메뉴 건너뛰기




Volumn 584, Issue 9, 2010, Pages 1760-1770

On the biogenesis of myelin membranes: Sorting, trafficking and cell polarity

Author keywords

Microdomain; Myelin; Myelin basic protein; Proteolipid protein; Sorting; Trafficking

Indexed keywords

CHOLESTEROL; GLYCOSPHINGOLIPID; MEMBRANE PROTEIN; MESSENGER RNA; MYELIN PROTEIN; PROTEIN KINASE C; PROTEOLIPID PROTEIN; SULFATIDE;

EID: 77951929406     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2009.10.085     Document Type: Review
Times cited : (120)

References (96)
  • 1
    • 33749033095 scopus 로고    scopus 로고
    • Rafts in oligodendrocytes: evidence and structure-function relationship
    • Gielen E., Baron W., Vandeven M., Steels P., Doekstra D., Ameloot M. Rafts in oligodendrocytes: evidence and structure-function relationship. Glia 2006, 54:499-512.
    • (2006) Glia , vol.54 , pp. 499-512
    • Gielen, E.1    Baron, W.2    Vandeven, M.3    Steels, P.4    Doekstra, D.5    Ameloot, M.6
  • 3
    • 71249151075 scopus 로고    scopus 로고
    • Role of oligodendroglial cytoskeleton in differentiation and myelination
    • Bauer N.G., Richter-Landsberg C., ffrench-Constant C. Role of oligodendroglial cytoskeleton in differentiation and myelination. Glia 2009, 57:1691-1705.
    • (2009) Glia , vol.57 , pp. 1691-1705
    • Bauer, N.G.1    Richter-Landsberg, C.2    ffrench-Constant, C.3
  • 4
    • 45949105768 scopus 로고    scopus 로고
    • Polarity development in oligodendrocytes: sorting and trafficking of myelin components
    • Maier O., Hoekstra D., Baron W. Polarity development in oligodendrocytes: sorting and trafficking of myelin components. J. Mol. Neurosci. 2008, 35:35-53.
    • (2008) J. Mol. Neurosci. , vol.35 , pp. 35-53
    • Maier, O.1    Hoekstra, D.2    Baron, W.3
  • 5
    • 0034534453 scopus 로고    scopus 로고
    • On the biogenesis of the myelin sheath: cognate polarized trafficking pathways in oligodendrocytes
    • De Vries H., Hoekstra D. On the biogenesis of the myelin sheath: cognate polarized trafficking pathways in oligodendrocytes. Glycoconj. J. 2000, 17:181-190.
    • (2000) Glycoconj. J. , vol.17 , pp. 181-190
    • De Vries, H.1    Hoekstra, D.2
  • 6
    • 0035869494 scopus 로고    scopus 로고
    • Membrane traffic in myelinating oligodendrocytes
    • Krämer E.M., Schardt A., Nave K. Membrane traffic in myelinating oligodendrocytes. Microscop. Res. Tech. 2001, 52:656-671.
    • (2001) Microscop. Res. Tech. , vol.52 , pp. 656-671
    • Krämer, E.M.1    Schardt, A.2    Nave, K.3
  • 7
    • 0031918326 scopus 로고    scopus 로고
    • An apical-type of trafficking pathway is present in cultured oligodendrocytes but the sphingolipid-enriched myelin membrane is the target of a basolateral pathway
    • De Vries H., Schrage C., Hoekstra D. An apical-type of trafficking pathway is present in cultured oligodendrocytes but the sphingolipid-enriched myelin membrane is the target of a basolateral pathway. Mol. Biol. Cell 1998, 9:599-609.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 599-609
    • De Vries, H.1    Schrage, C.2    Hoekstra, D.3
  • 8
    • 28644444772 scopus 로고    scopus 로고
    • The role of syntaxins in the specificity of vesicle targeting in polarized epithelial cells
    • ter Beest M.B., Chapin S.J., Avrahami D., Mostov K.E. The role of syntaxins in the specificity of vesicle targeting in polarized epithelial cells. Mol. Biol. Cell. 2005, 16:5784-5792.
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 5784-5792
    • ter Beest, M.B.1    Chapin, S.J.2    Avrahami, D.3    Mostov, K.E.4
  • 11
    • 3042542722 scopus 로고    scopus 로고
    • The subapical compartment: a traffic center in membrane polarity development
    • Hoekstra D., Tyteca D., van IJzendoorn S.C. The subapical compartment: a traffic center in membrane polarity development. J. Cell Sci. 2004, 117:183-192.
