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Volumn 28, Issue 23, 2008, Pages 7012-7029

Superfluous role of mammalian septins 3 and 5 in neuronal development and synaptic transmission

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN SEPTIN 3; PROTEIN SEPTIN 5; SEPTIN; UNCLASSIFIED DRUG;

EID: 57349193607     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.00035-08     Document Type: Article
Times cited : (43)

References (77)
  • 1
    • 0034494631 scopus 로고    scopus 로고
    • Evidence for functional differentiation among Drosophila septins in cytokinesis and cellularization
    • Adam, J. C., J. R. Pringle, and M. Peifer. 2000. Evidence for functional differentiation among Drosophila septins in cytokinesis and cellularization. Mol. Biol. Cell 11:3123-3135.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3123-3135
    • Adam, J.C.1    Pringle, J.R.2    Peifer, M.3
  • 3
    • 3142692470 scopus 로고    scopus 로고
    • Abnormalities of presynaptic protein CDCrel-1 in striatum of rats reared in social isolation: Relevance to neural connectivity in schizophrenia
    • Barr, A. M., C. E. Young, K. Sawada, W. S. Trimble, A. G. Phillips, and W. G. Honer. 2004. Abnormalities of presynaptic protein CDCrel-1 in striatum of rats reared in social isolation: relevance to neural connectivity in schizophrenia. Eur. J. Neurosci. 20:303-307.
    • (2004) Eur. J. Neurosci , vol.20 , pp. 303-307
    • Barr, A.M.1    Young, C.E.2    Sawada, K.3    Trimble, W.S.4    Phillips, A.G.5    Honer, W.G.6
  • 4
    • 0033363646 scopus 로고    scopus 로고
    • The septin CDCrel-1 binds syntaxin and inhibits exocytosis
    • Beites, C. L., H. Xie, R. Bowser, and W. S. Trimble. 1999. The septin CDCrel-1 binds syntaxin and inhibits exocytosis. Nat. Neurosci. 2:434-439.
    • (1999) Nat. Neurosci , vol.2 , pp. 434-439
    • Beites, C.L.1    Xie, H.2    Bowser, R.3    Trimble, W.S.4
  • 5
    • 0345236609 scopus 로고    scopus 로고
    • Mid2p stabilizes septin rings during cytokinesis in fission yeast
    • Berlin, A., A. Paoletti, and F. Chang. 2003. Mid2p stabilizes septin rings during cytokinesis in fission yeast. J. Cell Biol. 160:1083-1092.
    • (2003) J. Cell Biol , vol.160 , pp. 1083-1092
    • Berlin, A.1    Paoletti, A.2    Chang, F.3
  • 6
    • 0029616349 scopus 로고
    • Pre- and postsynaptic whole-cell recordings in the medial nucleus of the trapezoid body of the rat
    • Borst, J. G., F. Helmchen, and B. Sakmann. 1995. Pre- and postsynaptic whole-cell recordings in the medial nucleus of the trapezoid body of the rat. J. Physiol. 489:825-840.
    • (1995) J. Physiol , vol.489 , pp. 825-840
    • Borst, J.G.1    Helmchen, F.2    Sakmann, B.3
  • 7
    • 0031963588 scopus 로고    scopus 로고
    • Calcium current during a single action potential in a large presynaptic terminal of the rat brainstem
    • Borst, J. G., and B. Sakmann. 1998. Calcium current during a single action potential in a large presynaptic terminal of the rat brainstem. J. Physiol. 506:143-157.
    • (1998) J. Physiol , vol.506 , pp. 143-157
    • Borst, J.G.1    Sakmann, B.2
  • 8
    • 0027226219 scopus 로고
    • Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination
    • Brewer, G. J., J. R. Torricelli, E. K. Evege, and P. J. Price. 1993. Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination. J. Neurosci. Res. 35:567-576.
    • (1993) J. Neurosci. Res , vol.35 , pp. 567-576
    • Brewer, G.J.1    Torricelli, J.R.2    Evege, E.K.3    Price, P.J.4
  • 9
    • 0017153996 scopus 로고
    • A highly ordered ring of membrane-associated filaments in budding yeast
    • Byers, B., and L. Goetsch. 1976. A highly ordered ring of membrane-associated filaments in budding yeast. J. Cell Biol. 69:717-721.
