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Volumn 24, Issue 5, 2014, Pages 576-594

MARCKS regulates membrane targeting of Rab10 vesicles to promote axon development

Author keywords

axon growth; MARCKS; plasmalemmal precursor vesicles; Rab10

Indexed keywords

ACTIN; MEMBRANE PROTEIN; MYRISTOYLATED ALANINE-RICH C KINASE SUBSTRATE; PROTEIN BINDING; RAB PROTEIN; RAB10 PROTEIN, RAT; SIGNAL PEPTIDE;

EID: 84899923987     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2014.33     Document Type: Article
Times cited : (54)

References (60)
  • 1
    • 0020183576 scopus 로고
    • Calcium/phos-pholipid regulates phosphorylation of a Mr "87k" substrate protein in brain synaptosomes
    • Wu WC, Walaas SI, Nairn AC, Greengard P. Calcium/phos-pholipid regulates phosphorylation of a Mr "87k" substrate protein in brain synaptosomes. Proc Natl Acad Sci USA 1982; 79:5249-5253.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 5249-5253
    • Wu, W.C.1    Walaas, S.I.2    Nairn, A.C.3    Greengard, P.4
  • 2
    • 0037731790 scopus 로고
    • Molecular cloning characterization and expression of a cDNA encoding the "80-to 87-kDa" myristoylated alanine-rich C kinase substrate: A major cellular substrate for protein kinase C
    • Stumpo DJ, Graff JM, Albert KA, Greengard P, Blackshear PJ. Molecular cloning, characterization, and expression of a cDNA encoding the "80-to 87-kDa" myristoylated alanine-rich C kinase substrate: a major cellular substrate for protein kinase C. Proc Natl Acad Sci USA 1989; 86:4012-4016.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 4012-4016
    • Stumpo, D.J.1    Graff, J.M.2    Albert, K.A.3    Greengard, P.4    Blackshear, P.J.5
  • 3
    • 0025096430 scopus 로고
    • Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage flopodia
    • Rosen A, Keenan KF, Thelen M, Nairn AC, Aderem A. Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage flopodia. J Exp Med 1990; 172:1211-1215.
    • (1990) J Exp Med , vol.172 , pp. 1211-1215
    • Rosen, A.1    Keenan, K.F.2    Thelen, M.3    Nairn, A.C.4    Aderem, A.5
  • 4
    • 0026448867 scopus 로고
    • Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein appears to involve myristate-dependent binding in the absence of a myristoyl protein receptor
    • George DJ, Blackshear PJ. Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein appears to involve myristate-dependent binding in the absence of a myristoyl protein receptor. J Biol Chem 1992; 267:24879-24885.
    • (1992) J Biol Chem , vol.267 , pp. 24879-24885
    • George, D.J.1    Blackshear, P.J.2
  • 5
    • 0029053995 scopus 로고
    • Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein. Mutational analysis provides evidence for complex interactions
    • Swierczynski SL, Blackshear PJ. Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein. Mutational analysis provides evidence for complex interactions. J Biol Chem 1995; 270:13436-13445.
    • (1995) J Biol Chem , vol.270 , pp. 13436-13445
    • Swierczynski, S.L.1    Blackshear, P.J.2
  • 6
    • 0028909477 scopus 로고
    • Protein kinase C regulates MARCKS cycling between the plasma membrane and lysosomes in f-broblasts
    • Allen LA, Aderem A. Protein kinase C regulates MARCKS cycling between the plasma membrane and lysosomes in f-broblasts. EMBO J 1995; 14:1109-1121.
    • (1995) EMBO J , vol.14 , pp. 1109-1121
    • Allen, L.A.1    Aderem, A.2
  • 7
    • 0026513601 scopus 로고
    • MARCKS is an actin flament crosslinking protein regulated by protein kinase C and calcium-calmodulin
    • Hartwig JH, Thelen M, Rosen A, Janmey PA, Nairn AC, Aderem A. MARCKS is an actin flament crosslinking protein regulated by protein kinase C and calcium-calmodulin. Nature 1992; 356:618-622.
