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Volumn 13, Issue 5, 2003, Pages 535-544

Regulation of neuronal morphogenesis and synaptic function by Abl family kinases

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON NON RECEPTOR TYROSINE KINASE; CADHERIN; CELL RECEPTOR; ENZYME; GROWTH FACTOR RECEPTOR; INTEGRIN; LEUKOCYTE ANTIGEN; PROTEIN TYROSINE KINASE; RECEPTOR PROTEIN; UNCLASSIFIED DRUG;

EID: 0141891986     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.conb.2003.08.002     Document Type: Review
Times cited : (79)

References (74)
  • 1
    • 0032937828 scopus 로고    scopus 로고
    • Cycling, stressed-out and nervous: Cellular functions of c-Abl
    • Van Etten R.A. Cycling, stressed-out and nervous: cellular functions of c-Abl. Trends Cell Biol. 9:1999;179-186.
    • (1999) Trends Cell Biol. , vol.9 , pp. 179-186
    • Van Etten, R.A.1
  • 2
    • 0036391801 scopus 로고    scopus 로고
    • The Abl family kinases: Mechanisms of regulation and signaling
    • Pendergast A.M. The Abl family kinases: mechanisms of regulation and signaling. Adv. Cancer Res. 85:2002;51-100.
    • (2002) Adv. Cancer Res. , vol.85 , pp. 51-100
    • Pendergast, A.M.1
  • 3
  • 4
    • 0033614446 scopus 로고    scopus 로고
    • Chronic myeloid leukemia
    • Sawyers C.L. Chronic myeloid leukemia. N. Engl. J. Med. 340:1999;1330-1340.
    • (1999) N. Engl. J. Med. , vol.340 , pp. 1330-1340
    • Sawyers, C.L.1
  • 5
    • 0034064630 scopus 로고    scopus 로고
    • C-Abl: Activation and nuclear targets
    • Shaul Y. c-Abl: activation and nuclear targets. Cell Death Differ. 7:2000;10-16.
    • (2000) Cell Death Differ. , vol.7 , pp. 10-16
    • Shaul, Y.1
  • 6
    • 0024338902 scopus 로고
    • Drosophila abl tyrosine kinase in embryonic CNS axons: A role in axonogenesis is revealed through dosage-sensitive interactions with disabled
    • Gertler F.B., Bennett R.L., Clark M.J., Hoffmann F.M. Drosophila abl tyrosine kinase in embryonic CNS axons: a role in axonogenesis is revealed through dosage-sensitive interactions with disabled. Cell. 58:1989;103-113.
    • (1989) Cell , vol.58 , pp. 103-113
    • Gertler, F.B.1    Bennett, R.L.2    Clark, M.J.3    Hoffmann, F.M.4
  • 7
    • 0033082439 scopus 로고    scopus 로고
    • The tyrosine kinase Abl and its substrate enabled collaborate with the receptor phosphatase Dlar to control motor axon guidance
    • Wills Z., Bateman J., Korey C.A., Comer A., Van Vactor D. The tyrosine kinase Abl and its substrate enabled collaborate with the receptor phosphatase Dlar to control motor axon guidance. Neuron. 22:1999;301-312.
    • (1999) Neuron , vol.22 , pp. 301-312
    • Wills, Z.1    Bateman, J.2    Korey, C.A.3    Comer, A.4    Van Vactor, D.5
  • 8
    • 0037079061 scopus 로고    scopus 로고
    • A Drosophila homolog of cyclase-associated proteins collaborates with the Abl tyrosine kinase to control midline axon pathfinding
    • In this paper, the authors show that D-abl mutations lead to aberrant midline crossing by longitudinal axons. Heterozygosity for both D-abl and slit also leads to increased midline crossing. These data argue that D-Abl acts in a positive fashion to mediate repellent signaling downstream of Slit-Robo interactions.
    • Wills Z., Emerson M., Rusch J., Bikoff J., Baum B., Perrimon N., Van Vactor D. A Drosophila homolog of cyclase-associated proteins collaborates with the Abl tyrosine kinase to control midline axon pathfinding. Neuron. 36:2002;611-622 In this paper, the authors show that D-abl mutations lead to aberrant midline crossing by longitudinal axons. Heterozygosity for both D-abl and slit also leads to increased midline crossing. These data argue that D-Abl acts in a positive fashion to mediate repellent signaling downstream of Slit-Robo interactions.
    • (2002) Neuron. , vol.36 , pp. 611-622
    • Wills, Z.1    Emerson, M.2    Rusch, J.3    Bikoff, J.4    Baum, B.5    Perrimon, N.6    Van Vactor, D.7
  • 9
    • 0032554841 scopus 로고    scopus 로고
    • Roles of Armadillo, a Drosophila catenin, during central nervous system development
    • Loureiro J., Peifer M. Roles of Armadillo, a Drosophila catenin, during central nervous system development. Curr. Biol. 8:1998;622-632.
