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Volumn 68, Issue 9, 2011, Pages 512-525

Submembranous septins as relatively stable components of actin-based membrane skeleton

Author keywords

Cortical actin; Diffusion barrier; Fluorescence recovery after photobleaching; Membrane skeleton

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; ASPARTATE AMINOTRANSFERASE; JASPAMIDE; MEMBRANE PROTEIN; SCAFFOLD PROTEIN; SEPTIN; SYNTAXIN 1A;

EID: 80052964158     PISSN: 19493584     EISSN: 19493592     Source Type: Journal    
DOI: 10.1002/cm.20528     Document Type: Article
Times cited : (58)

References (63)
  • 1
    • 0015251678 scopus 로고
    • Neurotransmitter synthesis by neuroblastoma clones (neuroblast differentiation-cell culture-choline acetyltransferase-acetylcholinesterase-tyrosine hydroxylase-axons-dendrites)
    • Amano T, Richelson E, Nirenberg M. 1972. Neurotransmitter synthesis by neuroblastoma clones (neuroblast differentiation-cell culture-choline acetyltransferase-acetylcholinesterase-tyrosine hydroxylase-axons-dendrites). Proc Natl Acad Sci USA 69(1): 258-263.
    • (1972) Proc Natl Acad Sci USA , vol.69 , Issue.1 , pp. 258-263
    • Amano, T.1    Richelson, E.2    Nirenberg, M.3
  • 2
    • 0033363646 scopus 로고    scopus 로고
    • The septin CDCrel-1 binds syntaxin and inhibits exocytosis
    • Beites CL, Xie H, Bowser R, Trimble WS. 1999. The septin CDCrel-1 binds syntaxin and inhibits exocytosis. Nat Neurosci 2(5): 434-439.
    • (1999) Nat Neurosci , vol.2 , Issue.5 , pp. 434-439
    • Beites, C.L.1    Xie, H.2    Bowser, R.3    Trimble, W.S.4
  • 3
    • 12844273556 scopus 로고    scopus 로고
    • The septin Sept5/CDCrel-1 competes with alpha-SNAP for binding to the SNARE complex
    • Beites CL, Campbell KA, Trimble WS. 2005. The septin Sept5/CDCrel-1 competes with alpha-SNAP for binding to the SNARE complex. Biochem J 385(Pt. 2): 347-353.
    • (2005) Biochem J , vol.385 , Issue.PART 2 , pp. 347-353
    • Beites, C.L.1    Campbell, K.A.2    Trimble, W.S.3
  • 4
    • 64549158361 scopus 로고    scopus 로고
    • Septins and the lateral compartmentalization of eukaryotic membranes
    • Caudron F, Barral Y. 2009. Septins and the lateral compartmentalization of eukaryotic membranes. Dev Cell 16(4): 493-506.
    • (2009) Dev Cell , vol.16 , Issue.4 , pp. 493-506
    • Caudron, F.1    Barral, Y.2
  • 5
    • 0141541745 scopus 로고    scopus 로고
    • The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast
    • Caviston JP, Longtine M, Pringle JR, Bi E. 2003. The role of Cdc42p GTPase-activating proteins in assembly of the septin ring in yeast. Mol Biol Cell 14(10): 4051-4066.
    • (2003) Mol Biol Cell , vol.14 , Issue.10 , pp. 4051-4066
    • Caviston, J.P.1    Longtine, M.2    Pringle, J.R.3    Bi, E.4
  • 6
    • 77953592433 scopus 로고    scopus 로고
    • Cellular requirements for the small molecule forchlorfenuron to stabilize the septin cytoskeleton
    • DeMay BS, Meseroll RA, Occhipinti P, Gladfelter AS. 2010. Cellular requirements for the small molecule forchlorfenuron to stabilize the septin cytoskeleton. Cytoskeleton (Hoboken) 67(6): 383-399.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , Issue.6 , pp. 383-399
    • DeMay, B.S.1    Meseroll, R.A.2    Occhipinti, P.3    Gladfelter, A.S.4
  • 8
    • 0037345639 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of septin dynamics during the cell cycle
    • Dobbelaere J, Gentry MS, Hallberg RL, Barral Y. 2003. Phosphorylation-dependent regulation of septin dynamics during the cell cycle. Dev Cell 4(3): 345-357.