    • (1992) Nature , vol.356 , pp. 618-622
    • Hartwig, J.H.1    Thelen, M.2    Rosen, A.3    Janmey, P.A.4    Nairn, A.C.5    Aderem, A.6
  • 8
    • 0034717707 scopus 로고    scopus 로고
    • GAP43, MARCKS, and CAP23 modulate PI(4, 5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism
    • Laux T, Fukami K, Thelen M, Golub T, Frey D, Caroni P. GAP43, MARCKS, and CAP23 modulate PI(4, 5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism. J Cell Biol 2000; 149:1455-1472.
    • (2000) J Cell Biol , vol.149 , pp. 1455-1472
    • Laux, T.1    Fukami, K.2    Thelen, M.3    Golub, T.4    Frey, D.5    Caroni, P.6
  • 9
    • 0001704947 scopus 로고    scopus 로고
    • MARCKS regulates membrane ruffing and cell spreading
    • Myat MM, Anderson S, Allen LA, Aderem A. MARCKS regulates membrane ruffing and cell spreading. Curr Biol 1997; 7:611-614.
    • (1997) Curr Biol , vol.7 , pp. 611-614
    • Myat, M.M.1    Anderson, S.2    Allen, L.A.3    Aderem, A.4
  • 10
    • 0020957891 scopus 로고
    • Regional distribution of calcium-and cyclic adenosine 3′:5′-monophosphate-regulated protein phosphorylation systems in mammalian brain. II. Soluble systems
    • Walaas SI, Nairn AC, Greengard P. Regional distribution of calcium-and cyclic adenosine 3′:5′-monophosphate-regulated protein phosphorylation systems in mammalian brain. II. Soluble systems. J Neurosci 1983; 3:302-311.
    • (1983) J Neurosci , vol.3 , pp. 302-311
    • Walaas, S.I.1    Nairn, A.C.2    Greengard, P.3
  • 11
    • 1242266547 scopus 로고
    • Widespread occurrence of "87 kDa, " a major specifc substrate for protein kinase C
    • Albert KA, Walaas SI, Wang JK, Greengard P. Widespread occurrence of "87 kDa, " a major specifc substrate for protein kinase C. Proc Natl Acad Sci USA 1986; 83:2822-2826.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 2822-2826
    • Albert, K.A.1    Walaas, S.I.2    Wang, J.K.3    Greengard, P.4
  • 12
    • 0025423954 scopus 로고
    • Localization of the MARCKS (87 kDa) protein, a major spe-cifc substrate for protein kinase C, in rat brain
    • Ouimet CC, Wang JK, Walaas SI, Albert KA, Greengard P. Localization of the MARCKS (87 kDa) protein, a major spe-cifc substrate for protein kinase C, in rat brain. J Neurosci 1990; 10:1683-1698.
    • (1990) J Neurosci , vol.10 , pp. 1683-1698
    • Ouimet, C.C.1    Wang, J.K.2    Walaas, S.I.3    Albert, K.A.4    Greengard, P.5
  • 13
    • 0022648419 scopus 로고
    • Protein kinase C-stimulated phosphorylation in vitro of a Mr 80, 000 protein phosphorylated in response to phorbol esters and growth factors in intact fibroblasts. Distinction from protein kinase C and prominence in brain
    • Blackshear PJ, Wen L, Glynn BP, Witters LA. Protein kinase C-stimulated phosphorylation in vitro of a Mr 80, 000 protein phosphorylated in response to phorbol esters and growth factors in intact fibroblasts. Distinction from protein kinase C and prominence in brain. J Biol Chem 1986; 261:1459-1469.