    • (1998) Curr. Biol. , vol.8 , pp. 622-632
    • Loureiro, J.1    Peifer, M.2
  • 10
    • 0033083179 scopus 로고    scopus 로고
    • Profilin and the Abl tyrosine kinase are required for motor axon outgrowth in the Drosophila embryo
    • Wills Z., Marr L., Zinn K., Goodman C.S., Van Vactor D. Profilin and the Abl tyrosine kinase are required for motor axon outgrowth in the Drosophila embryo. Neuron. 22:1999;291-299.
    • (1999) Neuron , vol.22 , pp. 291-299
    • Wills, Z.1    Marr, L.2    Zinn, K.3    Goodman, C.S.4    Van Vactor, D.5
  • 11
    • 0033694911 scopus 로고    scopus 로고
    • Dosage-sensitive, reciprocal genetic interactions between the Abl tyrosine kinase and the putative GEF trio reveal trio's role in axon pathfinding
    • Liebl E.C., Forsthoefel D.J., Franco L.S., Sample S.H., Hess J.E., Cowger J.A., Chandler M.P., Shupert A.M., Seeger M.A. Dosage-sensitive, reciprocal genetic interactions between the Abl tyrosine kinase and the putative GEF trio reveal trio's role in axon pathfinding. Neuron. 26:2000;107-118.
    • (2000) Neuron , vol.26 , pp. 107-118
    • Liebl, E.C.1    Forsthoefel, D.J.2    Franco, L.S.3    Sample, S.H.4    Hess, J.E.5    Cowger, J.A.6    Chandler, M.P.7    Shupert, A.M.8    Seeger, M.A.9
  • 12
    • 0029148433 scopus 로고
    • Genetic interactions between the Drosophila Abelson (Abl) tyrosine kinase and failed axon connections (Fax), a novel protein in axon bundles
    • Hill K.K., Bedian V., Juang J.L., Hoffmann F.M. Genetic interactions between the Drosophila Abelson (Abl) tyrosine kinase and failed axon connections (Fax), a novel protein in axon bundles. Genetics. 141:1995;595-606.
    • (1995) Genetics , vol.141 , pp. 595-606
    • Hill, K.K.1    Bedian, V.2    Juang, J.L.3    Hoffmann, F.M.4
  • 13
    • 0027245960 scopus 로고
    • Dosage-sensitive modifiers of Drosophila Abl tyrosine kinase function: Prospero, a regulator of axonal outgrowth, and Disabled, a novel tyrosine kinase substrate
    • Gertler F.B., Hill K.K., Clark M.J., Hoffmann F.M. Dosage-sensitive modifiers of Drosophila Abl tyrosine kinase function: Prospero, a regulator of axonal outgrowth, and Disabled, a novel tyrosine kinase substrate. Genes Dev. 7:1993;441-453.
    • (1993) Genes Dev. , vol.7 , pp. 441-453
    • Gertler, F.B.1    Hill, K.K.2    Clark, M.J.3    Hoffmann, F.M.4
  • 14
    • 0032055258 scopus 로고    scopus 로고
    • A role for Abl in Notch signaling
    • Giniger E. A role for Abl in Notch signaling. Neuron. 20:1998;667-681.
    • (1998) Neuron , vol.20 , pp. 667-681
    • Giniger, E.1
  • 15
    • 0035945346 scopus 로고    scopus 로고
    • Abelson kinase regulates epithelial morphogenesis in Drosophila
    • Loss of both zygotic and maternal D-Abl stores leads to dramatic defects in neuronal morphogenesis. The authors also show that the loss of D-Abl function leads to defects in epithelial morphogenesis and migration during dorsal closure. The loss of D-Abl function reduces the amount of Armadillo (β-catenin) and α-catenin in adherens junctions, suggesting that Abl family kinases may regulate the formation or stability of these adhesive contacts between cells
    • Grevengoed E.E., Loureiro J.J., Jesse T.L., Peifer M. Abelson kinase regulates epithelial morphogenesis in Drosophila. J. Cell Biol. 155:2001;1185-1198 Loss of both zygotic and maternal D-Abl stores leads to dramatic defects in neuronal morphogenesis. The authors also show that the loss of D-Abl function leads to defects in epithelial morphogenesis and migration during dorsal closure. The loss of D-Abl function reduces the amount of Armadillo (β-catenin) and α-catenin in adherens junctions, suggesting that Abl family kinases may regulate the formation or stability of these adhesive contacts between cells.
