메뉴 건너뛰기




Volumn 106, Issue 3, 2008, Pages 1175-1183

Biochemical characterization of membrane-associated septin from rat brain

Author keywords

Heterooligomer; Lipid raft; Membrane; Polymerization; Septin

Indexed keywords

DETERGENT; MAGNESIUM CHLORIDE; MONOCLONAL ANTIBODY; OLIGOMER; SEPTIN; SEPTIN 11; SEPTIN 3;

EID: 48249138106     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2008.05450.x     Document Type: Article
Times cited : (6)

References (43)
  • 1
    • 0034707082 scopus 로고    scopus 로고
    • Insolubility of lipids in Triton X-100: Physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts)
    • Brown E. London D. A. (2000) Insolubility of lipids in Triton X-100: physical origin and relationship to sphingolipid/cholesterol membrane domains (rafts). Biochim. Biophys. Acta 1508, 182 195.
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 182-195
    • Brown, E.1    London, D.A.2
  • 2
  • 3
    • 33846834941 scopus 로고    scopus 로고
    • Targeted disruption of sept3, a heteromeric assembly partner of sept5 and sept7 in axons, has no effect on developing CNS neurons
    • Fujishima K., Kiyonari H., Kurisu J., Hirano T. Kengaku M. (2007) Targeted disruption of sept3, a heteromeric assembly partner of sept5 and sept7 in axons, has no effect on developing CNS neurons. J. Neurochem. 102, 77 92.
    • (2007) J. Neurochem. , vol.102 , pp. 77-92
    • Fujishima, K.1    Kiyonari, H.2    Kurisu, J.3    Hirano, T.4    Kengaku, M.5
  • 4
    • 0033583077 scopus 로고    scopus 로고
    • Characterization of a novel rat brain glycosylphosphatidylinositol- anchored protein (Kilon), a member of the IgLON cell adhesion molecule family
    • Funatsu N., Miyata S., Kumanogoh H., Shigeta M., Hamada K., Endo Y., Sokawa Y. Maekawa S. (1999) Characterization of a novel rat brain glycosylphosphatidylinositol-anchored protein (Kilon), a member of the IgLON cell adhesion molecule family. J. Biol. Chem. 274, 3224 3230.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3224-3230
    • Funatsu, N.1    Miyata, S.2    Kumanogoh, H.3    Shigeta, M.4    Hamada, K.5    Endo, Y.6    Sokawa, Y.7    Maekawa, S.8
  • 5
    • 0025954309 scopus 로고
    • Isolation of tyrosine-phosphorylated proteins and generation of monoclonal antibodies
    • Glenney J. R. (1991) Isolation of tyrosine-phosphorylated proteins and generation of monoclonal antibodies. Methods Enzymol. 201, 92 100.
    • (1991) Methods Enzymol. , vol.201 , pp. 92-100
    • Glenney, J.R.1
  • 6
    • 4644223252 scopus 로고    scopus 로고
    • Glycosynapses: Microdomains controlling carbohydrate-dependent cell adhesion and signaling
    • Hakomori S. (2004) Glycosynapses: microdomains controlling carbohydrate-dependent cell adhesion and signaling. An. Acad. Bras. Cienc. 76, 553 572.
    • (2004) An. Acad. Bras. Cienc. , vol.76 , pp. 553-572
    • Hakomori, S.1
  • 7
    • 0032103420 scopus 로고    scopus 로고
    • Subunit composition, protein interaction, and structure of the mammalian brain sec6/8 complex and septin filaments
    • Hsu S.-C., Hazuka C. D., Roth R., Foletti D. L., Heuser J. Scheller R. H. (1998) Subunit composition, protein interaction, and structure of the mammalian brain sec6/8 complex and septin filaments. Neuron 20, 1111 1122.
    • (1998) Neuron , vol.20 , pp. 1111-1122
    • Hsu, S.-C.1    Hazuka, C.D.2    Roth, R.3    Foletti, D.L.4    Heuser, J.5    Scheller, R.H.6
  • 8
    • 33846817344 scopus 로고    scopus 로고
    • Sept4, a component of presynaptic scaffold and Lewy bodies, is required for the suppression of α-synuclein neurotoxicity
    • Ihara M., Yamasaki N., Hagiwara A. et al. (2007) Sept4, a component of presynaptic scaffold and Lewy bodies, is required for the suppression of α-synuclein neurotoxicity. Neuron 53, 519 533.
    • (2007) Neuron , vol.53 , pp. 519-533
    • Ihara, M.1    Yamasaki, N.2    Hagiwara, A.3
  • 9
    • 33645295218 scopus 로고    scopus 로고
    • Lipid rafts in T cell receptor signaling