    • (1986) J Biol Chem , vol.261 , pp. 1459-1469
    • Blackshear, P.J.1    Wen, L.2    Glynn, B.P.3    Witters, L.A.4
  • 14
    • 0028883213 scopus 로고
    • MARCKS defciency in mice leads to abnormal brain development and perinatal death
    • Stumpo DJ, Bock CB, Tuttle JS, Blackshear PJ. MARCKS defciency in mice leads to abnormal brain development and perinatal death. Proc Natl Acad Sci USA 1995; 92:944-948.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 944-948
    • Stumpo, D.J.1    Bock, C.B.2    Tuttle, J.S.3    Blackshear, P.J.4
  • 15
    • 25644436461 scopus 로고    scopus 로고
    • Essential role for the PKC target MARCKS in maintaining dendritic spine morphology
    • Calabrese B, Halpain S. Essential role for the PKC target MARCKS in maintaining dendritic spine morphology. Neuron 2005; 48:77-90.
    • (2005) Neuron , vol.48 , pp. 77-90
    • Calabrese, B.1    Halpain, S.2
  • 16
    • 33750528518 scopus 로고    scopus 로고
    • Unphosphorylated MARCKS is involved in neurite initiation induced by insulinlike growth factor-I in SH-SY5Y cells
    • Shiraishi M, Tanabe A, Saito N, Sasaki Y. Unphosphorylated MARCKS is involved in neurite initiation induced by insulinlike growth factor-I in SH-SY5Y cells. J Cell Physiol 2006; 209:1029-1038.
    • (2006) J Cell Physiol , vol.209 , pp. 1029-1038
    • Shiraishi, M.1    Tanabe, A.2    Saito, N.3    Sasaki, Y.4
  • 17
    • 58149300222 scopus 로고    scopus 로고
    • Actin filament assembly by myristoylated alanine-rich C kinase substrate-phosphati-dylinositol-4, 5-diphosphate signaling is critical for dendrite branching
    • Li H, Chen G, Zhou B, Duan S. Actin filament assembly by myristoylated alanine-rich C kinase substrate-phosphati-dylinositol-4, 5-diphosphate signaling is critical for dendrite branching. Mol Biol Cell 2008; 19:4804-4813.
    • (2008) Mol Biol Cell , vol.19 , pp. 4804-4813
    • Li, H.1    Chen, G.2    Zhou, B.3    Duan, S.4
  • 18
    • 33845430955 scopus 로고    scopus 로고
    • Myristoylated, alanine-rich C-kinase substrate phosphoryla-tion regulates growth cone adhesion and pathfnding
    • Gatlin JC, Estrada-Bernal A, Sanford SD, Pfenninger KH. Myristoylated, alanine-rich C-kinase substrate phosphoryla-tion regulates growth cone adhesion and pathfnding. Mol Biol Cell 2006; 17:5115-5130.
    • (2006) Mol Biol Cell , vol.17 , pp. 5115-5130
    • Gatlin, J.C.1    Estrada-Bernal, A.2    Sanford, S.D.3    Pfenninger, K.H.4
  • 19
    • 69049095023 scopus 로고    scopus 로고
    • MARCKS modulates radial progenitor placement, proliferation and organization in the developing cerebral cortex
    • Weimer JM, Yokota Y, Stanco A, Stumpo DJ, Blackshear PJ, Anton ES. MARCKS modulates radial progenitor placement, proliferation and organization in the developing cerebral cortex. Development 2009; 136:2965-2975.
    • (2009) Development , vol.136 , pp. 2965-2975
    • Weimer, J.M.1    Yokota, Y.2    Stanco, A.3    Stumpo, D.J.4    Blackshear, P.J.5    Anton, E.S.6
  • 20
    • 84866276473 scopus 로고    scopus 로고
    • C-Jun N-termi-nal kinase phosphorylation of MARCKSL1 determines actin stability and migration in neurons and in cancer cells
    • Bjorkblom B, Padzik A, Mohammad H, et al. c-Jun N-termi-nal kinase phosphorylation of MARCKSL1 determines actin stability and migration in neurons and in cancer cells. Mol Cell Biol 2012; 32:3513-3526.