    • (2001) J. Cell Biol. , vol.155 , pp. 1185-1198
    • Grevengoed, E.E.1    Loureiro, J.J.2    Jesse, T.L.3    Peifer, M.4
  • 17
    • 0037018155 scopus 로고    scopus 로고
    • Modulation of the F-actin cytoskeleton by c-Abl tyrosine kinase in cell spreading and neurite extension
    • Here, Woodring et al. show that overexpression of Abl leads to actin microspike formation in fibroblasts and to short dendritic microspikes in cultured neurons
    • Woodring P.J., Litwack E.D., O'Leary D.D., Lucero G.R., Wang J.Y., Hunter T. Modulation of the F-actin cytoskeleton by c-Abl tyrosine kinase in cell spreading and neurite extension. J. Cell Biol. 156:2002;879-892 Here, Woodring, et al. show that overexpression of Abl leads to actin microspike formation in fibroblasts and to short dendritic microspikes in cultured neurons.
    • (2002) J. Cell Biol. , vol.156 , pp. 879-892
    • Woodring, P.J.1    Litwack, E.D.2    O'leary, D.D.3    Lucero, G.R.4    Wang, J.Y.5    Hunter, T.6
  • 19
    • 0034705292 scopus 로고    scopus 로고
    • Repulsive axon guidance: Abelson and Enabled play opposing roles downstream of the roundabout receptor
    • Bashaw G.J., Kidd T., Murray D., Pawson T., Goodman C.S. Repulsive axon guidance: Abelson and Enabled play opposing roles downstream of the roundabout receptor. Cell. 101:2000;703-715.
    • (2000) Cell , vol.101 , pp. 703-715
    • Bashaw, G.J.1    Kidd, T.2    Murray, D.3    Pawson, T.4    Goodman, C.S.5
  • 20
    • 0033957068 scopus 로고    scopus 로고
    • Slit proteins: Key regulators of axon guidance, axonal branching, and cell migration
    • Brose K., Tessier-Lavigne M. Slit proteins: key regulators of axon guidance, axonal branching, and cell migration. Curr. Opin. Neurobiol. 10:2000;95-102.
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 95-102
    • Brose, K.1    Tessier-Lavigne, M.2
  • 22
    • 0030030320 scopus 로고    scopus 로고
    • The transmembrane tyrosine phosphatase DLAR controls motor axon guidance in Drosophila
    • Krueger N.X., Van Vactor D., Wan H.I., Gelbart W.M., Goodman C.S., Saito H. The transmembrane tyrosine phosphatase DLAR controls motor axon guidance in Drosophila. Cell. 84:1996;611-622.
    • (1996) Cell , vol.84 , pp. 611-622
    • Krueger, N.X.1    Van Vactor, D.2    Wan, H.I.3    Gelbart, W.M.4    Goodman, C.S.5    Saito, H.6
  • 23
    • 0030861051 scopus 로고    scopus 로고
    • Axon patterning requires DN-cadherin, a novel neuronal adhesion receptor, in the Drosophila embryonic CNS
    • Iwai Y., Usui T., Hirano S., Steward R., Takeichi M., Uemura T. Axon patterning requires DN-cadherin, a novel neuronal adhesion receptor, in the Drosophila embryonic CNS. Neuron. 19:1997;77-89.
    • (1997) Neuron , vol.19 , pp. 77-89
    • Iwai, Y.1    Usui, T.2    Hirano, S.3    Steward, R.4    Takeichi, M.5    Uemura, T.6
  • 24
    • 0036800124 scopus 로고    scopus 로고
    • Activation of the repulsive receptor Roundabout inhibits N-cadherin-mediated cell adhesion
    • Slit binding to Robo can disrupt the function of N-cadherin. Activation of Robo leads to increased phosphorylation of β-catenin accompanied by a dissociation of β-catenin from N-cadherin. Abl is associated with Robo and may be responsible for β-catenin phosphorylation
    • Rhee J., Mahfooz N.S., Arregui C., Lilien J., Balsamo J., VanBerkum M.F. Activation of the repulsive receptor Roundabout inhibits N-cadherin-mediated cell adhesion. Nat. Cell Biol. 4:2002;798-805 Slit binding to Robo can disrupt the function of N-cadherin. Activation of Robo leads to increased phosphorylation of β-catenin accompanied by a dissociation of β-catenin from N-cadherin. Abl is associated with Robo and may be responsible for β-catenin phosphorylation.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 798-805
    • Rhee, J.1    Mahfooz, N.S.2    Arregui, C.3    Lilien, J.4    Balsamo, J.5    Vanberkum, M.F.6
  • 25
    • 0036500983 scopus 로고    scopus 로고
    • Brain Armadillo protein delta-catenin interacts with Abl tyrosine kinase and modulates cellular morphogenesis in response to growth factors
    • Lu Q., Mukhopadhyay N.K., Griffin J.D., Paredes M., Medina M., Kosik K.S. Brain Armadillo protein delta-catenin interacts with Abl tyrosine kinase and modulates cellular morphogenesis in response to growth factors. J. Neurosci. Res. 67:2002;618-624.