    • (1976) J. Cell Biol , vol.69 , pp. 717-721
    • Byers, B.1    Goetsch, L.2
  • 10
    • 0037383708 scopus 로고    scopus 로고
    • Molecular dissection of a yeast septin: Distinct domains are required for septin interaction, localization, and function
    • Casamayor, A., and M. Snyder. 2003. Molecular dissection of a yeast septin: distinct domains are required for septin interaction, localization, and function. Mol. Cell. Biol. 23:2762-2777.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 2762-2777
    • Casamayor, A.1    Snyder, M.2
  • 13
    • 0023905661 scopus 로고
    • The establishment of polarity by hippocampal neurons in culture
    • Dotti, C. G., C. A. Sullivan, and G. A. Banker. 1988. The establishment of polarity by hippocampal neurons in culture. J. Neurosci. 8:1454-1468.
    • (1988) J. Neurosci , vol.8 , pp. 1454-1468
    • Dotti, C.G.1    Sullivan, C.A.2    Banker, G.A.3
  • 14
    • 0028820410 scopus 로고
    • Localization and possible functions of Drosophila septins
    • Fares, H., M. Peifer, and J. R. Pringle. 1995. Localization and possible functions of Drosophila septins. Mol. Biol. Cell 6:1843-1859.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1843-1859
    • Fares, H.1    Peifer, M.2    Pringle, J.R.3
  • 15
    • 26844470092 scopus 로고    scopus 로고
    • Nucleotide binding and filament assembly of recombinant yeast septin complexes
    • Farkasovsky, M., P. Herter, B. Voss, and A. Wittinghofer. 2005. Nucleotide binding and filament assembly of recombinant yeast septin complexes. Biol. Chem. 386:643-656.
    • (2005) Biol. Chem , vol.386 , pp. 643-656
    • Farkasovsky, M.1    Herter, P.2    Voss, B.3    Wittinghofer, A.4
  • 16
    • 17644362990 scopus 로고    scopus 로고
    • Developmental transformation of the release modality at the calyx of Held synapse
    • Fedchyshyn, M. J., and L. Y. Wang. 2005. Developmental transformation of the release modality at the calyx of Held synapse. J. Neurosci. 25:4131-4140.
    • (2005) J. Neurosci , vol.25 , pp. 4131-4140
    • Fedchyshyn, M.J.1    Wang, L.Y.2
  • 18
    • 0028070807 scopus 로고
    • Direct patch recording from identified presynaptic terminals mediating glutamatergic EPSCs in the rat CNS, in vitro
    • Forsythe, I. D. 1994. Direct patch recording from identified presynaptic terminals mediating glutamatergic EPSCs in the rat CNS, in vitro. J. Physiol. 479:381-387.
    • (1994) J. Physiol , vol.479 , pp. 381-387
    • Forsythe, I.D.1
  • 19
    • 14444286600 scopus 로고    scopus 로고
    • Polymerization of purified yeast septins: Evidence that organized filament arrays may not be required for septin function
    • Frazier, J. A., M. L. Wong, M. S. Longtine, J. R. Pringle, M. Mann, T. J. Mitchison, and C. Field. 1998. Polymerization of purified yeast septins: evidence that organized filament arrays may not be required for septin function. J. Cell Biol. 143:737-749.
    • (1998) J. Cell Biol , vol.143 , pp. 737-749
    • Frazier, J.A.1    Wong, M.L.2    Longtine, M.S.3    Pringle, J.R.4    Mann, M.5    Mitchison, T.J.6    Field, C.7
  • 20
    • 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., H. Kiyonari, J. Kurisu, T. Hirano, and M. Kengaku. 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
  • 21
    • 21344446835 scopus 로고    scopus 로고
    • Expression profiling the human septin gene family
    • Hall, P. A., K. Jung, K. J. Hillan, and S. E. Russell. 2005. Expression profiling the human septin gene family. J. Pathol. 206:269-278.
    • (2005) J. Pathol , vol.206 , pp. 269-278
    • Hall, P.A.1    Jung, K.2    Hillan, K.J.3    Russell, S.E.4
  • 22
    • 0035511278 scopus 로고    scopus 로고
    • Limited numbers of recycling vesicles in small CNS nerve terminals: Implications for neural signaling and vesicular cycling
    • Harata, N., J. L. Pyle, A. M. Aravanis, M. Mozhayeva, E. T. Kavalali, and R. W. Tsien. 2001. Limited numbers of recycling vesicles in small CNS nerve terminals: implications for neural signaling and vesicular cycling. Trends Neurosci. 24:637-643.
