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Volumn 827, Issue , 2012, Pages 305-317

Identification of new interacting partners for atypical Rho GTPases: A SILAC-based approach

Author keywords

Atypical Rho GTPases; Immunoprecipitation; Interactome; Mass spectrometry; Nu PAGE gradient gel; Protein overexpression; Proteomics; SILAC; Silver staining

Indexed keywords

AMINO ACID; RHO GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 84855870204     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-442-1_20     Document Type: Article
Times cited : (2)

References (54)
  • 1
    • 34648844192 scopus 로고    scopus 로고
    • Taking Rho GTPases to the next level: The cellular functions of atypical Rho GTPases
    • DOI 10.1016/j.yexcr.2007.07.022, PII S0014482707003588
    • Aspenstrom, P., Ruusala, A., and Pacholsky, D. (2007) Taking Rho GTPases to the next level: the cellular functions of atypical Rho GTPases. Exp Cell Res 313, 3673-3679. (Pubitemid 47464235)
    • (2007) Experimental Cell Research , vol.313 , Issue.17 , pp. 3673-3679
    • Aspenstrom, P.1    Ruusala, A.2    Pacholsky, D.3
  • 2
    • 77957272673 scopus 로고    scopus 로고
    • Rho and Ras GTPases in axon growth, guidance, and branching
    • Hall, A., and Lalli, G. (2010) Rho and Ras GTPases in axon growth, guidance, and branching. Cold Spring Harb Perspect Biol 2, a001818.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Hall, A.1    Lalli, G.2
  • 3
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: New insights into their functions from in vivo studies
    • Heasman, S.J., and Ridley, A.J. (2008) Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat Rev Mol Cell Biol 9, 690-701.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 4
    • 33748994545 scopus 로고    scopus 로고
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • DOI 10.1016/j.tcb.2006.08.006, PII S0962892406002236, Membrane Dynamics
    • Ridley, A.J. (2006) Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking. Trends Cell Biol 16, 522-529. (Pubitemid 44444995)
    • (2006) Trends in Cell Biology , vol.16 , Issue.10 , pp. 522-529
    • Ridley, A.J.1
  • 5
    • 70249085230 scopus 로고    scopus 로고
    • Rho family GTPases and their regulators in lymphocytes
    • Tybulewicz, V.L., and Henderson, R.B. (2009) Rho family GTPases and their regulators in lymphocytes. Nat Rev Immunol 9, 630-644.
    • (2009) Nat Rev Immunol , vol.9 , pp. 630-644
    • Tybulewicz, V.L.1    Henderson, R.B.2
  • 6
    • 44449178868 scopus 로고    scopus 로고
    • Rho GTPases in cancer cell biology
    • Vega, F.M., and Ridley, A.J. (2008) Rho GTPases in cancer cell biology. FEBS Lett 582, 2093-2101.
    • (2008) FEBS Lett , vol.582 , pp. 2093-2101
    • Vega, F.M.1    Ridley, A.J.2
  • 7
    • 4444240175 scopus 로고    scopus 로고
    • Wrch1 is a GTPase-deficient Cdc42-like protein with unusual binding characteristics and cellular effects
    • DOI 10.1016/j.yexcr.2004.05.029, PII S0014482704002927
    • Saras, J., Wollberg, P., and Aspenstrom, P. (2004) Wrch1 is a GTPase-deficient Cdc42-like protein with unusual binding characteristics and cellular effects. Exp Cell Res 299, 356-369. (Pubitemid 39179803)
    • (2004) Experimental Cell Research , vol.299 , Issue.2 , pp. 356-369
    • Saras, J.1    Wollberg, P.2    Aspenstrom, P.3
  • 8
    • 0942268723 scopus 로고    scopus 로고
    • Rho GTPases have diverse effects on the organization of the actin filament system
    • DOI 10.1042/BJ20031041
    • Aspenström, P., Fransson, A., and Saras, J. (2004) Rho GTPases have diverse effects on the organization of the actin filament system. Biochem J 377, 327-337. (Pubitemid 38142188)
    • (2004) Biochemical Journal , vol.377 , Issue.2 , pp. 327-337
    • Aspenstrom, P.1    Fransson, A.2    Saras, J.3
  • 9
    • 2342418629 scopus 로고    scopus 로고
    • Rho-family GTPases: It's not only Rac and Rho (and i like it)
    • DOI 10.1242/jcs.01118