    • (2002) J. Neurosci. Res. , vol.67 , pp. 618-624
    • Lu, Q.1    Mukhopadhyay, N.K.2    Griffin, J.D.3    Paredes, M.4    Medina, M.5    Kosik, K.S.6
  • 27
    • 0035947801 scopus 로고    scopus 로고
    • Polarized distribution of alpha5 integrin in dendrites of hippocampal and cortical neurons
    • Bi X., Lynch G., Zhou J., Gall C.M. Polarized distribution of alpha5 integrin in dendrites of hippocampal and cortical neurons. J. Comp. Neurol. 435:2001;184-193.
    • (2001) J. Comp. Neurol. , vol.435 , pp. 184-193
    • Bi, X.1    Lynch, G.2    Zhou, J.3    Gall, C.M.4
  • 28
    • 0036682158 scopus 로고    scopus 로고
    • The integrin family of cell adhesion molecules has multiple functions within the CNS
    • Milner R., Campbell I.L. The integrin family of cell adhesion molecules has multiple functions within the CNS. J. Neurosci. Res. 69:2002;286-291.
    • (2002) J. Neurosci. Res. , vol.69 , pp. 286-291
    • Milner, R.1    Campbell, I.L.2
  • 29
    • 0033568349 scopus 로고    scopus 로고
    • C-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF
    • Plattner R., Kadlec L., DeMali K.A., Kazlauskas A., Pendergast A.M. c-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF. Genes Dev. 13:1999;2400-2411.
    • (1999) Genes Dev. , vol.13 , pp. 2400-2411
    • Plattner, R.1    Kadlec, L.2    Demali, K.A.3    Kazlauskas, A.4    Pendergast, A.M.5
  • 31
    • 0026012736 scopus 로고
    • PDGF A-chain gene is expressed by mammalian neurons during development and in maturity
    • Yeh H.J., Ruit K.G., Wang Y.X., Parks W.C., Snider W.D., Deuel T.F. PDGF A-chain gene is expressed by mammalian neurons during development and in maturity. Cell. 64:1991;209-216.
    • (1991) Cell , vol.64 , pp. 209-216
    • Yeh, H.J.1    Ruit, K.G.2    Wang, Y.X.3    Parks, W.C.4    Snider, W.D.5    Deuel, T.F.6
  • 33
    • 0031025728 scopus 로고    scopus 로고
    • Developmental expression of platelet-derived growth factor alpha-receptor in neurons and glial cells of the mouse CNS
    • Oumesmar B.N., Vignais L., Baron-Van Evercooren A. Developmental expression of platelet-derived growth factor alpha-receptor in neurons and glial cells of the mouse CNS. J. Neurosci. 17:1997;125-139.
    • (1997) J. Neurosci. , vol.17 , pp. 125-139
    • Oumesmar, B.N.1    Vignais, L.2    Baron-Van Evercooren, A.3
  • 34
    • 0027512554 scopus 로고
    • Developmental expression of the platelet-derived growth factor alpha-receptor gene in mammalian central nervous system
    • Yeh H.J., Silos-Santiago I., Wang Y.X., George R.J., Snider W.D., Deuel T.F. Developmental expression of the platelet-derived growth factor alpha-receptor gene in mammalian central nervous system. Proc. Natl. Acad. Sci. U.S.A. 90:1993;1952-1956.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 1952-1956
    • Yeh, H.J.1    Silos-Santiago, I.2    Wang, Y.X.3    George, R.J.4    Snider, W.D.5    Deuel, T.F.6
  • 35
    • 0028972764 scopus 로고
    • PDGF-alpha receptor is expressed by mature neurones of the central nervous system
    • Vignais L., Oumesmar B.N., Baron-Van Evercooren A.B. PDGF-alpha receptor is expressed by mature neurones of the central nervous system. Neuroreport. 6:1995;1993-1996.
    • (1995) Neuroreport , vol.6 , pp. 1993-1996
    • Vignais, L.1    Oumesmar, B.N.2    Baron-Van Evercooren, A.B.3
  • 36
    • 0025913156 scopus 로고
    • Neurotrophic activity of platelet-derived growth factor (PDGF): Rat neuronal cells possess functional PDGF beta-type receptors and respond to PDGF
    • Smits A., Kato M., Westermark B., Nister M., Heldin C.H., Funa K. Neurotrophic activity of platelet-derived growth factor (PDGF): Rat neuronal cells possess functional PDGF beta-type receptors and respond to PDGF. Proc. Natl. Acad. Sci. U.S.A. 88:1991;8159-8163.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 8159-8163
    • Smits, A.1    Kato, M.2    Westermark, B.3    Nister, M.4    Heldin, C.H.5    Funa, K.6
  • 37
    • 0030221511 scopus 로고    scopus 로고
    • CAM-FGF receptor interactions: A model for axonal growth
    • Doherty P., Walsh F.S. CAM-FGF receptor interactions: a model for axonal growth. Mol. Cell Neurosci. 8:1996;99-111.