    • Kabouridis P. S. (2006) Lipid rafts in T cell receptor signaling. Mol. Membr. Biol. 23, 49 57.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 49-57
    • Kabouridis, P.S.1
  • 10
    • 0142024473 scopus 로고    scopus 로고
    • Assembly of mammalian septins
    • Kinoshita M. (2003) Assembly of mammalian septins. J. Biochem. (Tokyo) 134, 491 496.
    • (2003) J. Biochem. (Tokyo) , vol.134 , pp. 491-496
    • Kinoshita, M.1
  • 11
    • 30844461245 scopus 로고    scopus 로고
    • Diversity of septin scaffolds
    • Kinoshita M. (2006) Diversity of septin scaffolds. Curr. Opin. Cell Biol. 18, 54 60.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 54-60
    • Kinoshita, M.1
  • 13
    • 29144514689 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis: New insights into caveolae and non-caveolar lipid raft carriers
    • Kirkham M. Parton R. G. (2005) Clathrin-independent endocytosis: new insights into caveolae and non-caveolar lipid raft carriers. Biochim. Biophys. Acta 1746, 349 363.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 349-363
    • Kirkham, M.1    Parton, R.G.2
  • 14
    • 26244468767 scopus 로고    scopus 로고
    • Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4
    • Kremer B. E., Haystead T. Macara I. G. (2005) Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4. Mol. Biol. Cell 16, 4648 4659.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4648-4659
    • Kremer, B.E.1    Haystead, T.2    MacAra, I.G.3
  • 15
    • 0034717707 scopus 로고    scopus 로고
    • GAP43, MARCKS, and CAP23 modulate PI(4,5)P2 at plasmalemmal rafts, and regulate cell cortex actin dynamics through common mechanism
    • Laux T., Fukami K., Thelen M., Golub T., Frey D. Caroni P. (2000) GAP43, MARCKS, and CAP23 modulate PI(4,5)P2 at plasmalemmal rafts, and regulate cell cortex actin dynamics through common mechanism. J. Cell Biol. 149, 1455 1471.
    • (2000) J. Cell Biol. , vol.149 , pp. 1455-1471
    • Laux, T.1    Fukami, K.2    Thelen, M.3    Golub, T.4    Frey, D.5    Caroni, P.6
  • 16
    • 33750082712 scopus 로고    scopus 로고
    • Structural analysis of septin 2, 6, and 7 complexes
    • Low C. Macara I. G. (2006) Structural analysis of septin 2, 6, and 7 complexes. J. Biol. Chem. 281, 30697 30706.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30697-30706
    • Low, C.1    MacAra, I.G.2
  • 17
    • 38049091552 scopus 로고    scopus 로고
    • 3D reconstruction of mammalian septin filaments
    • Lukoyanova N., Baldwin S. A. Trinick J. (2008) 3D reconstruction of mammalian septin filaments. J. Mol. Biol. 376, 1 7.
    • (2008) J. Mol. Biol. , vol.376 , pp. 1-7
    • Lukoyanova, N.1    Baldwin, S.A.2    Trinick, J.3
  • 18
    • 0027432974 scopus 로고
    • Purification and molecular cloning of a novel acidic calmodulin binding protein from rat brain
    • Maekawa S., Maekawa M., Hattori S. Nakamura S. (1993) Purification and molecular cloning of a novel acidic calmodulin binding protein from rat brain. J. Biol. Chem. 268, 13703 13709.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13703-13709
    • Maekawa, S.1    Maekawa, M.2    Hattori, S.3    Nakamura, S.4
  • 19
    • 0027998997 scopus 로고
    • Inhibitory effect of calmodulin on phosphorylation of NAP-22 with protein kinase C
    • Maekawa S., Murofushi H. Nakamura S. (1994) Inhibitory effect of calmodulin on phosphorylation of NAP-22 with protein kinase C. J. Biol. Chem. 269, 19462 19465.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19462-19465
    • Maekawa, S.1    Murofushi, H.2    Nakamura, S.3
  • 20
    • 0033597776 scopus 로고    scopus 로고
    • Cholesterol dependent localization of NAP-22 on a neuronal membrane microdomain (raft)
    • Maekawa S., Sato C., Kitajima K., Funatsu N., Kumanogoh H. Sokawa Y. (1999) Cholesterol dependent localization of NAP-22 on a neuronal membrane microdomain (raft). J. Biol. Chem. 274, 21369 21374.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21369-21374
    • Maekawa, S.1    Sato, C.2    Kitajima, K.3    Funatsu, N.4    Kumanogoh, H.5    Sokawa, Y.6
  • 21
    • 0037429689 scopus 로고    scopus 로고