    • Wennerberg, K., and Der, C.J. (2004) Rhofamily GTPases: it's not only Rac and Rho (and I like it). J Cell Sci 117, 1301-1312. (Pubitemid 38559808)
    • (2004) Journal of Cell Science , vol.117 , Issue.8 , pp. 1301-1312
    • Wennerberg, K.1    Der, C.J.2
  • 10
    • 33644843642 scopus 로고    scopus 로고
    • Function and regulation of Rnd proteins
    • DOI 10.1038/nrm1788, PII N1788
    • Chardin, P. (2006) Function and regulation of Rnd proteins. Nat Rev Mol Cell Biol 7, 54-62. (Pubitemid 43361572)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.1 , pp. 54-62
    • Chardin, P.1
  • 11
    • 17144379674 scopus 로고    scopus 로고
    • Critical and distinct roles of amino- and carboxyl-terminal sequences in regulation of the biological activity of the Chp atypical Rho GTPase
    • DOI 10.1074/jbc.M411300200
    • Chenette, E.J., Abo, A., and Der, C.J. (2005) Critical and distinct roles of amino- and carboxyl-terminal sequences in regulation of the biological activity of the Chp atypical Rho GTPase. J Biol Chem 280, 13784-13792. (Pubitemid 40517275)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.14 , pp. 13784-13792
    • Chenette, E.J.1    Abo, A.2    Der, C.J.3
  • 12
    • 55149099596 scopus 로고    scopus 로고
    • Characterization of RhoBTBdependent Cul3 ubiquitin ligase complexes - Evidence for an autoregulatory mechanism
    • Berthold, J., Schenkova, K., Ramos, S., Miura, Y., Furukawa, M., Aspenström, P., and Rivero, F. (2008) Characterization of RhoBTBdependent Cul3 ubiquitin ligase complexes-evidence for an autoregulatory mechanism. Exp Cell Res 314, 3453-3465.
    • (2008) Exp Cell Res , vol.314 , pp. 3453-3465
    • Berthold, J.1    Schenkova, K.2    Ramos, S.3    Miura, Y.4    Furukawa, M.5    Aspenström, P.6    Rivero, F.7
  • 13
    • 0036232358 scopus 로고    scopus 로고
    • Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers
    • DOI 10.1128/MCB.22.9.2952-2964.2002
    • Katoh, H., Harada, A., Mori, K., and Negishi, M. (2002) Socius is a novel Rnd GTPaseinteracting protein involved in disassembly of actin stress fibers. Mol Cell Biol 22, 2952-2964. (Pubitemid 34437454)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.9 , pp. 2952-2964
    • Katoh, H.1    Harada, A.2    Mori, K.3    Negishi, M.4
  • 15
    • 17144377069 scopus 로고    scopus 로고
    • RhoE function is regulated by ROCK I-mediated phosphorylation
    • DOI 10.1038/sj.emboj.7600612
    • Riento, K., Totty, N., Villalonga, P., Garg, R., Guasch, R., and Ridley, A.J. (2005) RhoE function is regulated by ROCK I-mediated phosphorylation. EMBO J 24, 1170-1180. (Pubitemid 40516600)
    • (2005) EMBO Journal , vol.24 , Issue.6 , pp. 1170-1180
    • Riento, K.1    Totty, N.2    Villalonga, P.3    Garg, R.4    Guasch, R.5    Ridley, A.J.6
  • 16
    • 27744567556 scopus 로고    scopus 로고
    • Interactome: Gateway into systems biology
    • DOI 10.1093/hmg/ddi335
    • Cusick, M.E., Klitgord, N., Vidal, M., and Hill, D.E. (2005) Interactome: gateway into systems biology. Hum Mol Genet 14 Spec No. 2, R171-181. (Pubitemid 41631885)
    • (2005) Human Molecular Genetics , vol.14 , Issue.SUPPL. 2
    • Cusick, M.E.1    Klitgord, N.2    Vidal, M.3    Hill, D.E.4
  • 17
    • 0037326081 scopus 로고    scopus 로고
    • Mass spectrometric-based approaches in quantitative proteomics
    • DOI 10.1016/S1046-2023(02)00303-1, PII S1046202302003031
    • Ong, S.E., Foster, L.J., and Mann, M. (2003) Mass spectrometric-based approaches in quantitative proteomics. Methods 29, 124-130. (Pubitemid 36269199)
    • (2003) Methods , vol.29 , Issue.2 , pp. 124-130
    • Ong, S.-E.1    Foster, L.J.2    Mann, M.3
  • 18
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong, S.E., and Mann, M. (2006) A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat Protoc 1, 2650-2660.
    • (2006) Nat Protoc , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 19
    • 34250372908 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture for quantitative proteomics