    • (1996) Mol. Cell Neurosci. , vol.8 , pp. 99-111
    • Doherty, P.1    Walsh, F.S.2
  • 38
    • 0033152924 scopus 로고    scopus 로고
    • Signal transduction underlying growth cone guidance by diffusible factors
    • Song H.J., Poo M.M. Signal transduction underlying growth cone guidance by diffusible factors. Curr. Opin. Neurobiol. 9:1999;355-363.
    • (1999) Curr. Opin. Neurobiol. , vol.9 , pp. 355-363
    • Song, H.J.1    Poo, M.M.2
  • 39
    • 0034598995 scopus 로고    scopus 로고
    • Direct interaction of nerve growth factor receptor, TrkA, with non-receptor tyrosine kinase, c-Abl, through the activation loop
    • Koch A., Mancini A., Stefan M., Niedenthal R., Niemann H., Tamura T. Direct interaction of nerve growth factor receptor, TrkA, with non-receptor tyrosine kinase, c-Abl, through the activation loop. FEBS Lett. 469:2000;72-76.
    • (2000) FEBS Lett. , vol.469 , pp. 72-76
    • Koch, A.1    Mancini, A.2    Stefan, M.3    Niedenthal, R.4    Niemann, H.5    Tamura, T.6
  • 40
    • 0034141280 scopus 로고    scopus 로고
    • Association of the Abl tyrosine kinase with the Trk nerve growth factor receptor
    • Yano H., Cong F., Birge R.B., Goff S.P., Chao M.V. Association of the Abl tyrosine kinase with the Trk nerve growth factor receptor. J. Neurosci. Res. 59:2000;356-364.
    • (2000) J. Neurosci. Res. , vol.59 , pp. 356-364
    • Yano, H.1    Cong, F.2    Birge, R.B.3    Goff, S.P.4    Chao, M.V.5
  • 41
    • 0035811562 scopus 로고    scopus 로고
    • Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor
    • Yu H.H., Zisch A.H., Dodelet V.C., Pasquale E.B. Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor. Oncogene. 20:2001;3995-4006.
    • (2001) Oncogene , vol.20 , pp. 3995-4006
    • Yu, H.H.1    Zisch, A.H.2    Dodelet, V.C.3    Pasquale, E.B.4
  • 42
    • 0028084328 scopus 로고
    • The COOH terminus of the c-Abl tyrosine kinase contains distinct F- and G-actin binding domains with bundling activity
    • Van Etten R.A., Jackson P.K., Baltimore D., Sanders M.C., Matsudaira P.T., Janmey P.A. The COOH terminus of the c-Abl tyrosine kinase contains distinct F- and G-actin binding domains with bundling activity. J. Cell Biol. 124:1994;325-340.
    • (1994) J. Cell Biol. , vol.124 , pp. 325-340
    • Van Etten, R.A.1    Jackson, P.K.2    Baltimore, D.3    Sanders, M.C.4    Matsudaira, P.T.5    Janmey, P.A.6
  • 43
    • 0035910059 scopus 로고    scopus 로고
    • The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-binding domains to bundle F-actin
    • Here, Wang et al. show that Arg can use two F-actin-binding domains to bundle F-actin in vitro. Arg requires both F-actin-binding domains to organize F-actin-rich protrusive structures at the fibroblast periphery. A C-terminal fragment lacking the kinase domain can form these structures, arguing that the F-actin-binding domains can directly organize F-actin in vivo
    • Wang Y., Miller A.L., Mooseker M.S., Koleske A.J. The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-binding domains to bundle F-actin. Proc. Natl. Acad. Sci. U.S.A. 98:2001;14865-14870 Here, Wang, et al. show that Arg can use two F-actin-binding domains to bundle F-actin in vitro. Arg requires both F-actin-binding domains to organize F-actin-rich protrusive structures at the fibroblast periphery. A C-terminal fragment lacking the kinase domain can form these structures, arguing that the F-actin-binding domains can directly organize F-actin in vivo.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 14865-14870
    • Wang, Y.1    Miller, A.L.2    Mooseker, M.S.3    Koleske, A.J.4
  • 46
    • 18444389953 scopus 로고    scopus 로고
    • Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility
    • The findings of this study provide evidence that Ena/VASP family proteins regulate actin filament elongation by protecting actin filament ends from the actions of capping protein. Electron microscopic visualization in cells with altered Ena/VASP protein function suggests that these proteins regulate cell motility by regulating the length and geometry of lamellipodial actin filaments
    • Bear J.E., Svitkina T.M., Krause M., Schafer D.A., Loureiro J.J., Strasser G.A., Maly I.V., Chaga O.Y., Cooper J.A., Borisy G.G., et al. Antagonism between Ena/VASP proteins and actin filament capping regulates fibroblast motility. Cell. 109:2002;509-521 The findings of this study provide evidence that Ena/VASP family proteins regulate actin filament elongation by protecting actin filament ends from the actions of capping protein. Electron microscopic visualization in cells with altered Ena/VASP protein function suggests that these proteins regulate cell motility by regulating the length and geometry of lamellipodial actin filaments.