    • (2004) J. Cell Sci. , vol.117 , pp. 183-192
    • Hoekstra, D.1    Tyteca, D.2    van IJzendoorn, S.C.3
  • 12
    • 33748487414 scopus 로고    scopus 로고
    • Myelin basic protein: a multifunctional protein
    • Boggs J.M. Myelin basic protein: a multifunctional protein. Cell. Mol. Life Sci. 2006, 63:145-1961.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 145-1961
    • Boggs, J.M.1
  • 13
    • 33947371742 scopus 로고    scopus 로고
    • Partitioning of myelin basic protein into membrane microdomains in a spontaneously demyelinating mouse model for multiple sclerosis
    • DeBruin L.S., Haines J.D., Bienzie D., Harauz G. Partitioning of myelin basic protein into membrane microdomains in a spontaneously demyelinating mouse model for multiple sclerosis. Biochem. Cell Biol. 2006, 84:993-1005.
    • (2006) Biochem. Cell Biol. , vol.84 , pp. 993-1005
    • DeBruin, L.S.1    Haines, J.D.2    Bienzie, D.3    Harauz, G.4
  • 17
    • 18344371641 scopus 로고    scopus 로고
    • Moving messages: the intracellular localization of mRNAs
    • St.Johnston D. Moving messages: the intracellular localization of mRNAs. Nat. Rev. Mol. Cell. Biol. 2005, 6:363-375.
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 363-375
    • St.Johnston, D.1
  • 21
    • 0033607521 scopus 로고    scopus 로고
    • Mutational analysis of a heterogenous nuclear ribonucleoprotein A2 response element for RNA trafficking
    • Munro T.P., Magee R.J., Kidd G.J., Carson J.H., Barbarese E., Smith L.M., Smith R. Mutational analysis of a heterogenous nuclear ribonucleoprotein A2 response element for RNA trafficking. J. Biol. Chem. 1999, 274:34389-34395.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34389-34395
    • Munro, T.P.1    Magee, R.J.2    Kidd, G.J.3    Carson, J.H.4    Barbarese, E.5    Smith, L.M.6    Smith, R.7
  • 23
    • 33746581893 scopus 로고    scopus 로고
    • Heterogenous nuclear ribonucleoprotein (hnRNP) E1 binds to hnRNP A2 and inhibits translation of A2 response element mRNAs
    • Kosturko L.D., Maggipinto M.J., Korza G., Lee J.W., Carson J.H., Barbarese E. Heterogenous nuclear ribonucleoprotein (hnRNP) E1 binds to hnRNP A2 and inhibits translation of A2 response element mRNAs. Mol. Biol. Cell 2006, 17:3521-3533.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3521-3533
    • Kosturko, L.D.1    Maggipinto, M.J.2    Korza, G.3    Lee, J.W.4    Carson, J.H.5    Barbarese, E.6
  • 25
    • 0031050896 scopus 로고    scopus 로고
    • Differential and cell-development dependent localization of myelin messenger RNAs in oligodendrocytes
    • De Vries H., De Jonge J.C., Schrage C., Van der Haar M.E., Hoekstra D. Differential and cell-development dependent localization of myelin messenger RNAs in oligodendrocytes. J. Neurosci. Res. 1997, 47:479-488.
    • (1997) J. Neurosci. Res. , vol.47 , pp. 479-488
    • De Vries, H.1    De Jonge, J.C.2    Schrage, C.3    Van der Haar, M.E.4    Hoekstra, D.5
  • 26
    • 0032717797 scopus 로고    scopus 로고
    • Myelin-associated oligodendrocytic basic protein mRNAs reside at different subcellular locations
    • Gould R.M., Freund C.M., Barbarese E. Myelin-associated oligodendrocytic basic protein mRNAs reside at different subcellular locations. J. Neurochem. 1999, 73:574-583.
    • (1999) J. Neurochem. , vol.73 , pp. 574-583
    • Gould, R.M.1    Freund, C.M.2    Barbarese, E.3
  • 27
    • 66149089362 scopus 로고    scopus 로고
    • Lovastatin induces the formation of abnormal myelin-like membrane sheets in primary oligodendrocytes
    • Maier O., De Jonge J., Nomden A., Hoekstra D., Baron W. Lovastatin induces the formation of abnormal myelin-like membrane sheets in primary oligodendrocytes. Glia 2009, 57:402-413.