    • (2012) Mol Cell Biol , vol.32 , pp. 3513-3526
    • Bjorkblom, B.1    Padzik, A.2    Mohammad, H.3
  • 21
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffc
    • Stenmark H. Rab GTPases as coordinators of vesicle traffc. Nat Rev Mol Cell Biol 2009; 10:513-525.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 22
    • 29944443664 scopus 로고    scopus 로고
    • The yeast lgl family member Sro7p is an effector of the secretory Rab GT-Pase Sec4p
    • Grosshans BL, Andreeva A, Gangar A, et al. The yeast lgl family member Sro7p is an effector of the secretory Rab GT-Pase Sec4p. J Cell Biol 2006; 172:55-66.
    • (2006) J Cell Biol , vol.172 , pp. 55-66
    • Grosshans, B.L.1    Andreeva, A.2    Gangar, A.3
  • 23
    • 0029123064 scopus 로고
    • Use of antisense oligonucle-otides to study Rab function in vivo
    • Huber LA, Dupree P, Dotti CG. Use of antisense oligonucle-otides to study Rab function in vivo. Methods Enzymol 1995; 257:302-312.
    • (1995) Methods Enzymol , vol.257 , pp. 302-312
    • Huber, L.A.1    Dupree, P.2    Dotti, C.G.3
  • 24
    • 80052773707 scopus 로고    scopus 로고
    • Lgl1 activation of Rab10 promotes axonal membrane traffcking underlying neuronal polarization
    • Wang T, Liu Y, Xu XH, et al. Lgl1 activation of Rab10 promotes axonal membrane traffcking underlying neuronal polarization. Dev Cell 2011; 21:431-444.
    • (2011) Dev Cell , vol.21 , pp. 431-444
    • Wang, T.1    Liu, Y.2    Xu, X.H.3
  • 25
    • 33947578085 scopus 로고    scopus 로고
    • Rab10, a target of the AS160 Rab GAP, is required for insulin-stimulated translocation of GLUT4 to the adipocyte plasma membrane
    • Sano H, Eguez L, Teruel MN, et al. Rab10, a target of the AS160 Rab GAP, is required for insulin-stimulated translocation of GLUT4 to the adipocyte plasma membrane. Cell Me-tab 2007; 5:293-303.
    • (2007) Cell Me-tab , vol.5 , pp. 293-303
    • Sano, H.1    Eguez, L.2    Teruel, M.N.3
  • 26
    • 59449108592 scopus 로고    scopus 로고
    • Alternative splicing in class v myosins determines association with Rab10
    • Roland JT, Lapierre LA, Goldenring JR. Alternative splicing in class V myosins determines association with Rab10. J Biol Chem 2009; 284:1213-1223.
    • (2009) J Biol Chem , vol.284 , pp. 1213-1223
    • Roland, J.T.1    Lapierre, L.A.2    Goldenring, J.R.3
  • 27
    • 84879658602 scopus 로고    scopus 로고
    • Myosin Vb controls biogenesis of post-Golgi Rab10 carriers during axon development
    • Liu Y, Xu XH, Chen Q, et al. Myosin Vb controls biogenesis of post-Golgi Rab10 carriers during axon development. Nat Commun 2013; 4:2005.
    • (2013) Nat Commun , vol.4 , pp. 2005
    • Liu, Y.1    Xu, X.H.2    Chen, Q.3
  • 28
    • 0026352185 scopus 로고
    • Protein kinase C substrate and inhibitor characteristics of peptides derived from the myristoylated alanine-rich C kinase substrate (MARCKS) protein phosphorylation site domain
    • Graff JM, Rajan RR, Randall RR, Nairn AC, Blackshear PJ. Protein kinase C substrate and inhibitor characteristics of peptides derived from the myristoylated alanine-rich C kinase substrate (MARCKS) protein phosphorylation site domain. J Biol Chem 1991; 266:14390-14398.