    • (2002) Cell , vol.109 , pp. 509-521
    • Bear, J.E.1    Svitkina, T.M.2    Krause, M.3    Schafer, D.A.4    Loureiro, J.J.5    Strasser, G.A.6    Maly, I.V.7    Chaga, O.Y.8    Cooper, J.A.9    Borisy, G.G.10
  • 47
    • 0025352201 scopus 로고
    • Genetic suppression of mutations in the Drosophila abl proto-oncogene homolog
    • Gertler F.B., Doctor J.S., Hoffmann F.M. Genetic suppression of mutations in the Drosophila abl proto-oncogene homolog. Science. 248:1990;857-860.
    • (1990) Science , vol.248 , pp. 857-860
    • Gertler, F.B.1    Doctor, J.S.2    Hoffmann, F.M.3
  • 48
    • 0028969388 scopus 로고
    • Enabled, a dosage-sensitive suppressor of mutations in the Drosophila Abl tyrosine kinase, encodes an Abl substrate with SH3 domain-binding properties
    • Gertler F.B., Comer A.R., Juang J.L., Ahern S.M., Clark M.J., Liebl E.C., Hoffmann F.M. Enabled, a dosage-sensitive suppressor of mutations in the Drosophila Abl tyrosine kinase, encodes an Abl substrate with SH3 domain-binding properties. Genes Dev. 9:1995;521-533.
    • (1995) Genes Dev. , vol.9 , pp. 521-533
    • Gertler, F.B.1    Comer, A.R.2    Juang, J.L.3    Ahern, S.M.4    Clark, M.J.5    Liebl, E.C.6    Hoffmann, F.M.7
  • 50
    • 0037415574 scopus 로고    scopus 로고
    • Mechanism of filopodia initiation by reorganization of a dendritic network
    • Nascent filopodia emerge from the cell membrane in association with localized concentrations of VASP. Filopodial actin bundles are capped by a tip complex that includes VASP and possibly other proteins. Svitkina et al. suggest that Ena/VASP proteins may regulate axon guidance by controlling the formation or reorganization of growth cone filopodia
    • Svitkina T.M., Bulanova E.A., Chaga O.Y., Vignjevic D.M., Kojima S., Vasiliev J.M., Borisy G.G. Mechanism of filopodia initiation by reorganization of a dendritic network. J. Cell Biol. 160:2003;409-421 Nascent filopodia emerge from the cell membrane in association with localized concentrations of VASP. Filopodial actin bundles are capped by a tip complex that includes VASP and possibly other proteins. Svitkina, et al. suggest that Ena/VASP proteins may regulate axon guidance by controlling the formation or reorganization of growth cone filopodia.
    • (2003) J. Cell Biol. , vol.160 , pp. 409-421
    • Svitkina, T.M.1    Bulanova, E.A.2    Chaga, O.Y.3    Vignjevic, D.M.4    Kojima, S.5    Vasiliev, J.M.6    Borisy, G.G.7
  • 51
    • 0038387454 scopus 로고    scopus 로고
    • Do filopodia enable growth cone guidance?
    • Koleske A.J. Do filopodia enable growth cone guidance? Sci. STKE. 183:2003;PE20.
    • (2003) Sci. STKE , vol.183 , pp. 20
    • Koleske, A.J.1
  • 52
    • 0031972950 scopus 로고    scopus 로고
    • Phosphorylation of enabled by the Drosophila Abelson tyrosine kinase regulates the in vivo function and protein-protein interactions of Enabled
    • Comer A.R., Ahern-Djamali S.M., Juang J.L., Jackson P.D., Hoffmann F.M. Phosphorylation of enabled by the Drosophila Abelson tyrosine kinase regulates the in vivo function and protein-protein interactions of Enabled. Mol. Cell Biol. 18:1998;152-160.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 152-160
    • Comer, A.R.1    Ahern-Djamali, S.M.2    Juang, J.L.3    Jackson, P.D.4    Hoffmann, F.M.5
  • 53
    • 0037821787 scopus 로고    scopus 로고
    • Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian Enabled (Mena) by c-Abl kinase
    • Tani K., Sato S., Sukezane T., Kojima H., Hirose H., Hanafusa H., Shishido T. Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian Enabled (Mena) by c-Abl kinase. J. Biol. Chem. 278:2003;21685-21692.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21685-21692
    • Tani, K.1    Sato, S.2    Sukezane, T.3    Kojima, H.4    Hirose, H.5    Hanafusa, H.6    Shishido, T.7
  • 54
    • 11944275667 scopus 로고
    • Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity
    • Dai Z., Pendergast A.M. Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity. Genes Dev. 9:1995;2569-2582.
