메뉴 건너뛰기




Volumn 25, Issue 13, 2005, Pages 5763-5776

Generation and characterization of Rac3 knockout mice

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MESSENGER RNA; RAC PROTEIN; RAC1 PROTEIN; RAC2 PROTEIN; RAC3 PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 20744460575     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.13.5763-5776.2005     Document Type: Article
Times cited : (104)

References (51)
  • 2
    • 0025944684 scopus 로고
    • Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1
    • Abo, A., E. Pick, A. Hall, N. Totty, C. G. Teahan, and A. W. Segal. 1991. Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1. Nature 353:668-670.
    • (1991) Nature , vol.353 , pp. 668-670
    • Abo, A.1    Pick, E.2    Hall, A.3    Totty, N.4    Teahan, C.G.5    Segal, A.W.6
  • 3
    • 0031852652 scopus 로고    scopus 로고
    • Overexpression of a neural-specific Rho family GTPase, cRac1B, selectively induces enhanced neuritogenesis and neurite branching in primary neurons
    • Albertinazzi, C., D. Gilardelli, S. Paris, R. Longhi, and I. de Curtis. 1998. Overexpression of a neural-specific Rho family GTPase, cRac1B, selectively induces enhanced neuritogenesis and neurite branching in primary neurons. J. Cell Biol. 142:815-825.
    • (1998) J. Cell Biol. , vol.142 , pp. 815-825
    • Albertinazzi, C.1    Gilardelli, D.2    Paris, S.3    Longhi, R.4    De Curtis, I.5
  • 6
    • 0345305736 scopus 로고    scopus 로고
    • Differential distribution of Rac1 and Rac3 GTPases in the developing mouse brain: Implications for a role of Rac3 in Purkinje cell differentiation
    • Bolis, A., S. Corbetta, A. Cioce, and I. de Curtis. 2003. Differential distribution of Rac1 and Rac3 GTPases in the developing mouse brain: implications for a role of Rac3 in Purkinje cell differentiation. Eur. J. Neurosci. 18:2417-2424.
    • (2003) Eur. J. Neurosci. , vol.18 , pp. 2417-2424
    • Bolis, A.1    Corbetta, S.2    Cioce, A.3    De Curtis, I.4
  • 7
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac take center stage
    • Burridge, K., and K. Wennerberg. 2004. Rho and Rac take center stage. Cell 116:167-179.
    • (2004) Cell , vol.116 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 8
    • 0033560924 scopus 로고    scopus 로고
    • Characterization of progressive motor deficits in mice transgenic for the human Huntington's Disease mutation
    • Carter, R. J., L. A. Lione, T. Humby, L. Mangiarini, A. Mahal, G. P. Bates, S. B. Dunnett, and A. J. Morton. 1999. Characterization of progressive motor deficits in mice transgenic for the human Huntington's Disease mutation. J. Neurosci. 15:3248-3257.
    • (1999) J. Neurosci. , vol.15 , pp. 3248-3257
    • Carter, R.J.1    Lione, L.A.2    Humby, T.3    Mangiarini, L.4    Mahal, A.5    Bates, G.P.6    Dunnett, S.B.7    Morton, A.J.8
  • 9
    • 0030864463 scopus 로고    scopus 로고
    • Purkinje cell expression of a mutant allele of SCA1 in transgenic mice leads to disparate effects on motor behaviors, followed by a progressive cerebellar dysfunction and histological alterations
    • Clark, H. B., E. N. Burright, W. S. Yunis, S. Larson, C. Wilcox, B. Hartman, A. Matilla, H. Y. Zoghbi, and H. T. Orr. 1997. Purkinje cell expression of a mutant allele of SCA1 in transgenic mice leads to disparate effects on motor behaviors, followed by a progressive cerebellar dysfunction and histological alterations. J. Neurosci. 17:7385-7395.