    • (2009) Glia , vol.57 , pp. 402-413
    • Maier, O.1    De Jonge, J.2    Nomden, A.3    Hoekstra, D.4    Baron, W.5
  • 28
    • 0030770987 scopus 로고    scopus 로고
    • Translocation of myelin basic protein mRNA in oligodendrocytes requires microtubules and kinesin
    • Carson J.H., Worboys K., Ainger K., Barbarese E. Translocation of myelin basic protein mRNA in oligodendrocytes requires microtubules and kinesin. Cell Mot. Cytoskel. 1997, 38:318-328.
    • (1997) Cell Mot. Cytoskel. , vol.38 , pp. 318-328
    • Carson, J.H.1    Worboys, K.2    Ainger, K.3    Barbarese, E.4
  • 29
    • 67649874745 scopus 로고    scopus 로고
    • Kif1b is essential for mRNA localization in oligodendrocytes and development of myelinated axons
    • Lyons D.A., Naylor S.G., Scholze A., Talbot W.S. Kif1b is essential for mRNA localization in oligodendrocytes and development of myelinated axons. Nat. Genet. 2009, 41:854-858.
    • (2009) Nat. Genet. , vol.41 , pp. 854-858
    • Lyons, D.A.1    Naylor, S.G.2    Scholze, A.3    Talbot, W.S.4
  • 30
    • 34447630642 scopus 로고    scopus 로고
    • The microtubule-associated protein tumor overexpressed gene/cytoskeleton-associated protein 5 is necessary for myelin basic protein expression in oligodendrocytes
    • Francone V.P., Maggipinto M.J., Kosturko L.D., Barbarese E. The microtubule-associated protein tumor overexpressed gene/cytoskeleton-associated protein 5 is necessary for myelin basic protein expression in oligodendrocytes. J. Neurosci. 2007, 27:7654-7662.
    • (2007) J. Neurosci. , vol.27 , pp. 7654-7662
    • Francone, V.P.1    Maggipinto, M.J.2    Kosturko, L.D.3    Barbarese, E.4
  • 31
    • 44149117017 scopus 로고    scopus 로고
    • Activation of oligodendroglial Fyn kinase enhances translation of mRNAs transported in hnRNP A2-dependent RNA granules
    • White R., Gonsior C., Krämer-Albers E.M., Stöhr N., Hüttelmaier S., Trotter J. Activation of oligodendroglial Fyn kinase enhances translation of mRNAs transported in hnRNP A2-dependent RNA granules. J. Cell Biol. 2008, 181:579-586.
    • (2008) J. Cell Biol. , vol.181 , pp. 579-586
    • White, R.1    Gonsior, C.2    Krämer-Albers, E.M.3    Stöhr, N.4    Hüttelmaier, S.5    Trotter, J.6
  • 32
    • 33846662786 scopus 로고    scopus 로고
    • Bicoid RNA localization requires specific binding of an endosomal sorting complex
    • Irion U., St.Johnston D. Bicoid RNA localization requires specific binding of an endosomal sorting complex. Nature 2007, 445:554-558.
    • (2007) Nature , vol.445 , pp. 554-558
    • Irion, U.1    St.Johnston, D.2
  • 33
  • 35
    • 4344670341 scopus 로고    scopus 로고
    • Involvement of the late secretory pathway in actin regulation and mRNA transport in yeast
    • Aranov S., Gerst J.E. Involvement of the late secretory pathway in actin regulation and mRNA transport in yeast. J. Biol. Chem. 2004, 279:36962-36971.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36962-36971
    • Aranov, S.1    Gerst, J.E.2
  • 36
    • 13544276472 scopus 로고    scopus 로고
    • The role of membranes and membrane trafficking in RNA localization
    • Cohen R.S. The role of membranes and membrane trafficking in RNA localization. Biol. Cell 2005, 97:5-18.
    • (2005) Biol. Cell , vol.97 , pp. 5-18
    • Cohen, R.S.1
  • 39
    • 0028316886 scopus 로고
    • Proteolipid protein interactions in transfectants: implications for myelin assembly
    • Sinoway M.P., Kitagawa K., Timsit S., Hashim G.A., Colman D.R. Proteolipid protein interactions in transfectants: implications for myelin assembly. J. Neurosci. Res. 1994, 37:551-562.
    • (1994) J. Neurosci. Res. , vol.37 , pp. 551-562
    • Sinoway, M.P.1    Kitagawa, K.2    Timsit, S.3    Hashim, G.A.4    Colman, D.R.5
  • 41
    • 0034597142 scopus 로고    scopus 로고
    • Assembly of myelin by association of proteolipid protein with cholesterol- and galactosylceramide-rich membrane domains
    • Simons M., Krämer E.M., Thiele C., Stoffel W., Trotter J. Assembly of myelin by association of proteolipid protein with cholesterol- and galactosylceramide-rich membrane domains. J. Cell Biol. 2000, 151:143-154.