    • Molecular characterization of the detergent-insoluble cholesterol-rich membrane microdomain (raft) of the central nervous system
    • Maekawa S., Iino S. Miyata S. (2003) Molecular characterization of the detergent-insoluble cholesterol-rich membrane microdomain (raft) of the central nervous system. Biochim. Biophys. Acta 1610, 261 270.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 261-270
    • Maekawa, S.1    Iino, S.2    Miyata, S.3
  • 22
    • 0033067455 scopus 로고    scopus 로고
    • Glucolipid-enriched caveolar and caveolae-like domains in the nervous system
    • Masserini M., Palestini P. Pitto M. (1999) Glucolipid-enriched caveolar and caveolae-like domains in the nervous system. J. Neurochem. 73, 1 11.
    • (1999) J. Neurochem. , vol.73 , pp. 1-11
    • Masserini, M.1    Palestini, P.2    Pitto, M.3
  • 23
    • 34547857399 scopus 로고    scopus 로고
    • Lipid components in the detergent-resistant membrane microdomain (DRM) obtained from the synaptic plasma membrane of rat brain
    • Matsuura D., Taguchi K., Yagisawa H. Maekawa S. (2007) Lipid components in the detergent-resistant membrane microdomain (DRM) obtained from the synaptic plasma membrane of rat brain. Neurosci. Lett. 423, 158 161.
    • (2007) Neurosci. Lett. , vol.423 , pp. 158-161
    • Matsuura, D.1    Taguchi, K.2    Yagisawa, H.3    Maekawa, S.4
  • 24
    • 0038383953 scopus 로고    scopus 로고
    • Polarized targeting of IgLON cell adhesion molecule OBCAM to dendrites in cultured neurons
    • Miyata S., Matsumoto N. Maekawa S. (2003) Polarized targeting of IgLON cell adhesion molecule OBCAM to dendrites in cultured neurons. Brain Res. 979, 129 136.
    • (2003) Brain Res. , vol.979 , pp. 129-136
    • Miyata, S.1    Matsumoto, N.2    Maekawa, S.3
  • 25
    • 11244292287 scopus 로고    scopus 로고
    • Biochemical and cell biological analyses of a mammalian septin complex, sept7/9b/11
    • Nagata K.-I., Asano T., Nozawa Y. Inagaki M. (2004) Biochemical and cell biological analyses of a mammalian septin complex, sept7/9b/11. J. Biol. Chem. 279, 55895 55904.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55895-55904
    • Nagata, K.-I.1    Asano, T.2    Nozawa, Y.3    Inagaki, M.4
  • 26
    • 0031684860 scopus 로고    scopus 로고
    • Purification and assembly of a septin complex from Drosophila embryos
    • Oegema K., Desai A., Wong M. I., Michison T. Field C. M. (1998) Purification and assembly of a septin complex from Drosophila embryos. Meth. Enzymol. 298, 279 295.
    • (1998) Meth. Enzymol. , vol.298 , pp. 279-295
    • Oegema, K.1    Desai, A.2    Wong, M.I.3    Michison, T.4    Field, C.M.5
  • 27
    • 0036132908 scopus 로고    scopus 로고
    • The septin CDCrel-1 is dispensable for normal development and neurotransmitter release
    • Peng X.-R., Jia Z., Zang Y., Ware J. Trimble W. S. (2002) The septin CDCrel-1 is dispensable for normal development and neurotransmitter release. Mol. Cell. Biol. 22, 378 387.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 378-387
    • Peng, X.-R.1    Jia, Z.2    Zang, Y.3    Ware, J.4    Trimble, W.S.5
  • 28
    • 1842484428 scopus 로고    scopus 로고
    • Lipid rafts and the regulation of exocytosis
    • Salaun C., James D. J. Chamberlain L. H. (2004) Lipid rafts and the regulation of exocytosis. Traffic 5, 255 264.
    • (2004) Traffic , vol.5 , pp. 255-264
    • Salaun, C.1    James, D.J.2    Chamberlain, L.H.3
  • 29
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • Schagger H., Cramer W. A. von Jagow G. (1994) Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 217, 220 230.
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schagger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 30
    • 2642575982 scopus 로고    scopus 로고
    • A barrier to lateral diffusion in the cleavage furrow of dividing mammalian cells
    • Schmidt K. Nichols B. J. (2004) A barrier to lateral diffusion in the cleavage furrow of dividing mammalian cells. Curr. Biol. 14, 1002 1006.