    • (1991) J Biol Chem , vol.266 , pp. 14390-14398
    • Graff, J.M.1    Rajan, R.R.2    Randall, R.R.3    Nairn, A.C.4    Blackshear, P.J.5
  • 30
    • 0027379143 scopus 로고
    • Oka-daic acid-sensitive protein phosphatases dephosphorylate MARCKS, a major protein kinase C substrate
    • Clarke PR, Siddhanti SR, Cohen P, Blackshear PJ. Oka-daic acid-sensitive protein phosphatases dephosphorylate MARCKS, a major protein kinase C substrate. FEBS Lett 1993; 336:37-42.
    • (1993) FEBS Lett , vol.336 , pp. 37-42
    • Clarke, P.R.1    Siddhanti, S.R.2    Cohen, P.3    Blackshear, P.J.4
  • 32
    • 0030579208 scopus 로고    scopus 로고
    • Nonmyristoylated MARCKS complements some but not all of the developmental defects associated with MARCKS def-ciency in mice
    • Swierczynski SL, Siddhanti SR, Tuttle JS, Blackshear PJ. Nonmyristoylated MARCKS complements some but not all of the developmental defects associated with MARCKS def-ciency in mice. Dev Biol 1996; 179:135-147.
    • (1996) Dev Biol , vol.179 , pp. 135-147
    • Swierczynski, S.L.1    Siddhanti, S.R.2    Tuttle, J.S.3    Blackshear, P.J.4
  • 33
    • 0035943628 scopus 로고    scopus 로고
    • Overexpression of the myristoylated alanine-rich C-kinase substrate inhibits cell adhesion to extracellular matrix components
    • Spizz G, Blackshear PJ. Overexpression of the myristoylated alanine-rich C-kinase substrate inhibits cell adhesion to extracellular matrix components. J Biol Chem 2001; 276:32264-32273.
    • (2001) J Biol Chem , vol.276 , pp. 32264-32273
    • Spizz, G.1    Blackshear, P.J.2
  • 34
    • 84864025889 scopus 로고    scopus 로고
    • A molecular network for the transport of the TI-VAMP/VAMP7 vesicles from cell center to periphery
    • Burgo A, Proux-Gillardeaux V, Sotirakis E, et al. A molecular network for the transport of the TI-VAMP/VAMP7 vesicles from cell center to periphery. Dev Cell 2012; 23:166-180.
    • (2012) Dev Cell , vol.23 , pp. 166-180
    • Burgo, A.1    Proux-Gillardeaux, V.2    Sotirakis, E.3
  • 35
    • 62849088750 scopus 로고    scopus 로고
    • Plasma membrane expansion: A neuron's Herculean task
    • Pfenninger KH. Plasma membrane expansion: a neuron's Herculean task. Nat Rev Neurosci 2009; 10:251-261.
    • (2009) Nat Rev Neurosci , vol.10 , pp. 251-261
    • Pfenninger, K.H.1
  • 36
    • 38849086625 scopus 로고    scopus 로고
    • The JIP1 scaffold protein regulates axonal development in cortical neurons
    • Dajas-Bailador F, Jones E V, Whitmarsh AJ. The JIP1 scaffold protein regulates axonal development in cortical neurons. Curr Biol 2008; 18:221-226.
    • (2008) Curr Biol , vol.18 , pp. 221-226
    • Dajas-Bailador, F.1    Jones, E.V.2    Whitmarsh, A.J.3
  • 37
    • 33750728621 scopus 로고    scopus 로고
    • Protrudin induces neurite formation by directional membrane trafficking
    • Shirane M, Nakayama KI. Protrudin induces neurite formation by directional membrane trafficking. Science 2006; 314:818-821.