    • (2000) J. Cell Biol. , vol.151 , pp. 143-154
    • Simons, M.1    Krämer, E.M.2    Thiele, C.3    Stoffel, W.4    Trotter, J.5
  • 42
    • 0028295710 scopus 로고
    • Inhibition of protein and lipid sulfation in oligodendrocytes blocks biological responses to FGF-2 and retards cytoarchitectural maturation, but not developmental lineage progression
    • Bansal R., Pfeiffer S.E. Inhibition of protein and lipid sulfation in oligodendrocytes blocks biological responses to FGF-2 and retards cytoarchitectural maturation, but not developmental lineage progression. Dev. Biol. 1994, 162:511-524.
    • (1994) Dev. Biol. , vol.162 , pp. 511-524
    • Bansal, R.1    Pfeiffer, S.E.2
  • 43
    • 0030602822 scopus 로고    scopus 로고
    • Myelination in the absence of galactocerebroside and sulfatide normal structure with abnormal function and regional instability
    • Coetzee T., Fujita N., Dupree J., Shi R., Blight A., Suzuki K., Suzuki K., Popko B. Myelination in the absence of galactocerebroside and sulfatide normal structure with abnormal function and regional instability. Cell 1996, 86:209-219.
    • (1996) Cell , vol.86 , pp. 209-219
    • Coetzee, T.1    Fujita, N.2    Dupree, J.3    Shi, R.4    Blight, A.5    Suzuki, K.6    Suzuki, K.7    Popko, B.8
  • 46
    • 0035892685 scopus 로고    scopus 로고
    • Mutually exclusive apicobasolateral sorting of two oligodendroglial membrane proteins, proteolipid protein and myelin/oligodendrocyte glycoprotein, in Madin-Darby canine kidney cells
    • Kroepfl J.F., Gardinier M.V. Mutually exclusive apicobasolateral sorting of two oligodendroglial membrane proteins, proteolipid protein and myelin/oligodendrocyte glycoprotein, in Madin-Darby canine kidney cells. J. Neurosci. Res. 2001, 66:1140-1148.
    • (2001) J. Neurosci. Res. , vol.66 , pp. 1140-1148
    • Kroepfl, J.F.1    Gardinier, M.V.2
  • 47
    • 0031852648 scopus 로고    scopus 로고
    • (Glyco)sphingolipids are sorted in sub-apical compartments in HepG2 cells. A role for non-Golgi-related intracellular sites in the polarized distribution of (glyco)sphingolipids
    • Van IJzendoorn S.C.D., Hoekstra D. (Glyco)sphingolipids are sorted in sub-apical compartments in HepG2 cells. A role for non-Golgi-related intracellular sites in the polarized distribution of (glyco)sphingolipids. J. Cell Biol. 1998, 142:683-696.
    • (1998) J. Cell Biol. , vol.142 , pp. 683-696
    • Van IJzendoorn, S.C.D.1    Hoekstra, D.2
  • 48
    • 66049138461 scopus 로고    scopus 로고
    • Comprehensive analysis of expression, subcellular localization, and cognate pairing of SNARE proteins in oligodendrocytes
    • Feldmann A., Winterstein C., White R., Trotter J., Krämer-Albers E.M. Comprehensive analysis of expression, subcellular localization, and cognate pairing of SNARE proteins in oligodendrocytes. J. Neurosci. Res. 2009, 87:1760-1772.
    • (2009) J. Neurosci. Res. , vol.87 , pp. 1760-1772
    • Feldmann, A.1    Winterstein, C.2    White, R.3    Trotter, J.4    Krämer-Albers, E.M.5
  • 49
    • 70449449887 scopus 로고    scopus 로고
    • The SNARE protein SNAP-29 interacts with the GTPase Rab3A: Implications for membrane trafficking in myelinating glia
    • Schardt A., Brinkmann B.G., Mitkovski M., Sereda M.W., Werner H.B., Nave K.A. The SNARE protein SNAP-29 interacts with the GTPase Rab3A: Implications for membrane trafficking in myelinating glia. J. Neurosci. Res. 2009, 87:3465-3479.
    • (2009) J. Neurosci. Res. , vol.87 , pp. 3465-3479
    • Schardt, A.1    Brinkmann, B.G.2    Mitkovski, M.3    Sereda, M.W.4    Werner, H.B.5    Nave, K.A.6
  • 50
    • 0037092050 scopus 로고    scopus 로고
    • Overexpression of the myelin proteolipid protein leads to accumulation of cholesterol and proteolipid protein in endosomes/lysosomes: implications for Pelizaeus-Merzbacher disease
    • Simons M., Krämer E.M., Macchi P., Rathke-Hartlieb S., Trotter J., Nave K.A., Schulz J.B. Overexpression of the myelin proteolipid protein leads to accumulation of cholesterol and proteolipid protein in endosomes/lysosomes: implications for Pelizaeus-Merzbacher disease. J. Cell Biol. 2002, 157:327-336.