    • (2001) Trends Neurosci , vol.24 , pp. 637-643
    • Harata, N.1    Pyle, J.L.2    Aravanis, A.M.3    Mozhayeva, M.4    Kavalali, E.T.5    Tsien, R.W.6
  • 23
    • 0015193588 scopus 로고
    • Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis
    • Hartwell, L. H. 1971. Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis. Exp. Cell Res. 69:265-276.
    • (1971) Exp. Cell Res , vol.69 , pp. 265-276
    • Hartwell, L.H.1
  • 24
    • 0032103420 scopus 로고    scopus 로고
    • Subunit composition, protein interactions, and structures of the mammalian brain Sec6/8 complex and septin filaments
    • Hsu, S. C., C. D. Hazuka, R. Roth, D. L. Foletti, J. Heuser, and R. H. Scheller. 1998. Subunit composition, protein interactions, and structures 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
  • 28
    • 0032101896 scopus 로고    scopus 로고
    • Developmental changes in calcium channel types mediating synaptic transmission in rat auditory brainstem
    • Iwasaki, S., and T. Takahashi. 1998. Developmental changes in calcium channel types mediating synaptic transmission in rat auditory brainstem. J. Physiol. 509:419-423.
    • (1998) J. Physiol , vol.509 , pp. 419-423
    • Iwasaki, S.1    Takahashi, T.2
  • 30
    • 21844456266 scopus 로고    scopus 로고
    • Septins: Traffic control at the cytokinesis intersection
    • Joo, E., C. W. Tsang, and W. S. Trimble. 2005. Septins: traffic control at the cytokinesis intersection. Traffic 6:626-634.
    • (2005) Traffic , vol.6 , pp. 626-634
    • Joo, E.1    Tsang, C.W.2    Trimble, W.S.3
  • 32
    • 0034639356 scopus 로고    scopus 로고
    • Differential localization of septins in the mouse brain
    • Kinoshita, A., M. Noda, and M. Kinoshita. 2000. Differential localization of septins in the mouse brain. J. Comp. Neurol. 428:223-239.
    • (2000) J. Comp. Neurol , vol.428 , pp. 223-239
    • Kinoshita, A.1    Noda, M.2    Kinoshita, M.3
  • 33
    • 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
  • 35
    • 0030943556 scopus 로고    scopus 로고
    • Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures
    • Kinoshita, M., S. Kumar, A. Mizoguchi, C. Ide, A. Kinoshita, T. Haraguchi, Y. Hiraoka, and M. Noda. 1997. Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures. Genes Dev. 11:1535-1547.
    • (1997) Genes Dev , vol.11 , 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
  • 37
    • 0032490945 scopus 로고    scopus 로고
    • Kinetics and regulation of fast endocytosis at hippocampal synapses
    • Klingauf, J., E. T. Kavalali, and R. W. Tsien. 1998. Kinetics and regulation of fast endocytosis at hippocampal synapses. Nature 394:581-585.
    • (1998) Nature , vol.394 , pp. 581-585
    • Klingauf, J.1    Kavalali, E.T.2    Tsien, R.W.3
  • 39
    • 33646803455 scopus 로고    scopus 로고
    • Platelet septin complexes form rings and associate with the microtubular network
    • Martinez, C., J. Corral, J. A. Dent., L. Sesma, V. Vicente, and J. Ware. 2006. Platelet septin complexes form rings and associate with the microtubular network. J. Thromb. Haemost. 4:1388-1395.
    • (2006) J. Thromb. Haemost , vol.4 , pp. 1388-1395
    • Martinez, C.1    Corral, J.2    Dent, J.A.3    Sesma, L.4    Vicente, V.5    Ware, J.6
  • 40
    • 4744365805 scopus 로고    scopus 로고
    • Human septin-septin interactions as a prerequisite for targeting septin complexes in the cytosol
    • Martinez, C., M. A. Sanjuan, J. A. Dent, L. Karlsson, and J. Ware. 2004. Human septin-septin interactions as a prerequisite for targeting septin complexes in the cytosol. Biochem. J. 382:783-791.