    • (2006) Science , vol.314 , pp. 818-821
    • Shirane, M.1    Nakayama, K.I.2
  • 38
    • 0025744372 scopus 로고
    • A novel fuorescent ceramide analogue for studying membrane traffc in animal cells: Accumulation at the Golgi apparatus results in altered spectral properties of the sphingolipid precursor
    • Pagano RE, Martin OC, Kang HC, Haugland RP. A novel fuorescent ceramide analogue for studying membrane traffc in animal cells: accumulation at the Golgi apparatus results in altered spectral properties of the sphingolipid precursor. J Cell Biol 1991; 11 3:1267-1279.
    • (1991) J Cell Biol , vol.11 , Issue.3 , pp. 1267-1279
    • Pagano, R.E.1    Martin, O.C.2    Kang, H.C.3    Haugland, R.P.4
  • 39
    • 33847134439 scopus 로고    scopus 로고
    • Neuronal polarity: From extracellular signals to intracellular mechanisms
    • Arimura N, Kaibuchi K. Neuronal polarity: from extracellular signals to intracellular mechanisms. Nat Rev Neurosci 2007; 8:194-205.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 194-205
    • Arimura, N.1    Kaibuchi, K.2
  • 40
    • 0033583284 scopus 로고    scopus 로고
    • The role of local actin instability in axon formation
    • Bradke F, Dotti CG. The role of local actin instability in axon formation. Science 1999; 283:1931-1934.
    • (1999) Science , vol.283 , pp. 1931-1934
    • Bradke, F.1    Dotti, C.G.2
  • 41
    • 0026513601 scopus 로고
    • Marcks is an actin flament cross-linking protein regulated by protein-kinase-c and calcium calmodulin
    • Hartwig JH, Thelen M, Rosen A, Janmey PA, Nairn AC, Aderem A. Marcks is an actin flament cross-linking protein regulated by protein-kinase-c and calcium calmodulin. Nature 1992; 356:618-622.
    • (1992) Nature , vol.356 , pp. 618-622
    • Hartwig, J.H.1    Thelen, M.2    Rosen, A.3    Janmey, P.A.4    Nairn, A.C.5    Aderem, A.6
  • 42
    • 0034717707 scopus 로고    scopus 로고
    • GAP43, MARCKS, and CAP23 modulate PI(4, 5)P-2 at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism
    • Laux T, Fukami K, Thelen M, Golub T, Frey D, Caroni P. GAP43, MARCKS, and CAP23 modulate PI(4, 5)P-2 at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism. J Cell Biol 2000; 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
  • 43
    • 33747589931 scopus 로고    scopus 로고
    • IGF-1 receptor is essential for the establishment of hippocampal neuronal polarity
    • Sosa L, Dupraz S, Laurino L, et al. IGF-1 receptor is essential for the establishment of hippocampal neuronal polarity. Nat Neurosci 2006; 9:993-995.
    • (2006) Nat Neurosci , vol.9 , pp. 993-995
    • Sosa, L.1    Dupraz, S.2    Laurino, L.3
  • 44
    • 34247478454 scopus 로고    scopus 로고
    • LKB1/STRAD promotes axon initiation during neuronal polarization
    • Shelly M, Cancedda L, Heilshorn S, Sumbre G, Poo MM. LKB1/STRAD promotes axon initiation during neuronal polarization. Cell 2007; 129:565-577.
    • (2007) Cell , vol.129 , pp. 565-577
    • Shelly, M.1    Cancedda, L.2    Heilshorn, S.3    Sumbre, G.4    Poo, M.M.5
  • 45
    • 55049087015 scopus 로고    scopus 로고
    • The regulated exocytosis of enlargeosomes is mediated by a SNARE machinery that includes VAMP4
    • Cocucci E, Racchetti G, Rupnik M, Meldolesi J. The regulated exocytosis of enlargeosomes is mediated by a SNARE machinery that includes VAMP4. J Cell Sci 2008; 121:2983-2991.