    • (2002) J. Cell Biol. , vol.157 , pp. 327-336
    • Simons, M.1    Krämer, E.M.2    Macchi, P.3    Rathke-Hartlieb, S.4    Trotter, J.5    Nave, K.A.6    Schulz, J.B.7
  • 51
    • 33751108519 scopus 로고    scopus 로고
    • Perturbed interactions of mutant proteolipid protein/DM20 with cholesterol and lipid rafts in oligodendroglia: implications for dysmyelination in spastic paraplegia
    • Krämer-Albers E.M., Gehrig-Burger K., Thiele C., Trotter J., Nave K.A. Perturbed interactions of mutant proteolipid protein/DM20 with cholesterol and lipid rafts in oligodendroglia: implications for dysmyelination in spastic paraplegia. J. Neurosci. 2006, 26:11743-11752.
    • (2006) J. Neurosci. , vol.26 , pp. 11743-11752
    • Krämer-Albers, E.M.1    Gehrig-Burger, K.2    Thiele, C.3    Trotter, J.4    Nave, K.A.5
  • 52
    • 20044370505 scopus 로고    scopus 로고
    • High cholesterol level is essential for myelin membrane growth
    • Saher G., Brügger B., Lappe-Siefke C., et al. High cholesterol level is essential for myelin membrane growth. Nat. Neurosci. 2005, 8:468-475.
    • (2005) Nat. Neurosci. , vol.8 , pp. 468-475
    • Saher, G.1    Brügger, B.2    Lappe-Siefke, C.3
  • 53
    • 35348934237 scopus 로고    scopus 로고
    • Transcriptional control of cholesterol biosynthesis in Schwann cells by axonal neuregulin 1
    • Pertusa M., Morenilla-Papao C., Carteron C., Viana F., Cabedo H. Transcriptional control of cholesterol biosynthesis in Schwann cells by axonal neuregulin 1. J. Biol. Chem. 2007, 282:28768-28778.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28768-28778
    • Pertusa, M.1    Morenilla-Papao, C.2    Carteron, C.3    Viana, F.4    Cabedo, H.5
  • 54
    • 55749104704 scopus 로고    scopus 로고
    • A defect of sphingolipid metabolism modifies the properties of normal appearing white matter in multiple sclerosis
    • Wheeler D., Bandaru V.V.R., Calabresi P.A., Nath A., Heughey N.J. A defect of sphingolipid metabolism modifies the properties of normal appearing white matter in multiple sclerosis. Brain 2008, 131:3092-3102.
    • (2008) Brain , vol.131 , pp. 3092-3102
    • Wheeler, D.1    Bandaru, V.V.R.2    Calabresi, P.A.3    Nath, A.4    Heughey, N.J.5
  • 55
    • 33846926110 scopus 로고    scopus 로고
    • White matter rafting - membrane microdomains in myelin
    • DeBruin L.S., Harauz G. White matter rafting - membrane microdomains in myelin. Neurochem. Res. 2007, 32:213-228.
    • (2007) Neurochem. Res. , vol.32 , pp. 213-228
    • DeBruin, L.S.1    Harauz, G.2
  • 59
    • 6944244056 scopus 로고    scopus 로고
    • Sigma-1 receptors at galactosylceramide-enriched lipid microdomains regulate oligodendrocyte differentiation
    • Hayashi T., Su T.P. Sigma-1 receptors at galactosylceramide-enriched lipid microdomains regulate oligodendrocyte differentiation. Proc. Natl. Acad. Sci. USA 2004, 101:14949-14954.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14949-14954
    • Hayashi, T.1    Su, T.P.2
  • 60
    • 33644502874 scopus 로고    scopus 로고
    • Sulfatide is essential for the maintenance of CNS myelin and axon structure
    • Marcus J., Honigbaum S., Shroff S., Honke K., Rosenbluth J., Dupree J.L. Sulfatide is essential for the maintenance of CNS myelin and axon structure. Glia 2006, 53:372-381.