    • (2003) Dev Cell , vol.4 , Issue.3 , pp. 345-357
    • Dobbelaere, J.1    Gentry, M.S.2    Hallberg, R.L.3    Barral, Y.4
  • 11
    • 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(1): 77-92.
    • (2007) J Neurochem , vol.102 , Issue.1 , pp. 77-92
    • Fujishima, K.1    Kiyonari, H.2    Kurisu, J.3    Hirano, T.4    Kengaku, M.5
  • 12
    • 0037054546 scopus 로고    scopus 로고
    • Phospholipids undergo hop diffusion in compartmentalized cell membrane
    • Fujiwara T, Ritchie K, Murakoshi H, Jacobson K, Kusumi A. 2002. Phospholipids undergo hop diffusion in compartmentalized cell membrane. J Cell Biol 157(6): 1071-1081.
    • (2002) J Cell Biol , vol.157 , Issue.6 , pp. 1071-1081
    • Fujiwara, T.1    Ritchie, K.2    Murakoshi, H.3    Jacobson, K.4    Kusumi, A.5
  • 13
    • 77955858279 scopus 로고    scopus 로고
    • Control of cortical rigidity by the cytoskeleton: emerging roles for septins
    • Gilden J, Krummel MF. 2010. Control of cortical rigidity by the cytoskeleton: emerging roles for septins. Cytoskeleton (Hoboken) 67(8): 477-486.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , Issue.8 , pp. 477-486
    • Gilden, J.1    Krummel, M.F.2
  • 14
    • 0030474931 scopus 로고    scopus 로고
    • Assembly of ring canals in the male germ line from structural components of the contractile ring
    • Hime GR, Brill JA, Fuller MT. 1996. Assembly of ring canals in the male germ line from structural components of the contractile ring. J Cell Sci 109 (Pt. 12): 2779-2788.
    • (1996) J Cell Sci , vol.109 , Issue.PART 12 , pp. 2779-2788
    • Hime, G.R.1    Brill, J.A.2    Fuller, M.T.3
  • 15
    • 0019859146 scopus 로고
    • Quick-freeze, deep-etch visualization of the cytoskeleton beneath surface differentiations of intestinal epithelial cells
    • Hirokawa N, Heuser JE. 1981. Quick-freeze, deep-etch visualization of the cytoskeleton beneath surface differentiations of intestinal epithelial cells. J Cell Biol 91(2 Pt. 1): 399-409.
    • (1981) J Cell Biol , vol.91 , Issue.2 PART 1 , pp. 399-409
    • Hirokawa, N.1    Heuser, J.E.2
  • 16
    • 57649194799 scopus 로고    scopus 로고
    • Forchlorfenuron alters mammalian septin assembly, organization, and dynamics
    • Hu Q, Nelson WJ, Spiliotis ET. 2008. Forchlorfenuron alters mammalian septin assembly, organization, and dynamics. J Biol Chem 283(43): 29563-29571.
    • (2008) J Biol Chem , vol.283 , Issue.43 , pp. 29563-29571
    • Hu, Q.1    Nelson, W.J.2    Spiliotis, E.T.3
  • 17
    • 77954841928 scopus 로고    scopus 로고
    • A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution
    • Hu Q, Milenkovic L, Jin H, Scott MP, Nachury MV, Spiliotis ET, Nelson WJ. 2010. A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution. Science 329(5990): 436-439.
    • (2010) Science , vol.329 , Issue.5990 , pp. 436-439
    • Hu, Q.1    Milenkovic, L.2    Jin, H.3    Scott, M.P.4    Nachury, M.V.5    Spiliotis, E.T.6    Nelson, W.J.7
  • 19
    • 20044369350 scopus 로고    scopus 로고
    • Cortical organization by the septin cytoskeleton is essential for structural and mechanical integrity of mammalian spermatozoa
    • Ihara M, Kinoshita A, Yamada S, Tanaka H, Tanigaki A, Kitano A, Goto M, Okubo K, Nishiyama H, Ogawa O, et al. 2005. Cortical organization by the septin cytoskeleton is essential for structural and mechanical integrity of mammalian spermatozoa. Dev Cell 8(3): 343-352.