    • (1997) J. Neurosci. , vol.17 , pp. 7385-7395
    • Clark, H.B.1    Burright, E.N.2    Yunis, W.S.3    Larson, S.4    Wilcox, C.5    Hartman, B.6    Matilla, A.7    Zoghbi, H.Y.8    Orr, H.T.9
  • 10
    • 3142570811 scopus 로고    scopus 로고
    • Differential corticostriatal plasticity during fast and slow motor skill learning in mice
    • Costa, R. M., D. Cohen, and M. A. Nicodelis. 2004. Differential corticostriatal plasticity during fast and slow motor skill learning in mice. Curr. Biol. 14:1124-1134.
    • (2004) Curr. Biol. , vol.14 , pp. 1124-1134
    • Costa, R.M.1    Cohen, D.2    Nicodelis, M.A.3
  • 11
    • 0033578272 scopus 로고    scopus 로고
    • Behavioral phenotyping of transgenic and knockout mice: Experimental design and evaluation of general health, sensory functions, motor abilities, and specific behavioral tests
    • Crawley, J. N. 1999. Behavioral phenotyping of transgenic and knockout mice: experimental design and evaluation of general health, sensory functions, motor abilities, and specific behavioral tests. Brain Res. 835:18-26.
    • (1999) Brain Res. , vol.835 , pp. 18-26
    • Crawley, J.N.1
  • 13
    • 0036533662 scopus 로고    scopus 로고
    • The Rac2 guanosine triphosphatase regulates B lymphocyte antigen receptor responses and chemotaxis and is required for establishment of B-1a and marginal zone B lymphocytes
    • Croker, B. A., D. M. Tarlinton, L. A. Cluse, A. J. Tuxen, A. Light, F. C. Yang, D. A. Williams, and A. W. Roberts. 2002. The Rac2 guanosine triphosphatase regulates B lymphocyte antigen receptor responses and chemotaxis and is required for establishment of B-1a and marginal zone B lymphocytes. J. Immunol. 168:3376-3386.
    • (2002) J. Immunol. , vol.168 , pp. 3376-3386
    • Croker, B.A.1    Tarlinton, D.M.2    Cluse, L.A.3    Tuxen, A.J.4    Light, A.5    Yang, F.C.6    Williams, D.A.7    Roberts, A.W.8
  • 14
    • 4344713872 scopus 로고    scopus 로고
    • Changes in motoric, exploratory and emotional behaviours and neuronal acetylcholine content and 5-HT turnover in histidine decarboxylase-KO mice
    • Dere, E., M. A. De Souza-Silva, R. E. Spieler, J. S. Lin, H. Ohtsu, H. L. Haas, and J. P. Huston. 2004. Changes in motoric, exploratory and emotional behaviours and neuronal acetylcholine content and 5-HT turnover in histidine decarboxylase-KO mice. Eur. J. Neurosci. 20:1051-1058.
    • (2004) Eur. J. Neurosci. , vol.20 , pp. 1051-1058
    • Dere, E.1    De Souza-Silva, M.A.2    Spieler, R.E.3    Lin, J.S.4    Ohtsu, H.5    Haas, H.L.6    Huston, J.P.7
  • 15
    • 0024425981 scopus 로고
    • Rac, a novel ras-related family of proteins that are botulinum toxin substrates
    • Didsbury, J., R. F. Weber, G. M. Bokoch, T. Evans, and R. Snyderman. 1989. Rac, a novel ras-related family of proteins that are botulinum toxin substrates. J. Biol. Chem. 264:16378-16382.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16378-16382
    • Didsbury, J.1    Weber, R.F.2    Bokoch, G.M.3    Evans, T.4    Snyderman, R.5
  • 16
    • 70449177837 scopus 로고
    • A note on a simple apparatus for detecting neurological deficit in rats and mice
    • Dunham, N. W., and T. S. Miya. 1957. A note on a simple apparatus for detecting neurological deficit in rats and mice. J. Am. Pharm. Assoc. 46:208-209.