    • (2004) Biochem. J , vol.382 , pp. 783-791
    • Martinez, C.1    Sanjuan, M.A.2    Dent, J.A.3    Karlsson, L.4    Ware, J.5
  • 41
    • 10044294813 scopus 로고    scopus 로고
    • Mammalian septin function in hemostasis and beyond
    • Martinez, C., and J. Ware. 2004. Mammalian septin function in hemostasis and beyond. Exp. Biol. Med. 229:1111-1119.
    • (2004) Exp. Biol. Med , vol.229 , pp. 1111-1119
    • Martinez, C.1    Ware, J.2
  • 42
    • 0037195256 scopus 로고    scopus 로고
    • GTP binding induces filament assembly of a recombinant septin
    • Mendoza, M., A. A. Hyman, and M. Glotzer. 2002. GTP binding induces filament assembly of a recombinant septin. Curr. Biol. 12:1858-1863.
    • (2002) Curr. Biol , vol.12 , pp. 1858-1863
    • Mendoza, M.1    Hyman, A.A.2    Glotzer, M.3
  • 43
    • 11244292287 scopus 로고    scopus 로고
    • Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11
    • Nagata, K., T. Asano, Y. Nozawa, and M. Inagaki. 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.1    Asano, T.2    Nozawa, Y.3    Inagaki, M.4
  • 44
    • 0032008553 scopus 로고    scopus 로고
    • Vesicle pools and Ca2 microdomains: New tools for understanding their roles in neurotransmitter release
    • Neher, E. 1998. Vesicle pools and Ca2 microdomains: new tools for understanding their roles in neurotransmitter release. Neuron 20:389-399.
    • (1998) Neuron , vol.20 , pp. 389-399
    • Neher, E.1
  • 46
    • 34547121710 scopus 로고    scopus 로고
    • Analysis of septins across kingdoms reveals orthology and new motifs
    • Pan, F., R. L. Malmberg, and M. Momany. 2007. Analysis of septins across kingdoms reveals orthology and new motifs. BMC Evol. Biol. 7:103.
    • (2007) BMC Evol. Biol , vol.7 , pp. 103
    • Pan, F.1    Malmberg, R.L.2    Momany, M.3
  • 47
    • 0036132908 scopus 로고    scopus 로고
    • The septin CDCrel-1 is dispensable for normal development and neurotransmitter release
    • Peng, X. R., Z. Jia, Y. Zhang, J. Ware, and W. S. Trimble. 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    Zhang, Y.3    Ware, J.4    Trimble, W.S.5
  • 51
    • 0035863051 scopus 로고    scopus 로고
    • Quantitative relationship between transmitter release and calcium current at the calyx of Held synapse
    • Sakaba, T., and E. Neher. 2001. Quantitative relationship between transmitter release and calcium current at the calyx of Held synapse. J. Neurosci. 21:462-476.
    • (2001) J. Neurosci , vol.21 , pp. 462-476
    • Sakaba, T.1    Neher, E.2
  • 52
    • 0025048136 scopus 로고
    • The P-loop-a common motif in ATP- and GTP-binding proteins
    • Saraste, M., P. R. Sibbald, and A. Wittinghofer. 1990. The P-loop-a common motif in ATP- and GTP-binding proteins. Trends Biochem. Sci. 15:430-434.
    • (1990) Trends Biochem. Sci , vol.15 , pp. 430-434
    • Saraste, M.1    Sibbald, P.R.2    Wittinghofer, A.3
  • 53
    • 0033152473 scopus 로고    scopus 로고
    • Released fraction and total size of a pool of immediately available transmitter quanta at a calyx synapse
    • Schneggenburger, R., A. C. Meyer, and E. Neher. 1999. Released fraction and total size of a pool of immediately available transmitter quanta at a calyx synapse. Neuron 23:399-409.
    • (1999) Neuron , vol.23 , pp. 399-409
    • Schneggenburger, R.1    Meyer, A.C.2    Neher, E.3
  • 54
    • 0037474299 scopus 로고    scopus 로고
    • Borg/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments
    • Sheffield, P. J., C. J. Oliver, B. E. Kremer, S. Sheng, Z. Shao, and I. G. Macara. 2003. Borg/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments. J. Biol. Chem. 278:3483- 3488.