    • (2005) Dev Cell , vol.8 , Issue.3 , pp. 343-352
    • Ihara, M.1    Kinoshita, A.2    Yamada, S.3    Tanaka, H.4    Tanigaki, A.5    Kitano, A.6    Goto, M.7    Okubo, K.8    Nishiyama, H.9    Ogawa, O.10
  • 20
    • 33846817344 scopus 로고    scopus 로고
    • Sept4, a component of presynaptic scaffold and lewy bodies, is required for the suppression of alpha-synuclein neurotoxicity
    • Ihara M, Yamasaki N, Hagiwara A, Tanigaki A, Kitano A, Hikawa R, Tomimoto H, Noda M, Takanashi M, Mori H, et al. 2007. Sept4, a component of presynaptic scaffold and lewy bodies, is required for the suppression of alpha-synuclein neurotoxicity. Neuron 53(4): 519-533.
    • (2007) Neuron , vol.53 , Issue.4 , pp. 519-533
    • Ihara, M.1    Yamasaki, N.2    Hagiwara, A.3    Tanigaki, A.4    Kitano, A.5    Hikawa, R.6    Tomimoto, H.7    Noda, M.8    Takanashi, M.9    Mori, H.10
  • 22
    • 35548961325 scopus 로고    scopus 로고
    • Mammalian SEPT2 is required for scaffolding nonmuscle myosin II and its kinases
    • Joo E, Surka MC, Trimble WS. 2007. Mammalian SEPT2 is required for scaffolding nonmuscle myosin II and its kinases. Dev Cell 13(5): 677-690.
    • (2007) Dev Cell , vol.13 , Issue.5 , pp. 677-690
    • Joo, E.1    Surka, M.C.2    Trimble, W.S.3
  • 24
    • 0035954427 scopus 로고    scopus 로고
    • Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B
    • Kimura H, Cook PR. 2001. Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B. J Cell Biol 153(7): 1341-1353.
    • (2001) J Cell Biol , vol.153 , Issue.7 , pp. 1341-1353
    • Kimura, H.1    Cook, P.R.2
  • 25
    • 1642494582 scopus 로고    scopus 로고
    • Measuring histone and polymerase dynamics in living cells
    • Kimura H, Hieda M, Cook PR. 2004. Measuring histone and polymerase dynamics in living cells. Methods Enzymol 375: 381-393.
    • (2004) Methods Enzymol , vol.375 , pp. 381-393
    • Kimura, H.1    Hieda, M.2    Cook, P.R.3
  • 26
    • 0034639356 scopus 로고    scopus 로고
    • Differential localization of septins in the mouse brain
    • Kinoshita A, Noda M, Kinoshita M. 2000. Differential localization of septins in the mouse brain. J Comp Neurol 428(2): 223-239.
    • (2000) J Comp Neurol , vol.428 , Issue.2 , pp. 223-239
    • Kinoshita, A.1    Noda, M.2    Kinoshita, M.3
  • 27
    • 0030943556 scopus 로고    scopus 로고
    • Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures
    • Kinoshita M, Kumar S, Mizoguchi A, Ide C, Kinoshita A, Haraguchi T, Hiraoka Y, Noda M. 1997. Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures. Genes Dev 11(12): 1535-1547.
    • (1997) Genes Dev , vol.11 , Issue.12 , pp. 1535-1547
    • Kinoshita, M.1    Kumar, S.2    Mizoguchi, A.3    Ide, C.4    Kinoshita, A.5    Haraguchi, T.6    Hiraoka, Y.7    Noda, M.8
  • 29
    • 0842324006 scopus 로고    scopus 로고
    • Mammalian septin Sept2 modulates the activity of GLAST, a glutamate transporter in astrocytes
    • Kinoshita N, Kimura K, Matsumoto N, Watanabe M, Fukaya M, Ide C. 2004. Mammalian septin Sept2 modulates the activity of GLAST, a glutamate transporter in astrocytes. Genes Cells 9(1): 1-14.
    • (2004) Genes Cells , vol.9 , Issue.1 , pp. 1-14
    • Kinoshita, N.1    Kimura, K.2    Matsumoto, N.3    Watanabe, M.4    Fukaya, M.5    Ide, C.6
  • 31
    • 26244468767 scopus 로고    scopus 로고
    • Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4
    • Kremer BE, Haystead T, Macara IG. 2005. Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4. Mol Biol Cell 16(10): 4648-4659.
    • (2005) Mol Biol Cell , vol.16 , Issue.10 , pp. 4648-4659
    • Kremer, B.E.1    Haystead, T.2    Macara, I.G.3
  • 32
    • 34548289288 scopus 로고    scopus 로고
    • Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7
    • Kremer BE, Adang LA, Macara IG. 2007. Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7. Cell 130(5): 837-850.