    • (2006) Glia , vol.53 , pp. 372-381
    • Marcus, J.1    Honigbaum, S.2    Shroff, S.3    Honke, K.4    Rosenbluth, J.5    Dupree, J.L.6
  • 61
    • 13444274593 scopus 로고    scopus 로고
    • Alteration of the extracellular matrix interferes with raft-association of neurofascin in oligodendrocytes. Potential significance for multiple sclerosis?
    • Maier O., van der Heide T., van Dam A.M., Baron W., de Vries H., Hoekstra D. Alteration of the extracellular matrix interferes with raft-association of neurofascin in oligodendrocytes. Potential significance for multiple sclerosis?. Mol. Cell Neurosci. 2005, 28:390-401.
    • (2005) Mol. Cell Neurosci. , vol.28 , pp. 390-401
    • Maier, O.1    van der Heide, T.2    van Dam, A.M.3    Baron, W.4    de Vries, H.5    Hoekstra, D.6
  • 62
    • 0032820934 scopus 로고    scopus 로고
    • Internalization and sorting of plasma membrane sphingolipid analogues in differentiating oligodendrocytes
    • Watanabe R., Asakura K., Rodriguez M., Pagano R.E. Internalization and sorting of plasma membrane sphingolipid analogues in differentiating oligodendrocytes. J. Neurochem. 1999, 73:1375-1383.
    • (1999) J. Neurochem. , vol.73 , pp. 1375-1383
    • Watanabe, R.1    Asakura, K.2    Rodriguez, M.3    Pagano, R.E.4
  • 63
    • 42549119962 scopus 로고    scopus 로고
    • Distinct endocytic recycling of myelin proteins promotes oligodendroglial membrane remodeling
    • Winterstein C., Trotter J., Krämer-Albers E.-M. Distinct endocytic recycling of myelin proteins promotes oligodendroglial membrane remodeling. J. Cell Sci. 2008, 121:834-842.
    • (2008) J. Cell Sci. , vol.121 , pp. 834-842
    • Winterstein, C.1    Trotter, J.2    Krämer-Albers, E.-M.3
  • 64
    • 0031927361 scopus 로고    scopus 로고
    • Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: an electrostatic model and experimental results
    • Denisov G., Wanaski S., Luan P., Glaser M., McLaughlin S. Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-bisphosphate: an electrostatic model and experimental results. Biophys. J. 1998, 74:731-744.
    • (1998) Biophys. J. , vol.74 , pp. 731-744
    • Denisov, G.1    Wanaski, S.2    Luan, P.3    Glaser, M.4    McLaughlin, S.5
  • 65
    • 7044241296 scopus 로고    scopus 로고
    • Do proteins facilitate the formation of cholesterol-rich domains?
    • Epand R.M. Do proteins facilitate the formation of cholesterol-rich domains?. Biochim. Biophys. Acta 2004, 1666:227-238.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 227-238
    • Epand, R.M.1
  • 66
    • 38749087608 scopus 로고    scopus 로고
    • Lateral reorganization of myelin lipid domains by myelin basic protein studied at the air-water interface
    • Hu Y., Israelachvili J. Lateral reorganization of myelin lipid domains by myelin basic protein studied at the air-water interface. Colloid. Surf. B: Biointerfaces 2008, 62:22-30.
    • (2008) Colloid. Surf. B: Biointerfaces , vol.62 , pp. 22-30
    • Hu, Y.1    Israelachvili, J.2
  • 69
    • 32344450851 scopus 로고    scopus 로고
    • His36Pro point-mutated proteolipid protein retained in the endoplasmic reticulum of oligodendrocytes in the shaking Pup
    • Song J., Goetz B.D., Duncan I.D. His36Pro point-mutated proteolipid protein retained in the endoplasmic reticulum of oligodendrocytes in the shaking Pup. Glia 2006, 53:257-265.
    • (2006) Glia , vol.53 , pp. 257-265
    • Song, J.1    Goetz, B.D.2    Duncan, I.D.3
  • 70
    • 0028226949 scopus 로고
    • Many naturally occurring mutations of myelin proteolipid protein impair its intracellular transport
    • Gow A., Friedrich V.L., Lazzarini R.A. Many naturally occurring mutations of myelin proteolipid protein impair its intracellular transport. J. Neurosci. Res. 1994, 37:574-583.