    • (2003) J. Biol. Chem , vol.278 , 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
  • 57
    • 31644446955 scopus 로고    scopus 로고
    • Here come the septins: Novel polymers that coordinate intracellular functions and organization
    • Spiliotis, E. T., and W. J. Nelson. 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
  • 59
    • 0028878175 scopus 로고
    • Estimates for the pool size of releasable quanta at a single central synapse and for the time required to refill the pool
    • Stevens, C. F., and T. Tsujimoto. 1995. Estimates for the pool size of releasable quanta at a single central synapse and for the time required to refill the pool. Proc. Natl. Acad. Sci. USA 92:846-849.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 846-849
    • Stevens, C.F.1    Tsujimoto, T.2
  • 60
    • 0036798406 scopus 로고    scopus 로고
    • The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis
    • Surka, M. C., C. W. Tsang, and W. S. Trimble. 2002. The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis. Mol. Biol. Cell 13:3532-3545.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3532-3545
    • Surka, M.C.1    Tsang, C.W.2    Trimble, W.S.3
  • 61
    • 35348834213 scopus 로고    scopus 로고
    • Role of septin cytoskeleton in spine morphogenesis and dendrite development in neurons
    • Tada, T., A. Simonetta, M. Batterton, M. Kinoshita, D. Edbauer, and M. Sheng. 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
  • 62
    • 0345057349 scopus 로고    scopus 로고
    • An anillin homologue, Mid2p, acts during fission yeast cytokinesis to organize the septin ring and promote cell separation
    • Tasto, J. J., J. L. Morrell, and K. L. Gould. 2003. An anillin homologue, Mid2p, acts during fission yeast cytokinesis to organize the septin ring and promote cell separation. J. Cell Biol. 160:1093-1103.
    • (2003) J. Cell Biol , vol.160 , pp. 1093-1103
    • Tasto, J.J.1    Morrell, J.L.2    Gould, K.L.3
  • 63
    • 0025780879 scopus 로고
    • Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene
    • Tybulewicz, V. L., C. E. Crawford, P. K. Jackson, R. T. Bronson, and R. C. Mulligan. 1991. Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene. Cell 65:1153-1163.
    • (1991) Cell , vol.65 , pp. 1153-1163
    • Tybulewicz, V.L.1    Crawford, C.E.2    Jackson, P.K.3    Bronson, R.T.4    Mulligan, R.C.5
  • 64
    • 4644251602 scopus 로고    scopus 로고
    • Protein-protein interactions governing septin heteropentamer assembly and septin filament organization in Saccharomyces cerevisiae
    • Versele, M., B. Gullbrand, M. J. Shulewitz, V. J. Cid, S. Bahmanyar, R. E. Chen, P. Barth, T. Alber, and J. Thorner. 2004. Protein-protein interactions governing septin heteropentamer assembly and septin filament organization in Saccharomyces cerevisiae. Mol. Biol. Cell 15:4568-4583.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4568-4583
    • Versele, M.1    Gullbrand, B.2    Shulewitz, M.J.3    Cid, V.J.4    Bahmanyar, S.5    Chen, R.E.6    Barth, P.7    Alber, T.8    Thorner, J.9
  • 65
    • 23744499989 scopus 로고    scopus 로고
    • Some assembly required: Yeast septins provide the instruction manual
    • Versele, M., and J. Thorner. 2005. Some assembly required: yeast septins provide the instruction manual. Trends Cell Biol. 15:414-424.
    • (2005) Trends Cell Biol , vol.15 , pp. 414-424
    • Versele, M.1    Thorner, J.2
  • 66
    • 0032560828 scopus 로고    scopus 로고
    • High-frequency firing helps replenish the readily releasable pool of synaptic vesicles
    • Wang, L. Y., and L. K. Kaczmarek. 1998. High-frequency firing helps replenish the readily releasable pool of synaptic vesicles. Nature 394:384-388.
    • (1998) Nature , vol.394 , pp. 384-388
    • Wang, L.Y.1    Kaczmarek, L.K.2
  • 67
    • 0032707610 scopus 로고    scopus 로고
    • ++-dependent vesicle pool dynamics and short term synaptic depression
    • ++-dependent vesicle pool dynamics and short term synaptic depression. Biophys. J. 77:2418-2429.
    • (1999) Biophys. J , vol.77 , pp. 2418-2429
    • Weis, S.1    Schneggenburger, R.2    Neher, E.3
  • 68
    • 0033555416 scopus 로고    scopus 로고
    • Calcium channel types with distinct presynaptic localization couple differentially to transmitter release in single calyx-type synapses
    • Wu, L. G., R. E. Westenbroek, J. G. Borst, W. A. Catterall, and B. Sakmann. 1999. Calcium channel types with distinct presynaptic localization couple differentially to transmitter release in single calyx-type synapses. J. Neurosci. 19:726-736.