    • (2007) Cell , vol.130 , Issue.5 , pp. 837-850
    • Kremer, B.E.1    Adang, L.A.2    Macara, I.G.3
  • 33
    • 9644284452 scopus 로고    scopus 로고
    • Single-molecule tracking of membrane molecules: plasma membrane compartmentalization and dynamic assembly of raft-philic signaling molecules
    • Kusumi A, Ike H, Nakada C, Murase K, Fujiwara T. 2005. Single-molecule tracking of membrane molecules: plasma membrane compartmentalization and dynamic assembly of raft-philic signaling molecules. Semin Immunol 17(1): 3-21.
    • (2005) Semin Immunol , vol.17 , Issue.1 , pp. 3-21
    • Kusumi, A.1    Ike, H.2    Nakada, C.3    Murase, K.4    Fujiwara, T.5
  • 34
    • 77953814967 scopus 로고    scopus 로고
    • The annulus of the mouse sperm tail is required to establish a membrane diffusion barrier that is engaged during the late steps of spermiogenesis
    • Kwitny S, Klaus AV, Hunnicutt GR. 2010. The annulus of the mouse sperm tail is required to establish a membrane diffusion barrier that is engaged during the late steps of spermiogenesis. Biol Reprod 82(4): 669-678.
    • (2010) Biol Reprod , vol.82 , Issue.4 , pp. 669-678
    • Kwitny, S.1    Klaus, A.V.2    Hunnicutt, G.R.3
  • 35
    • 0023075439 scopus 로고
    • Distribution of myosin and relationship to actin organization in cortical and subcortical areas of antibody-labelled, quick-frozen, deep-etched fibroblast cytoskeletons
    • Lawson D. 1987. Distribution of myosin and relationship to actin organization in cortical and subcortical areas of antibody-labelled, quick-frozen, deep-etched fibroblast cytoskeletons. Cell Motil Cytoskeleton 7(4): 368-380.
    • (1987) Cell Motil Cytoskeleton , vol.7 , Issue.4 , pp. 368-380
    • Lawson, D.1
  • 37
    • 71049147069 scopus 로고    scopus 로고
    • Septins: molecular partitioning and the generation of cellular asymmetry
    • McMurray MA, Thorner J. 2009. Septins: molecular partitioning and the generation of cellular asymmetry. Cell Div 4: 18.
    • (2009) Cell Div , vol.4 , pp. 18
    • McMurray, M.A.1    Thorner, J.2
  • 38
    • 0030048198 scopus 로고    scopus 로고
    • Labeling neural cells using adenoviral gene transfer of membrane-targeted GFP
    • Moriyoshi K, Richards LJ, Akazawa C, O'Leary DD, Nakanishi S. 1996. Labeling neural cells using adenoviral gene transfer of membrane-targeted GFP. Neuron 16(2): 255-260.
    • (1996) Neuron , vol.16 , Issue.2 , pp. 255-260
    • Moriyoshi, K.1    Richards, L.J.2    Akazawa, C.3    O'Leary, D.D.4    Nakanishi, S.5
  • 39
    • 33748579946 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography
    • Morone N, Fujiwara T, Murase K, Kasai RS, Ike H, Yuasa S, Usukura J, Kusumi A. 2006. Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography. J Cell Biol 174(6): 851-862.
    • (2006) J Cell Biol , vol.174 , Issue.6 , pp. 851-862
    • Morone, N.1    Fujiwara, T.2    Murase, K.3    Kasai, R.S.4    Ike, H.5    Yuasa, S.6    Usukura, J.7    Kusumi, A.8
  • 40
  • 41
    • 0034618062 scopus 로고    scopus 로고
    • Functional analysis of a human homologue of the Drosophila actin binding protein anillin suggests a role in cytokinesis
    • Oegema K, Savoian MS, Mitchison TJ, Field CM. 2000. Functional analysis of a human homologue of the Drosophila actin binding protein anillin suggests a role in cytokinesis. J Cell Biol 150(3): 539-552.
    • (2000) J Cell Biol , vol.150 , Issue.3 , pp. 539-552
    • Oegema, K.1    Savoian, M.S.2    Mitchison, T.J.3    Field, C.M.4
  • 42
    • 0036132908 scopus 로고    scopus 로고
    • The septin CDCrel-1 is dispensable for normal development and neurotransmitter release
    • Peng XR, Jia Z, Zhang Y, Ware J, Trimble WS. 2002. The septin CDCrel-1 is dispensable for normal development and neurotransmitter release. Mol Cell Biol 22(1): 378-387.