    • (1957) J. Am. Pharm. Assoc. , vol.46 , pp. 208-209
    • Dunham, N.W.1    Miya, T.S.2
  • 17
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville, S., and A. Hall. 2002. Rho GTPases in cell biology. Nature 420:629-635.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 20
    • 0030824832 scopus 로고    scopus 로고
    • Characterization of RAC3, a novel member of the Rho family
    • Haataja, L., J. Groffen, and N. Heisterkamp. 1997. Characterization of RAC3, a novel member of the Rho family. J. Biol. Chem. 272:20384-20388.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20384-20388
    • Haataja, L.1    Groffen, J.2    Heisterkamp, N.3
  • 21
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. 1998. Rho GTPases and the actin cytoskeleton. Science 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 22
    • 0019775996 scopus 로고
    • Immunohistochemical mapping of vitamin D-dependent calcium-binding protein in brain
    • Jande, S. S., L. Maler, and D. E. Lawson. 1981. Immunohistochemical mapping of vitamin D-dependent calcium-binding protein in brain. Nature 294:765-767.
    • (1981) Nature , vol.294 , pp. 765-767
    • Jande, S.S.1    Maler, L.2    Lawson, D.E.3
  • 23
    • 0025874249 scopus 로고
    • Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA
    • Kinsella, B. T., R. A. Erdman, and W. A. Maltese. 1991. Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA. J. Biol. Chem. 266:9786-9794.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9786-9794
    • Kinsella, B.T.1    Erdman, R.A.2    Maltese, W.A.3
  • 24
    • 0026335622 scopus 로고
    • Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2
    • Knaus, U. G., P. G. Heyworth, T. Evans, J. T. Curnutte, and J. M. Bokoch. 1991. Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2. Science 254:1512-1515.
    • (1991) Science , vol.254 , pp. 1512-1515
    • Knaus, U.G.1    Heyworth, P.G.2    Evans, T.3    Curnutte, J.T.4    Bokoch, J.M.5
  • 25
    • 0012510457 scopus 로고
    • Rotorod sensorimotor learning in cerebellar mutant mice
    • Lalonde, R., A. N. Bensoula, and M. Filali. 1995. Rotorod sensorimotor learning in cerebellar mutant mice. Neurosci. Res. 42:3-6.
    • (1995) Neurosci. Res. , vol.42 , pp. 3-6
    • Lalonde, R.1    Bensoula, A.N.2    Filali, M.3
  • 26
    • 0017643426 scopus 로고
    • RNA molecular weight determinations by gel electrophoresis under denaturing conditions, a critical reexamination
    • Lehrach, H., D. Diamond, J. M. Wozney, and H. Boedtker. 1977. RNA molecular weight determinations by gel electrophoresis under denaturing conditions, a critical reexamination. Biochemistry 16:4743-4751.
    • (1977) Biochemistry , vol.16 , pp. 4743-4751
    • Lehrach, H.1    Diamond, D.2    Wozney, J.M.3    Boedtker, H.4
  • 27
    • 0012602360 scopus 로고
    • On the cerebellum and motor learning
    • Llinas, R., and J. P. Welsh. 1993. On the cerebellum and motor learning. Curr. Opin. Neurobiol. 9:58-65.
    • (1993) Curr. Opin. Neurobiol. , vol.9 , pp. 58-65
    • Llinas, R.1    Welsh, J.P.2
  • 28
    • 0034574572 scopus 로고    scopus 로고
    • Rho GTPases in neuronal morphogenesis
    • Luo, L. 2000. Rho GTPases in neuronal morphogenesis. Nat. Rev. Neurosci. 1:173-180.
    • (2000) Nat. Rev. Neurosci. , vol.1 , pp. 173-180
    • Luo, L.1
  • 29
    • 0030844902 scopus 로고    scopus 로고
    • Differential expression of distinct members of Rho family GTP-binding proteins during neuronal development: Identification of Rac1B, a new neural-specific member of the family
    • Malosio, M. L., D. Gilardelli, S. Paris, C. Albertinazzi, and I. de Curtis. 1997. Differential expression of distinct members of Rho family GTP-binding proteins during neuronal development: identification of Rac1B, a new neural-specific member of the family. J. Neurosci. 17:6717-6728.
    • (1997) J. Neurosci. , vol.17 , pp. 6717-6728
    • Malosio, M.L.1    Gilardelli, D.2    Paris, S.3    Albertinazzi, C.4    De Curtis, I.5
  • 30
    • 0025352661 scopus 로고
    • Microtubule-associated proteins and the determination of neuronal form
    • Matus, A. 1990. Microtubule-associated proteins and the determination of neuronal form. J. Physiol. (Paris) 84:134-137.