    • (2004) Curr. Biol. , vol.14 , pp. 1002-1006
    • Schmidt, K.1    Nichols, B.J.2
  • 32
    • 0037474299 scopus 로고    scopus 로고
    • Borg/septin and the assembly of mammalian septin heterodimers, trimers, and filaments
    • Sheffield P. J., Oliver C. J., Kremer B. E., Sheng S., Shao Z. Macara I. S. (2003) Borg/septin and the assembly of mammalian septin heterodimers, trimers, and filaments. J. Biol. Chem. 278, 3483 3489.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3483-3489
    • Sheffield, P.J.1    Oliver, C.J.2    Kremer, B.E.3    Sheng, S.4    Shao, Z.5    MacAra, I.S.6
  • 34
    • 31644446955 scopus 로고    scopus 로고
    • Here come the septins: Novel polymers that coordinate intracellular functions and organization
    • Spiliotis E. T. Nelson W. J. (2006) Here come the septins: novel polymers that coordinate intracellular functions and organization. J. Cell Sci. 119, 4 10.
    • (2006) J. Cell Sci. , vol.119 , pp. 4-10
    • Spiliotis, E.T.1    Nelson, W.J.2
  • 35
    • 35348834213 scopus 로고    scopus 로고
    • Role of septin cytoskeleton in spine morphogenesis and dendrite development in neurons
    • Tada T., Simonetta A., Batterton M., Kinoshita M., Edbauer D. Sheng M. (2007) Role of septin cytoskeleton in spine morphogenesis and dendrite development in neurons. Curr. Biol. 17, 1752 1758.
    • (2007) Curr. Biol. , vol.17 , pp. 1752-1758
    • Tada, T.1    Simonetta, A.2    Batterton, M.3    Kinoshita, M.4    Edbauer, D.5    Sheng, M.6
  • 36
    • 23844512460 scopus 로고    scopus 로고
    • Biochemical and morphologic evidence of the interaction of oligodendrocyte membrane rafts with actin filaments
    • Taguchi K., Yoshinaka K., Yoshino K.-I., Yonezawa K. Maekawa S. (2005) Biochemical and morphologic evidence of the interaction of oligodendrocyte membrane rafts with actin filaments. J. Neurosci. Res. 81, 218 225.
    • (2005) J. Neurosci. Res. , vol.81 , pp. 218-225
    • Taguchi, K.1    Yoshinaka, K.2    Yoshino, K.-I.3    Yonezawa, K.4    Maekawa, S.5
  • 39
    • 33749165924 scopus 로고    scopus 로고
    • Structural insights into yeast septin organization from polarized fluorescence microscopy
    • Vrabioiu A. Mitchison T. J. (2006) Structural insights into yeast septin organization from polarized fluorescence microscopy. Nature 443, 466 469.
    • (2006) Nature , vol.443 , pp. 466-469
    • Vrabioiu, A.1    Mitchison, T.J.2
  • 40
    • 35348907374 scopus 로고    scopus 로고
    • The GTP-binding protein septin 7 is critical for dendrite branching and dendritic-spine morphology
    • Xie T., Vessey J. P., Konecna A., Dahm R., Macchl P. Kiebler M. A. (2007) The GTP-binding protein septin 7 is critical for dendrite branching and dendritic-spine morphology. Curr. Biol. 17, 1746 1751.
    • (2007) Curr. Biol. , vol.17 , pp. 1746-1751
    • Xie, T.1    Vessey, J.P.2    Konecna, A.3    Dahm, R.4    MacChl, P.5    Kiebler, M.A.6
  • 41
    • 4344573131 scopus 로고    scopus 로고
    • Phosphorylation of septin 3 on ser-91 by cGMP-dependent protein kinase-I in nerve terminals
    • Xue J., Milburn P. J., Hanna B. T., Graham M. E., Rostas J. A. Robinson P. J. (2004) Phosphorylation of septin 3 on ser-91 by cGMP-dependent protein kinase-I in nerve terminals. Biochem. J. 381, 753 760.
    • (2004) Biochem. J. , vol.381 , pp. 753-760
    • Xue, J.1    Milburn, P.J.2    Hanna, B.T.3    Graham, M.E.4    Rostas, J.A.5    Robinson, P.J.6
  • 42
  • 43
    • 2542446264 scopus 로고    scopus 로고
    • Identification of V-ATPase as a major component in the raft fraction prepared from the synaptic plasma membrane and the synaptic vesicle of rat brain
    • Yoshinaka K., Kumanogoh H., Nakamura S. Maekawa S. (2004) Identification of V-ATPase as a major component in the raft fraction prepared from the synaptic plasma membrane and the synaptic vesicle of rat brain. Neurosci. Lett. 363, 168 172.
    • (2004) Neurosci. Lett. , vol.363 , pp. 168-172
    • Yoshinaka, K.1    Kumanogoh, H.2    Nakamura, S.3    Maekawa, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.