    • (2002) Mol Cell Biol , vol.22 , Issue.1 , pp. 378-387
    • Peng, X.R.1    Jia, Z.2    Zhang, Y.3    Ware, J.4    Trimble, W.S.5
  • 45
    • 0037474299 scopus 로고    scopus 로고
    • Borg/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments
    • Sheffield PJ, Oliver CJ, Kremer BE, Sheng S, Shao Z, Macara IG. 2003. Borg/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments. J Biol Chem 278(5): 3483-3488.
    • (2003) J Biol Chem , vol.278 , Issue.5 , pp. 3483-3488
    • Sheffield, P.J.1    Oliver, C.J.2    Kremer, B.E.3    Sheng, S.4    Shao, Z.5    Macara, I.G.6
  • 47
    • 24644441368 scopus 로고    scopus 로고
    • The comings and goings of actin: coupling protrusion and retraction in cell motility
    • Small JV, Resch GP. 2005. The comings and goings of actin: coupling protrusion and retraction in cell motility. Curr Opin Cell Biol 17(5): 517-523.
    • (2005) Curr Opin Cell Biol , vol.17 , Issue.5 , pp. 517-523
    • Small, J.V.1    Resch, G.P.2
  • 48
    • 77953590866 scopus 로고    scopus 로고
    • Regulation of microtubule organization and functions by septin GTPases
    • Spiliotis ET. 2010. Regulation of microtubule organization and functions by septin GTPases. Cytoskeleton (Hoboken) 67(6): 339-345.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , Issue.6 , pp. 339-345
    • Spiliotis, E.T.1
  • 49
    • 15244346231 scopus 로고    scopus 로고
    • A mitotic septin scaffold required for mammalian chromosome congression and segregation
    • Spiliotis ET, Kinoshita M, Nelson WJ. 2005. A mitotic septin scaffold required for mammalian chromosome congression and segregation. Science 307(5716): 1781-1785.
    • (2005) Science , vol.307 , Issue.5716 , pp. 1781-1785
    • Spiliotis, E.T.1    Kinoshita, M.2    Nelson, W.J.3
  • 50
    • 38749147682 scopus 로고    scopus 로고
    • Epithelial polarity requires septin coupling of vesicle transport to polyglutamylated microtubules
    • Spiliotis ET, Hunt SJ, Hu Q, Kinoshita M, Nelson WJ. 2008. Epithelial polarity requires septin coupling of vesicle transport to polyglutamylated microtubules. J Cell Biol 180(2): 295-303.
    • (2008) J Cell Biol , vol.180 , Issue.2 , pp. 295-303
    • Spiliotis, E.T.1    Hunt, S.J.2    Hu, Q.3    Kinoshita, M.4    Nelson, W.J.5
  • 51
    • 13244291467 scopus 로고    scopus 로고
    • FRAP analysis of binding: proper and fitting
    • Sprague BL, McNally JG. 2005. FRAP analysis of binding: proper and fitting. Trends Cell Biol 15(2): 84-91.
    • (2005) Trends Cell Biol , vol.15 , Issue.2 , pp. 84-91
    • Sprague, B.L.1    McNally, J.G.2
  • 53
    • 0036798406 scopus 로고    scopus 로고
    • The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis
    • Surka MC, Tsang CW, Trimble WS. 2002. The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis. Mol Biol Cell 13(10): 3532-3545.
    • (2002) Mol Biol Cell , vol.13 , Issue.10 , pp. 3532-3545
    • Surka, M.C.1    Tsang, C.W.2    Trimble, W.S.3
  • 54
    • 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(20): 1752-1758.
    • (2007) Curr Biol , vol.17 , Issue.20 , pp. 1752-1758
    • Tada, T.1    Simonetta, A.2    Batterton, M.3    Kinoshita, M.4    Edbauer, D.5    Sheng, M.6
  • 55
    • 58349115398 scopus 로고    scopus 로고
    • Septin-mediated uniform bracing of phospholipid membranes
    • Tanaka-Takiguchi Y, Kinoshita M, Takiguchi K. 2009. Septin-mediated uniform bracing of phospholipid membranes. Curr Biol 19(2): 140-145.
