by MAPK on its interactions with actin and actin binding to a lipid membrane in vitro
    • DOI 10.1021/bi0519194
    • Boggs JM, Rangaraj G, Gao W, Heng YM (2006) Effect of phosphorylation of myelin basic protein by MAPK on its interactions with actin and actin binding to a lipid membrane in vitro. Biochemistry 45:391-401 (Pubitemid 43100406)
    • (2006) Biochemistry , vol.45 , Issue.2 , pp. 391-401
    • Boggs, J.M.1    Rangaraj, G.2    Gao, W.3    Heng, Y.-M.4
  • 84
    • 0024567052 scopus 로고
    • The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein
    • Wood DD, Moscarello MA (1989) The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein. J Biol Chem 264:5121-5127 (Pubitemid 19092925)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.9 , pp. 5121-5127
    • Wood, D.D.1    Moscarello, M.A.2
  • 86
    • 77957922714 scopus 로고    scopus 로고
    • Secondary structure and solvent accessibility of a calmodulin-binding C-terminal segment of membrane-associated myelin basic protein
    • Homchaudhuri L, De AM, Nilsson SB, Bessonov K, Smith GS, Bamm VV, Musse AA, Harauz G, Boggs JM (2010) Secondary structure and solvent accessibility of a calmodulin-binding C-terminal segment of membrane-associated myelin basic protein. Biochemistry 49:8955-8966
    • (2010) Biochemistry , vol.49 , pp. 8955-8966
    • Homchaudhuri, L.1    De Am Nilsson, S.B.2    Bessonov, K.3    Smith, G.S.4    Bamm, V.V.5    Musse, A.A.6    Harauz, G.7    Boggs, J.M.8
  • 87
    • 0029879141 scopus 로고    scopus 로고
    • Immunolocalization of 17 and 21.5 kDa MBP isoforms in compact myelin and radial component
    • Karthigasan J, Garvey JS, Ramamurthy GV, Kirschner DA (1996) Immunolocalization of 17 and 21.5 kDa MBP isoforms in compact myelin and radial component. J Neurocytol 25:1-7
    • (1996) J Neurocytol , vol.25 , pp. 1-7
    • Karthigasan, J.1    Garvey, J.S.2    Ramamurthy, G.V.3    Kirschner, D.A.4
  • 88
    • 77951929406 scopus 로고    scopus 로고
    • On the biogenesis of myelin membranes: Sorting, trafficking and cell polarity
    • Baron W, Hoekstra D (2010) On the biogenesis of myelin membranes: sorting, trafficking and cell polarity. FEBS Lett 584:1760-1770
    • (2010) FEBS Lett , vol.584 , pp. 1760-1770
    • Baron, W.1    Hoekstra, D.2
  • 89
    • 45949105768 scopus 로고    scopus 로고
    • Polarity development in oligodendrocytes: Sorting and trafficking of myelin components
    • Maier O, Hoekstra D, Baron W (2008) Polarity development in oligodendrocytes: sorting and trafficking of myelin components. J Mol Neurosci 35:35-53
    • (2008) J Mol Neurosci , vol.35 , pp. 35-53
    • Maier, O.1    Hoekstra, D.2    Baron, W.3
  • 91
    • 0036773738 scopus 로고    scopus 로고
    • Claudin-based barrier in simple and stratified cellular sheets
    • DOI 10.1016/S0955-0674(02)00362-9
    • Tsukita S, Furuse M (2002) Claudin-based barrier in simple and stratified cellular sheets. Curr Opin Cell Biol 14:531-536 (Pubitemid 35251880)
    • (2002) Current Opinion in Cell Biology , vol.14 , Issue.5 , pp. 531-536
    • Tsukita, S.1    Furuse, M.2
  • 92
    • 77954422347 scopus 로고    scopus 로고
    • Oligodendrocytes in mouse corpus callosum are coupled via gap junction channels formed by connexin47 and connexin32
    • Maglione M, Tress O, Haas B, Karram K, Trotter J, Willecke K, Kettenmann H (2010) Oligodendrocytes in mouse corpus callosum are coupled via gap junction channels formed by connexin47 and connexin32. Glia 58:1104-1117
    • (2010) Glia , vol.58 , pp. 1104-1117
    • Maglione, M.1    Tress, O.2    Haas, B.3    Karram, K.4    Trotter, J.5    Willecke, K.6    Kettenmann, H.7
  • 93
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • DOI 10.1074/jbc.273.45.29745
    • Fanning AS, Jameson BJ, Jesaitis LA, Anderson JM (1998) The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton. J Biol Chem 273:29745-29753 (Pubitemid 28509986)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.45 , pp. 29745-29753
    • Fanning, A.S.1    Jameson, B.J.2    Jesaitis, L.A.3    Anderson, J.M.4


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