    • (1999) J. Neurosci , vol.19 , pp. 726-736
    • Wu, L.G.1    Westenbroek, R.E.2    Borst, J.G.3    Catterall, W.A.4    Sakmann, B.5
  • 69
    • 0032911523 scopus 로고    scopus 로고
    • Characterization of the mammalian septin H5: Distinct patterns of cytoskeletal and membrane association from other septin proteins
    • Xie, H., M. Surka, J. Howard, and W. S. Trimble. 1999. Characterization of the mammalian septin H5: distinct patterns of cytoskeletal and membrane association from other septin proteins. Cell Motil. Cytoskeleton 43:52-62.
    • (1999) Cell Motil. Cytoskeleton , vol.43 , pp. 52-62
    • Xie, H.1    Surka, M.2    Howard, J.3    Trimble, W.S.4
  • 70
    • 35348907374 scopus 로고    scopus 로고
    • The GTP-binding protein Septin 7 is critical for dendrite branching and dendritic-spine morphology
    • Xie, Y., J. P. Vessey, A. Konecna, R. Dahm, P. Macchi, and M. A. Kiebler. 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, Y.1    Vessey, J.P.2    Konecna, A.3    Dahm, R.4    Macchi, P.5    Kiebler, M.A.6
  • 71
    • 0032808957 scopus 로고    scopus 로고
    • Retroviral promoter-trap insertion into a novel mammalian septin gene expressed during mouse neuronal development
    • Xiong, J. W., A. Leahy, and H. Stuhlmann. 1999. Retroviral promoter-trap insertion into a novel mammalian septin gene expressed during mouse neuronal development. Mech. Dev. 86:183-191.
    • (1999) Mech. Dev , vol.86 , pp. 183-191
    • Xiong, J.W.1    Leahy, A.2    Stuhlmann, H.3
  • 72
    • 4344573131 scopus 로고    scopus 로고
    • Phosphorylation of septin 3 on Ser-91 by cGMP-dependent protein kinase-I in nerve terminals
    • Xue, J., P. J. Milburn, B. T. Hanna, M. E. Graham, J. A. Rostas, and P. J. Robinson. 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
  • 73
    • 7244262110 scopus 로고    scopus 로고
    • Septin 3 (G-septin) is a developmentally regulated phosphoprotein enriched in presynaptic nerve terminals
    • Xue, J., C. W. Tsang, W. P. Gai, C. S. Malladi, W. S. Trimble, J. A. Rostas, and P. J. Robinson. 2004. Septin 3 (G-septin) is a developmentally regulated phosphoprotein enriched in presynaptic nerve terminals. J. Neurochem. 91: 579-590.
    • (2004) J. Neurochem , vol.91 , 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
  • 75
    • 0032496621 scopus 로고    scopus 로고
    • Structure and expression of the human septin gene HCDCREL-1
    • Yagi, M., B. Zieger, G. J. Roth, and J. Ware. 1998. Structure and expression of the human septin gene HCDCREL-1. Gene 212:229-236.
    • (1998) Gene , vol.212 , pp. 229-236
    • Yagi, M.1    Zieger, B.2    Roth, G.J.3    Ware, J.4
  • 76
    • 33744985276 scopus 로고    scopus 로고
    • Amplitude and kinetics of action potential-evoked Ca2 current and its efficacy in triggering transmitter release at the developing calyx of held synapse
    • Yang, Y. M., and L. Y. Wang. 2006. Amplitude and kinetics of action potential-evoked Ca2 current and its efficacy in triggering transmitter release at the developing calyx of held synapse. J. Neurosci. 26:5698-5708.
    • (2006) J. Neurosci , vol.26 , pp. 5698-5708
    • Yang, Y.M.1    Wang, L.Y.2
  • 77
    • 0033576647 scopus 로고    scopus 로고
    • Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP
    • Zhang, J., C. Kong, H. Xie, P. S. McPherson, S. Grinstein, and W. S. Trimble. 1999. Phosphatidylinositol polyphosphate binding to the mammalian septin H5 is modulated by GTP. Curr. Biol. 9:1458-1467.
    • (1999) Curr. Biol , vol.9 , 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.