    • (1994) J. Neurosci. Res. , vol.37 , pp. 574-583
    • Gow, A.1    Friedrich, V.L.2    Lazzarini, R.A.3
  • 71
    • 33846379145 scopus 로고    scopus 로고
    • Visualizing the localization of sulfoglycosphingolipids in lipid raft domains in model membranes and sperm membrane extracts
    • Weerachatyanukul W., Probodh I., Kongmanas K., Tanphaichitr N., Johnston L.J. Visualizing the localization of sulfoglycosphingolipids in lipid raft domains in model membranes and sperm membrane extracts. Biochim. Biophys. Acta 2007, 1768:299-310.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 299-310
    • Weerachatyanukul, W.1    Probodh, I.2    Kongmanas, K.3    Tanphaichitr, N.4    Johnston, L.J.5
  • 72
    • 33846827116 scopus 로고    scopus 로고
    • Sulfatide with different fatty acids has unique distributions in cerebellum as imaged by time of flight secondary ion mass spectrometry (TOF-SIMS)
    • Pernber Z., Richter K., Mansson J.E., Nygren H. Sulfatide with different fatty acids has unique distributions in cerebellum as imaged by time of flight secondary ion mass spectrometry (TOF-SIMS). Biochim. Biophys. Acta 2007, 177:202-209.
    • (2007) Biochim. Biophys. Acta , vol.177 , pp. 202-209
    • Pernber, Z.1    Richter, K.2    Mansson, J.E.3    Nygren, H.4
  • 73
    • 40849086666 scopus 로고    scopus 로고
    • Myelin glycosphingolipids, galactosylceramide and sulfatide, participate in carbohydrate-carbohydrate interactions between apposed membranes and may form glycosynapses between oligodendrocyte and/or myelin membranes
    • Boggs J.M., Gao W., Hirahara Y. Myelin glycosphingolipids, galactosylceramide and sulfatide, participate in carbohydrate-carbohydrate interactions between apposed membranes and may form glycosynapses between oligodendrocyte and/or myelin membranes. Biochim. Biophys. Acta 2008, 1780:445-455.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 445-455
    • Boggs, J.M.1    Gao, W.2    Hirahara, Y.3
  • 74
    • 55049091909 scopus 로고    scopus 로고
    • Distinct stages of myelination regulated by gamma-secretase and astrocytes in a rapidly myelinating CNS coculture system
    • Watkins T.A., Emery B., Mulinyawe S., Barres B.A. Distinct stages of myelination regulated by gamma-secretase and astrocytes in a rapidly myelinating CNS coculture system. Neuron 2008, 60:555-569.
    • (2008) Neuron , vol.60 , pp. 555-569
    • Watkins, T.A.1    Emery, B.2    Mulinyawe, S.3    Barres, B.A.4
  • 75
    • 70449338186 scopus 로고    scopus 로고
    • Disposition of axonal caspr with respect to glial cell membranes: implications for the process of myelination
    • Pedraza L., Huang J.K., Colman D. Disposition of axonal caspr with respect to glial cell membranes: implications for the process of myelination. J. Neurosci. Res. 2009, 87:3480-3491.
    • (2009) J. Neurosci. Res. , vol.87 , pp. 3480-3491
    • Pedraza, L.1    Huang, J.K.2    Colman, D.3
  • 80
    • 33748797722 scopus 로고    scopus 로고
    • Fibronectin impedes " myelin" sheet-directed flow in oligodendrocytes: a role for beta 1 integrin-mediated PKC signaling pathway in vesicular trafficking
    • Šišková Z., Baron W., de Vries H., Hoekstra D. Fibronectin impedes " myelin" sheet-directed flow in oligodendrocytes: a role for beta 1 integrin-mediated PKC signaling pathway in vesicular trafficking. Mol. Cell. Neurosci. 2006, 33:150-159.
    • (2006) Mol. Cell. Neurosci. , vol.33 , pp. 150-159
    • Šišková, Z.1    Baron, W.2    de Vries, H.3    Hoekstra, D.4
  • 81
    • 14844341307 scopus 로고    scopus 로고
    • Integrin-growth factor interactions as regulators of oligodendroglial development and function
    • Baron W., Colognato H., ffrench-Constant C. Integrin-growth factor interactions as regulators of oligodendroglial development and function. Glia 2005, 49:367-479.
    • (2005) Glia , vol.49 , pp. 367-479
    • Baron, W.1    Colognato, H.2    ffrench-Constant, C.3
  • 84
    • 69049118154 scopus 로고    scopus 로고
    • {beta}1 integrins are required for normal CNS myelination and promote AKT-dependent myelin outgrowth
    • Barros C.S., Nguyen T., Spence r K.S., Nishiyama A., Colognato H., Müller U. {beta}1 integrins are required for normal CNS myelination and promote AKT-dependent myelin outgrowth. Development 2009, 136:2717-2724.