    • (1990) J. Physiol. (Paris) , vol.84 , pp. 134-137
    • Matus, A.1
  • 31
    • 0041466271 scopus 로고    scopus 로고
    • Differences among eight inbred strains of mice in motor ability and motor learning on a rotorod
    • McFadyen, M. P., G. Kusek, V. J. Bolivar, and L. Flaherty. 2003. Differences among eight inbred strains of mice in motor ability and motor learning on a rotorod. Genes Brain Behav. 2:214-219.
    • (2003) Genes Brain Behav. , vol.2 , pp. 214-219
    • McFadyen, M.P.1    Kusek, G.2    Bolivar, V.J.3    Flaherty, L.4
  • 33
    • 0025754114 scopus 로고
    • The murine rac1 gene: CDNA cloning, tissue distribution and regulated expression of rac1 mRNA by disassembly of actin microfilaments
    • Moll, J., G. Sansig, E. Fattori, and H. van der Putten. 1991. The murine rac1 gene: cDNA cloning, tissue distribution and regulated expression of rac1 mRNA by disassembly of actin microfilaments. Oncogene 6:863-866.
    • (1991) Oncogene , vol.6 , pp. 863-866
    • Moll, J.1    Sansig, G.2    Fattori, E.3    Van Der Putten, H.4
  • 34
    • 0034661746 scopus 로고    scopus 로고
    • Small GTPases Rac and Rho in the maintenance of dendritic spines and branches in hippocampal pyramidal neurons
    • Nakayama, A. Y., M. B. Harms, and L. Luo. 2000. Small GTPases Rac and Rho in the maintenance of dendritic spines and branches in hippocampal pyramidal neurons. J. Neurosci. 20:5329-5338.
    • (2000) J. Neurosci. , vol.20 , pp. 5329-5338
    • Nakayama, A.Y.1    Harms, M.B.2    Luo, L.3
  • 36
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • Olson, M. F., A. Ashworth, and A. Hall. 1995. An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. Science 269:1270-1272.
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 37
    • 0037232481 scopus 로고    scopus 로고
    • Fgfr3 expression by astrocytes and their precursors: Evidence that astrocytes and oligodendrocytes originate in distinct neuroepithelial domains
    • Pringle, N. P., W.-P. Yu, M. Howell1, J. S. Colvin, D. M. Ornitz, and W. D. Richardson. 2003. Fgfr3 expression by astrocytes and their precursors: evidence that astrocytes and oligodendrocytes originate in distinct neuroepithelial domains. Development 130:93-102.
    • (2003) Development , vol.130 , pp. 93-102
    • Pringle, N.P.1    Yu, W.-P.2    Howell, M.3    Colvin, J.S.4    Ornitz, D.M.5    Richardson, W.D.6
  • 38
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A. J., H. F. Paterson, C. L. Johnston, D. Diekmann, and A. Hall. 1992. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70:401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 40
    • 0025370728 scopus 로고
    • A member of the ras gene superfamily is expressed specifically in T, B and myeloid hemopoietic cells
    • Shirsat, N. V., R. J. Pignolo, B. L. Kreider, and G. Rovera. 1990. A member of the ras gene superfamily is expressed specifically in T, B and myeloid hemopoietic cells. Oncogene 5:769-772.
    • (1990) Oncogene , vol.5 , pp. 769-772
    • Shirsat, N.V.1    Pignolo, R.J.2    Kreider, B.L.3    Rovera, G.4
  • 41
    • 17644438421 scopus 로고    scopus 로고
    • Impaired cerebellar long-term potentiation in type I adenylyl cyclase mutant mice
    • Storm, D. R., C. Hansel, B. Hacker, A. Parent, and D. J. Linden. 1998. Impaired cerebellar long-term potentiation in type I adenylyl cyclase mutant mice. Neuron 1:199-210.