    • (1995) Genes Dev. , vol.9 , pp. 2569-2582
    • Dai, Z.1    Pendergast, A.M.2
  • 55
    • 0028844631 scopus 로고
    • Abl-interactor-1, a novel SH3 protein binding to the carboxy-terminal portion of the Abl protein, suppresses v-abl transforming activity
    • Shi Y., Alin K., Goff S.P. Abl-interactor-1, a novel SH3 protein binding to the carboxy-terminal portion of the Abl protein, suppresses v-abl transforming activity. Genes Dev. 9:1995;2583-2597.
    • (1995) Genes Dev. , vol.9 , pp. 2583-2597
    • Shi, Y.1    Alin, K.2    Goff, S.P.3
  • 56
    • 0029992950 scopus 로고    scopus 로고
    • Identification of ArgBP1, an Arg protein tyrosine kinase binding protein that is the human homologue of a CNS-specific Xenopus gene
    • Wang B., Mysliwiec T., Krainc D., Jensen R.A., Sonoda G., Testa J.R., Golemis E.A., Kruh G.D. Identification of ArgBP1, an Arg protein tyrosine kinase binding protein that is the human homologue of a CNS-specific Xenopus gene. Oncogene. 12:1996;1921-1929.
    • (1996) Oncogene , vol.12 , pp. 1921-1929
    • Wang, B.1    Mysliwiec, T.2    Krainc, D.3    Jensen, R.A.4    Sonoda, G.5    Testa, J.R.6    Golemis, E.A.7    Kruh, G.D.8
  • 58
    • 0035811020 scopus 로고    scopus 로고
    • The Abl interactor proteins localize to sites of actin polymerization at the tips of lamellipodia and filopodia
    • Stradal T., Courtney K.D., Rottner K., Hahne P., Small J.V., Pendergast A.M. The Abl interactor proteins localize to sites of actin polymerization at the tips of lamellipodia and filopodia. Curr. Biol. 11:2001;891-895.
    • (2001) Curr. Biol. , vol.11 , pp. 891-895
    • Stradal, T.1    Courtney, K.D.2    Rottner, K.3    Hahne, P.4    Small, J.V.5    Pendergast, A.M.6
  • 59
    • 0033575909 scopus 로고    scopus 로고
    • Drosophila Abelson interacting protein (dAbi) is a positive regulator of Abelson tyrosine kinase activity
    • Juang J.L., Hoffmann F.M. Drosophila Abelson interacting protein (dAbi) is a positive regulator of Abelson tyrosine kinase activity. Oncogene. 18:1999;5138-5147.
    • (1999) Oncogene , vol.18 , pp. 5138-5147
    • Juang, J.L.1    Hoffmann, F.M.2
  • 60
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop A.L., Hall A. Rho GTPases and their effector proteins. Biochem. J. 348:2000;241-255.
    • (2000) Biochem. J. , vol.348 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 61
    • 0034659526 scopus 로고    scopus 로고
    • Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism
    • Arthur W.T., Petch L.A., Burridge K. Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism. Curr. Biol. 10:2000;719-722.
    • (2000) Curr. Biol. , vol.10 , pp. 719-722
    • Arthur, W.T.1    Petch, L.A.2    Burridge, K.3
  • 62
    • 0037853126 scopus 로고    scopus 로고
    • Cadherin engagement inhibits RhoA via p190RhoGAP
    • Noren N.K., Arthur W.T., Burridge K. Cadherin engagement inhibits RhoA via p190RhoGAP. J. Biol. Chem. 278:2003;13615-13618.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13615-13618
    • Noren, N.K.1    Arthur, W.T.2    Burridge, K.3
  • 63
    • 0035913909 scopus 로고    scopus 로고
    • Regulating axon branch stability: The role of p190 RhoGAP in repressing a retraction signaling pathway
    • Billuart P., Winter C.G., Maresh A., Zhao X., Luo L. Regulating axon branch stability: the role of p190 RhoGAP in repressing a retraction signaling pathway. Cell. 107:2001;195-207.
    • (2001) Cell , vol.107 , pp. 195-207
    • Billuart, P.1    Winter, C.G.2    Maresh, A.3    Zhao, X.4    Luo, L.5
  • 64
    • 0035071323 scopus 로고    scopus 로고
    • P190 RhoGAP is the principal Src substrate in brain and regulates axon outgrowth, guidance and fasciculation
    • Brouns M.R., Matheson S.F., Settleman J. p190 RhoGAP is the principal Src substrate in brain and regulates axon outgrowth, guidance and fasciculation. Nat. Cell Biol. 3:2001;361-367.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 361-367
    • Brouns, M.R.1    Matheson, S.F.2    Settleman, J.3
  • 65
    • 0037187643 scopus 로고    scopus 로고
    • Drosophila liprin-alpha and the receptor phosphatase Dlar control synapse morphogenesis
    • Kaufmann N., DeProto J., Ranjan R., Wan H., Van Vactor D. Drosophila liprin-alpha and the receptor phosphatase Dlar control synapse morphogenesis. Neuron. 34:2002;27-38.