    • (2008) J Cell Sci , vol.121 , pp. 2983-2991
    • Cocucci, E.1    Racchetti, G.2    Rupnik, M.3    Meldolesi, J.4
  • 46
    • 0033571899 scopus 로고    scopus 로고
    • Subcellular localization of tetanus neurotoxin-insensitive vesicle-associated membrane protein (VAMP)/VAMP7 in neuronal cells: Evidence for a novel membrane compartment
    • Coco S, Raposo G, Martinez S, et al. Subcellular localization of tetanus neurotoxin-insensitive vesicle-associated membrane protein (VAMP)/VAMP7 in neuronal cells: evidence for a novel membrane compartment. J Neurosci 1999; 19:9803-9812.
    • (1999) J Neurosci , vol.19 , pp. 9803-9812
    • Coco, S.1    Raposo, G.2    Martinez, S.3
  • 47
    • 0035371405 scopus 로고    scopus 로고
    • A common exo-cytotic mechanism mediates axonal and dendritic outgrowth
    • Martinez-Arca S, Coco S, Mainguy G, et al. A common exo-cytotic mechanism mediates axonal and dendritic outgrowth. J Neurosci 2001; 21:3830-3838.
    • (2001) J Neurosci , vol.21 , pp. 3830-3838
    • Martinez-Arca, S.1    Coco, S.2    Mainguy, G.3
  • 48
    • 0034657922 scopus 로고    scopus 로고
    • Role of tetanus neurotoxin insensitive vesicle-associated membrane protein (TI-VAMP) in vesicular transport mediating neurite outgrowth
    • Martinez-Arca S, Alberts P, Zahraoui A, Louvard D, Galli T. Role of tetanus neurotoxin insensitive vesicle-associated membrane protein (TI-VAMP) in vesicular transport mediating neurite outgrowth. J Cell Biol 2000; 149:889-900.
    • (2000) J Cell Biol , vol.149 , pp. 889-900
    • Martinez-Arca, S.1    Alberts, P.2    Zahraoui, A.3    Louvard, D.4    Galli, T.5
  • 49
    • 77952928699 scopus 로고    scopus 로고
    • Integrin signaling switches the cy-toskeletal and exocytic machinery that drives neuritogenesis
    • Gupton SL, Gertler FB. Integrin signaling switches the cy-toskeletal and exocytic machinery that drives neuritogenesis. Dev Cell 2010; 18:725-736.
    • (2010) Dev Cell , vol.18 , pp. 725-736
    • Gupton, S.L.1    Gertler, F.B.2
  • 50
    • 0029949638 scopus 로고    scopus 로고
    • Growth cone collapse and inhibition of neurite growth by Botulinum neurotoxin C1: A t-SNARE is involved in axonal growth
    • Igarashi M, Kozaki S, Terakawa S, Kawano S, Ide C, Komiya Y. Growth cone collapse and inhibition of neurite growth by Botulinum neurotoxin C1: a t-SNARE is involved in axonal growth. J Cell Biol 1996; 134:205-215.
    • (1996) J Cell Biol , vol.134 , pp. 205-215
    • Igarashi, M.1    Kozaki, S.2    Terakawa, S.3    Kawano, S.4    Ide, C.5    Komiya, Y.6
  • 51
    • 0029917555 scopus 로고    scopus 로고
    • Common and distinct fusion proteins in axonal growth and transmitter release
    • Osen-Sand A, Staple JK, Naldi E, et al. Common and distinct fusion proteins in axonal growth and transmitter release. J Comp Neurol 1996; 367:222-234.
    • (1996) J Comp Neurol , vol.367 , pp. 222-234
    • Osen-Sand, A.1    Staple, J.K.2    Naldi, E.3
  • 52
    • 33645746320 scopus 로고    scopus 로고
    • Omega-3 and omega-6 fatty acids stimulate cell membrane expansion by acting on syntaxin 3
    • Darios F, Davletov B. Omega-3 and omega-6 fatty acids stimulate cell membrane expansion by acting on syntaxin 3. Nature 2006; 440:813-817.