    • (1998) Neuron , vol.1 , pp. 199-210
    • Storm, D.R.1    Hansel, C.2    Hacker, B.3    Parent, A.4    Linden, D.J.5
  • 43
    • 2442527679 scopus 로고    scopus 로고
    • Morphological development and maturation of the GABAergic synapses in the mouse cerebellar granular layer
    • Takayama, C., and Y. Inoue. 2004. Morphological development and maturation of the GABAergic synapses in the mouse cerebellar granular layer. Brain Res. Dev. Brain Res. 150:177-190.
    • (2004) Brain Res. Dev. Brain Res. , vol.150 , pp. 177-190
    • Takayama, C.1    Inoue, Y.2
  • 44
    • 0034212667 scopus 로고    scopus 로고
    • The small GTP-binding protein TC10 promotes nerve elongation in neuronal cells, and its expression is induced during nerve regeneration in rats
    • Tanabe, K., T. Tachibana, T. Yamashita, Y. H. Che, Y. Yoneda, T. Ochi, M. Tohyama, H. Yoshikawa, and H. Kiyama. 2000. The small GTP-binding protein TC10 promotes nerve elongation in neuronal cells, and its expression is induced during nerve regeneration in rats. J. Neurosci. 20:4138-4144.
    • (2000) J. Neurosci. , vol.20 , pp. 4138-4144
    • Tanabe, K.1    Tachibana, T.2    Yamashita, T.3    Che, Y.H.4    Yoneda, Y.5    Ochi, T.6    Tohyama, M.7    Yoshikawa, H.8    Kiyama, H.9
  • 45
    • 0029814712 scopus 로고    scopus 로고
    • Role of protein kinases in nerve terminal maturation and function
    • Valtorta, F., F. Benfenati, and H. Basudev. 1996. Role of protein kinases in nerve terminal maturation and function. Biochem. Soc. Trans. 24:645-653.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 645-653
    • Valtorta, F.1    Benfenati, F.2    Basudev, H.3
  • 46
    • 0024232977 scopus 로고
    • Synaptophysin (p38) at the frog neuromuscular junction: Its incorporation into the plasma membrane and recycling after intense quantal secretion
    • Valtorta, F., R. Jahn, R. Fesce, P. Greengard, and B. Ceccarelli. 1988. Synaptophysin (p38) at the frog neuromuscular junction: its incorporation into the plasma membrane and recycling after intense quantal secretion. J. Cell Biol. 107:2719-2730.
    • (1988) J. Cell Biol. , vol.107 , pp. 2719-2730
    • Valtorta, F.1    Jahn, R.2    Fesce, R.3    Greengard, P.4    Ceccarelli, B.5
  • 47
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and C. D'Souza-Schorey. 1997. Rho GTPases and signaling networks. Genes Dev. 11:2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 50
    • 1842426910 scopus 로고    scopus 로고
    • Rac1-deficient macrophages exhibit defects in cell spreading and membrane ruffling but not migration
    • Wells, C. M., M. Walmsley, S. Ooi, V. Tybulewicz, and A. J. Ridley. 2004. Rac1-deficient macrophages exhibit defects in cell spreading and membrane ruffling but not migration. J. Cell Sci. 117:1259-1268.
    • (2004) J. Cell Sci. , vol.117 , pp. 1259-1268
    • Wells, C.M.1    Walmsley, M.2    Ooi, S.3    Tybulewicz, V.4    Ridley, A.J.5
  • 51
    • 8444239999 scopus 로고    scopus 로고
    • Rac2-deficient murine macrophages have selective defects in superoxide production and phagocytosis of opsonized particles
    • Yamauchi, A., C. Kim, S. Li, C. C. Marchal, J. Towe, S. J. Atkinson, and M. C. Dinauer. 2004. Rac2-deficient murine macrophages have selective defects in superoxide production and phagocytosis of opsonized particles. J. Immunol. 173:5971-5979.
    • (2004) J. Immunol. , vol.173 , pp. 5971-5979
    • Yamauchi, A.1    Kim, C.2    Li, S.3    Marchal, C.C.4    Towe, J.5    Atkinson, S.J.6    Dinauer, M.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.