    • (2009) Curr Biol , vol.19 , Issue.2 , pp. 140-145
    • Tanaka-Takiguchi, Y.1    Kinoshita, M.2    Takiguchi, K.3
  • 57
    • 33749165924 scopus 로고    scopus 로고
    • Structural insights into yeast septin organization from polarized fluorescence microscopy
    • Vrabioiu AM, Mitchison TJ. 2006. Structural insights into yeast septin organization from polarized fluorescence microscopy. Nature 443(7110): 466-469.
    • (2006) Nature , vol.443 , Issue.7110 , pp. 466-469
    • Vrabioiu, A.M.1    Mitchison, T.J.2
  • 58
    • 0037039770 scopus 로고    scopus 로고
    • Single-molecule speckle analysis of actin filament turnover in lamellipodia
    • Watanabe N, Mitchison TJ. 2002. Single-molecule speckle analysis of actin filament turnover in lamellipodia. Science 295(5557): 1083-1086.
    • (2002) Science , vol.295 , Issue.5557 , pp. 1083-1086
    • Watanabe, N.1    Mitchison, T.J.2
  • 59
    • 35348907374 scopus 로고    scopus 로고
    • The GTP-binding protein Septin 7 is critical for dendrite branching and dendritic-spine morphology
    • Xie Y, Vessey JP, Konecna A, Dahm R, Macchi P, Kiebler MA. 2007. The GTP-binding protein Septin 7 is critical for dendrite branching and dendritic-spine morphology. Curr Biol 17(20): 1746-1751.
    • (2007) Curr Biol , vol.17 , Issue.20 , pp. 1746-1751
    • Xie, Y.1    Vessey, J.P.2    Konecna, A.3    Dahm, R.4    Macchi, P.5    Kiebler, M.A.6
  • 60
    • 7244262110 scopus 로고    scopus 로고
    • Septin 3 (G-septin) is a developmentally regulated phosphoprotein enriched in presynaptic nerve terminals
    • Xue J, Tsang CW, Gai WP, Malladi CS, Trimble WS, Rostas JA, Robinson PJ. 2004. Septin 3 (G-septin) is a developmentally regulated phosphoprotein enriched in presynaptic nerve terminals. J Neurochem 91(3): 579-590.
    • (2004) J Neurochem , vol.91 , Issue.3 , pp. 579-590
    • Xue, J.1    Tsang, C.W.2    Gai, W.P.3    Malladi, C.S.4    Trimble, W.S.5    Rostas, J.A.6    Robinson, P.J.7
  • 61
    • 33646794407 scopus 로고    scopus 로고
    • Glutamate transporters GLAST and EAAT4 regulate postischemic Purkinje cell death: an in vivo study using a cardiac arrest model in mice lacking GLAST or EAAT4
    • Yamashita A, Makita K, Kuroiwa T, Tanaka K. 2006. Glutamate transporters GLAST and EAAT4 regulate postischemic Purkinje cell death: an in vivo study using a cardiac arrest model in mice lacking GLAST or EAAT4. Neurosci Res 55(3): 264-270.
    • (2006) Neurosci Res , vol.55 , Issue.3 , pp. 264-270
    • Yamashita, A.1    Makita, K.2    Kuroiwa, T.3    Tanaka, K.4
  • 62
    • 77954463587 scopus 로고    scopus 로고
    • Septins regulate developmental switching from microdomain to nanodomain coupling of Ca(2+) influx to neurotransmitter release at a central synapse
    • Yang YM, Fedchyshyn MJ, Grande G, Aitoubah J, Tsang CW, Xie H, Ackerley CA, Trimble WS, Wang LY. 2010. Septins regulate developmental switching from microdomain to nanodomain coupling of Ca(2+) influx to neurotransmitter release at a central synapse. Neuron 67(1): 100-115.
    • (2010) Neuron , vol.67 , Issue.1 , pp. 100-115
    • Yang, Y.M.1    Fedchyshyn, M.J.2    Grande, G.3    Aitoubah, J.4    Tsang, C.W.5    Xie, H.6    Ackerley, C.A.7    Trimble, W.S.8    Wang, L.Y.9
  • 63
    • 0033576647 scopus 로고    scopus 로고
    • Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP
    • Zhang J, Kong C, Xie H, McPherson PS, Grinstein S, Trimble WS. 1999. Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP. Curr Biol 9(24): 1458-1467.
    • (1999) Curr Biol , vol.9 , Issue.24 , pp. 1458-1467
    • Zhang, J.1    Kong, C.2    Xie, H.3    McPherson, P.S.4    Grinstein, S.5    Trimble, W.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.