    • (2002) Neuron , vol.34 , pp. 27-38
    • Kaufmann, N.1    Deproto, J.2    Ranjan, R.3    Wan, H.4    Van Vactor, D.5
  • 66
    • 0037340357 scopus 로고    scopus 로고
    • Abl family nonreceptor tyrosine kinases modulate short-term synaptic plasticity
    • This study shows that Abl and Arg localize to hippocampal synapses where their activity is required for short-term synaptic plasticity
    • Moresco E.M., Scheetz A.J., Bornmann W.G., Koleske A.J., Fitzsimonds R.M. Abl family nonreceptor tyrosine kinases modulate short-term synaptic plasticity. J. Neurophysiol. 89:2003;1678-1687 This study shows that Abl and Arg localize to hippocampal synapses where their activity is required for short-term synaptic plasticity.
    • (2003) J. Neurophysiol. , vol.89 , pp. 1678-1687
    • Moresco, E.M.1    Scheetz, A.J.2    Bornmann, W.G.3    Koleske, A.J.4    Fitzsimonds, R.M.5
  • 67
    • 0034279193 scopus 로고    scopus 로고
    • Structural and functional alterations of neuromuscular junctions in NCAM-deficient mice
    • Rafuse V.F., Polo-Parada L., Landmesser L.T. Structural and functional alterations of neuromuscular junctions in NCAM-deficient mice. J. Neurosci. 20:2000;6529-6539.
    • (2000) J. Neurosci. , vol.20 , pp. 6529-6539
    • Rafuse, V.F.1    Polo-Parada, L.2    Landmesser, L.T.3
  • 68
    • 0035819071 scopus 로고    scopus 로고
    • Alterations in transmission, vesicle dynamics, and transmitter release machinery at NCAM-deficient neuromuscular junctions
    • Polo-Parada L., Bose C.M., Landmesser L.T. Alterations in transmission, vesicle dynamics, and transmitter release machinery at NCAM-deficient neuromuscular junctions. Neuron. 32:2001;815-828.
    • (2001) Neuron , vol.32 , pp. 815-828
    • Polo-Parada, L.1    Bose, C.M.2    Landmesser, L.T.3
  • 69
    • 0037079063 scopus 로고    scopus 로고
    • Fear memory formation involves p190 RhoGAP and ROCK proteins through a GRB2-mediated complex
    • Lamprecht R., Farb C.R., LeDoux J.E. Fear memory formation involves p190 RhoGAP and ROCK proteins through a GRB2-mediated complex. Neuron. 36:2002;727-738.
    • (2002) Neuron , vol.36 , pp. 727-738
    • Lamprecht, R.1    Farb, C.R.2    Ledoux, J.E.3
  • 71
    • 0035909994 scopus 로고    scopus 로고
    • Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells
    • Ting A.Y., Kain K.H., Klemke R.L., Tsien R.Y. Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells. Proc. Natl. Acad. Sci. U.S.A. 98:2001;15003-15008.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 15003-15008
    • Ting, A.Y.1    Kain, K.H.2    Klemke, R.L.3    Tsien, R.Y.4
  • 72
    • 0034634597 scopus 로고    scopus 로고
    • C-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines
    • Brasher B.B., Van Etten R.A. c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines. J. Biol. Chem. 275:2000;35631-35637.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35631-35637
    • Brasher, B.B.1    Van Etten, R.A.2
  • 73
    • 0037508877 scopus 로고    scopus 로고
    • Two distinct phosphorylation pathways have additive effects on Abl family kinase activation
    • Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J. Two distinct phosphorylation pathways have additive effects on Abl family kinase activation. Mol. Cell Biol. 23:2003;3884-3896.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 3884-3896
    • Tanis, K.Q.1    Veach, D.2    Duewel, H.S.3    Bornmann, W.G.4    Koleske, A.J.5
  • 74
    • 0038392756 scopus 로고    scopus 로고
    • Postsynaptic requirement for Abl kinases in assembly of the neuromuscular junction
    • This study demonstrates that Abl family kinases are localized to muscles at the mouse NMJ. Abl and Arg are required for the agrin-induced clustering of acetylcholine receptors on the postsynaptic membrane of the NMJ in cultured myotubes, where they complex with and phosphorylate the muscle-specific receptor tyrosine kinase
    • Finn A.J., Feng G., Pendergast A.M. Postsynaptic requirement for Abl kinases in assembly of the neuromuscular junction. Nat. Neurosci. 6: 2003;717-723 This study demonstrates that Abl family kinases are localized to muscles at the mouse NMJ. Abl and Arg are required for the agrin-induced clustering of acetylcholine receptors on the postsynaptic membrane of the NMJ in cultured myotubes, where they complex with and phosphorylate the muscle-specific receptor tyrosine kinase.
    • (2003) Nat. Neurosci. , vol.6 , pp. 717-723
    • Finn, A.J.1    Feng, G.2    Pendergast, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.