    • (2006) Nature , vol.440 , pp. 813-817
    • Darios, F.1    Davletov, B.2
  • 53
    • 70350324643 scopus 로고    scopus 로고
    • The TC10-Exo70 complex is essential for membrane expansion and axonal speci-fcation in developing neurons
    • Dupraz S, Grassi D, Bernis ME, et al. The TC10-Exo70 complex is essential for membrane expansion and axonal speci-fcation in developing neurons. J Neurosci 2009; 29:13292-13301.
    • (2009) J Neurosci , vol.29 , pp. 13292-13301
    • Dupraz, S.1    Grassi, D.2    Bernis, M.E.3
  • 54
    • 67649963291 scopus 로고    scopus 로고
    • RalA and the exocyst complex infuence neuronal polarity through PAR-3 and aPKC
    • Lalli G. RalA and the exocyst complex infuence neuronal polarity through PAR-3 and aPKC. J Cell Sci 2009; 122:1499-1506.
    • (2009) J Cell Sci , vol.122 , pp. 1499-1506
    • Lalli, G.1
  • 55
    • 84873358822 scopus 로고    scopus 로고
    • Rab10 GTPase regulates ER dynamics and morphology
    • English AR, Voeltz GK. Rab10 GTPase regulates ER dynamics and morphology. Nat Cell Biol 2013; 15:169-178.
    • (2013) Nat Cell Biol , vol.15 , pp. 169-178
    • English, A.R.1    Voeltz, G.K.2
  • 56
    • 84893086471 scopus 로고    scopus 로고
    • JIP1 mediates anterograde transport of Rab10 cargos during neuronal polarization
    • Deng CY, Lei WL, Xu XH, Ju XC, Liu Y, Luo ZG. JIP1 mediates anterograde transport of Rab10 cargos during neuronal polarization. J Neurosci 2014; 34:1710-1723.
    • (2014) J Neurosci , vol.34 , pp. 1710-1723
    • Deng, C.Y.1    Lei, W.L.2    Xu, X.H.3    Ju, X.C.4    Liu, Y.5    Luo, Z.G.6
  • 57
    • 79958059534 scopus 로고    scopus 로고
    • Rab6, Rab8, and MICAL3 cooperate in controlling docking and fusion of exocytotic carriers
    • Grigoriev I, Yu KL, Martinez-Sanchez E, et al. Rab6, Rab8, and MICAL3 cooperate in controlling docking and fusion of exocytotic carriers. Curr Biol 2011; 21:967-974.
    • (2011) Curr Biol , vol.21 , pp. 967-974
    • Grigoriev, I.1    Yu, K.L.2    Martinez-Sanchez, E.3
  • 58
    • 65549104155 scopus 로고    scopus 로고
    • Anterograde transport of TrkB in axons is mediated by direct interaction with Slp1 and Rab27
    • Arimura N, Kimura T, Nakamuta S, et al. Anterograde transport of TrkB in axons is mediated by direct interaction with Slp1 and Rab27. Dev Cell 2009; 16:675-686.
    • (2009) Dev Cell , vol.16 , pp. 675-686
    • Arimura, N.1    Kimura, T.2    Nakamuta, S.3
  • 59
    • 33644968948 scopus 로고    scopus 로고
    • MKLP1 requires specific domains for its dendritic targeting
    • Xu X, He C, Zhang Z, Chen Y. MKLP1 requires specific domains for its dendritic targeting. J Cell Sci 2006; 119:452-458.
    • (2006) J Cell Sci , vol.119 , pp. 452-458
    • Xu, X.1    He, C.2    Zhang, Z.3    Chen, Y.4
  • 60
    • 0035584249 scopus 로고    scopus 로고
    • Effcient gene transfer into the embryonic mouse brain using in vivo electroporation
    • Saito T, Nakatsuji N. Effcient gene transfer into the embryonic mouse brain using in vivo electroporation. Dev Biol 2001; 240:237-246.
    • (2001) Dev Biol , vol.240 , pp. 237-246
    • Saito, T.1    Nakatsuji, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.