    • (2009) Development , vol.136 , pp. 2717-2724
    • Barros, C.S.1    Nguyen, T.2    Spence, R.K.S.3    Nishiyama, A.4    Colognato, H.5    Müller, U.6
  • 87
    • 34047126867 scopus 로고    scopus 로고
    • Rho regulates membrane transport in the endocytic pathway to control plasma membrane specialization in oligodendroglial cells
    • Kippert A., Trajkovic K., Rajendran L., Ries J., Simons M. Rho regulates membrane transport in the endocytic pathway to control plasma membrane specialization in oligodendroglial cells. J. Neurosci. 2007, 27:3560-3570.
    • (2007) J. Neurosci. , vol.27 , pp. 3560-3570
    • Kippert, A.1    Trajkovic, K.2    Rajendran, L.3    Ries, J.4    Simons, M.5
  • 89
    • 71249088803 scopus 로고    scopus 로고
    • Tenascin C and tenascin R similarly prevent the formation of myelin membranes in a RhoA-dependent manner, but antagonistically regulate the expression of myelin basic protein via a separate pathway
    • Czopka T., Von Holst A., Schmidt G., Ffrench-Constant C., Faissner N. Tenascin C and tenascin R similarly prevent the formation of myelin membranes in a RhoA-dependent manner, but antagonistically regulate the expression of myelin basic protein via a separate pathway. Glia 2009, 57:1790-1801.
    • (2009) Glia , vol.57 , pp. 1790-1801
    • Czopka, T.1    Von Holst, A.2    Schmidt, G.3    Ffrench-Constant, C.4    Faissner, N.5
  • 91
    • 67651177571 scopus 로고    scopus 로고
    • An integrin-contactin complex regulates CNS myelination by differential Fyn phosphorylation
    • Laursen L.S., Chan C.W., ffrench-Constant C. An integrin-contactin complex regulates CNS myelination by differential Fyn phosphorylation. J. Neurosci. 2009, 29:9174-9185.
    • (2009) J. Neurosci. , vol.29 , pp. 9174-9185
    • Laursen, L.S.1    Chan, C.W.2    ffrench-Constant, C.3
  • 92
    • 0033570948 scopus 로고    scopus 로고
    • Protein kinase C prevents oligodendrocyte differentiation: modulation of actin cytoskeleton and cognate polarized membrane traffic
    • Baron W., de Vries E.J., de Vries H., Hoekstra D. Protein kinase C prevents oligodendrocyte differentiation: modulation of actin cytoskeleton and cognate polarized membrane traffic. J. Neurobiol. 1999, 41:385-398.
    • (1999) J. Neurobiol. , vol.41 , pp. 385-398
    • Baron, W.1    de Vries, E.J.2    de Vries, H.3    Hoekstra, D.4
  • 93
    • 0034029228 scopus 로고    scopus 로고
    • PDGF and FGF-2 signaling in oligodendrocyte progenitor cells: regulation of proliferation activity and differentiation by multiple intracellular signaling pathways
    • Baron W., Metz B., De Vries H., Hoekstra D. PDGF and FGF-2 signaling in oligodendrocyte progenitor cells: regulation of proliferation activity and differentiation by multiple intracellular signaling pathways. Mol. Cell. Neurosci. 2000, 15:314-329.
    • (2000) Mol. Cell. Neurosci. , vol.15 , pp. 314-329
    • Baron, W.1    Metz, B.2    De Vries, H.3    Hoekstra, D.4
  • 94
    • 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 J. 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 2009, 48:2385-2393.
    • (2009) Biochemistry , vol.48 , pp. 2385-2393
    • Homchaudhuri, L.1    Polverini, E.2    Gao, W.3    Harauz, G.4    Boggs, J.5
  • 95
    • 0032559544 scopus 로고    scopus 로고
    • Disrupted proteolipid protein trafficking results in oligodendrocyte apoptosis in an animal model of Pelizaeus-Merzbacher disease
    • Gow A., Southwood C.M., Lazzarini R.A. Disrupted proteolipid protein trafficking results in oligodendrocyte apoptosis in an animal model of Pelizaeus-Merzbacher disease. J. Cell Biol. 1998, 140:925-934.
    • (1998) J. Cell Biol. , vol.140 , pp. 925-934
    • Gow, A.1    Southwood, C.M.2    Lazzarini, R.A.3
  • 96
    • 0033964123 scopus 로고    scopus 로고
    • Mal, a proteolipid in glycosphingolipid enriched domains: functional implications in myelin and beyond
    • Frank M. Mal, a proteolipid in glycosphingolipid enriched domains: functional implications in myelin and beyond. Prog. Neurobiol. 2000, 60:531-544.
    • (2000) Prog. Neurobiol. , vol.60 , pp. 531-544
    • Frank, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.