    • DOI 10.1385/1-59745-255-6:37, Quantitative Proteomics by Mass Spectrometry
    • Ong, S. E., and Mann, M. (2007) Stable isotope labeling by amino acids in cell culture for quantitative proteomics. Methods Mol Biol 359, 37-52. (Pubitemid 350183220)
    • (2007) Methods in Molecular Biology , vol.359 , pp. 37-52
    • Ong, S.-E.1    Mann, M.2
  • 20
    • 30744464873 scopus 로고    scopus 로고
    • Insulin-dependent interactions of proteins with GLUT4 revealed through stable isotope labeling by amino acids in cell culture (SILAC)
    • DOI 10.1021/pr0502626
    • Foster, L.J., Rudich, A., Talior, I., Patel, N., Huang, X., Furtado, L.M., Bilan, P.J., Mann, M., and Klip, A. (2006) Insulin-dependent interactions of proteins with GLUT4 revealed through stable isotope labeling by amino acids in cell culture (SILAC). J Proteome Res 5, 64-75. (Pubitemid 43100798)
    • (2006) Journal of Proteome Research , vol.5 , Issue.1 , pp. 64-75
    • Foster, L.J.1    Rudich, A.2    Talior, I.3    Patel, N.4    Huang, X.5    Furtado, L.M.6    Bilan, P.J.7    Mann, M.8    Klip, A.9
  • 21
    • 33845329203 scopus 로고    scopus 로고
    • Functional and quantitative proteomics using SILAC
    • DOI 10.1038/nrm2067, PII NRM2067
    • Mann, M. (2006) Functional and quantitative proteomics using SILAC. Nat Rev Mol Cell Biol 7, 952-958. (Pubitemid 44871421)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.12 , pp. 952-958
    • Mann, M.1
  • 22
    • 33751230224 scopus 로고    scopus 로고
    • Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK)
    • DOI 10.1038/nmeth972, PII NMETH972
    • Selbach, M., and Mann, M. (2006) Protein interaction screening by quantitative immunoprecipitation combined with knockdown (QUICK). Nat Methods 3, 981-983. (Pubitemid 44782696)
    • (2006) Nature Methods , vol.3 , Issue.12 , pp. 981-983
    • Selbach, M.1    Mann, M.2
  • 23
    • 40849108777 scopus 로고    scopus 로고
    • Mapping the integrin-linked kinase interactome using SILAC
    • Dobreva, I., Fielding, A., Foster, L.J., and Dedhar, S. (2008) Mapping the integrin-linked kinase interactome using SILAC. J Proteome Res 7, 1740-1749.
    • (2008) J Proteome Res , vol.7 , pp. 1740-1749
    • Dobreva, I.1    Fielding, A.2    Foster, L.J.3    Dedhar, S.4
  • 26
    • 65649154049 scopus 로고    scopus 로고
    • StatQuant: A post-quantification analysis toolbox for improving quantitative mass spectrometry
    • van Breukelen, B., van den Toorn, H.W., Drugan, M.M., and Heck, A.J. (2009) StatQuant: a post-quantification analysis toolbox for improving quantitative mass spectrometry. Bioinformatics 25, 1472-1473.
    • (2009) Bioinformatics , vol.25 , pp. 1472-1473
    • Van Breukelen, B.1    Van Den Toorn, H.W.2    Drugan, M.M.3    Heck, A.J.4
  • 27
    • 33646117742 scopus 로고    scopus 로고
    • The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking
    • Fransson, S., Ruusala, A., and Aspenström, P. (2006) The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking. Biochem Biophys Res Commun 344, 500-510.
    • (2006) Biochem Biophys Res Commun , vol.344 , pp. 500-510
    • Fransson, S.1    Ruusala, A.2    Aspenström, P.3
  • 28
    • 64549112144 scopus 로고    scopus 로고
    • Pink1 forms a multiprotein complex with Miro and Milton, linking Pink1 function to mitochondrial trafficking
    • Weihofen, A., Thomas, K.J., Ostaszewski, B.L., Cookson, M.R., and Selkoe, D.J. (2009) Pink1 forms a multiprotein complex with Miro and Milton, linking Pink1 function to mitochondrial trafficking. Biochemistry 48, 2045-2052.
    • (2009) Biochemistry , vol.48 , pp. 2045-2052
    • Weihofen, A.1    Thomas, K.J.2    Ostaszewski, B.L.3    Cookson, M.R.4    Selkoe, D.J.5
  • 29
    • 1942434716 scopus 로고    scopus 로고
    • RhoBTB2 is a substrate of the mammalian Cul3 ubiquitin ligase complex
    • DOI 10.1101/gad.1177904
    • Wilkins, A., Ping, Q., and Carpenter, C.L. (2004) RhoBTB2 is a substrate of the mammalian Cul3 ubiquitin ligase complex. Genes Dev 18, 856-861. (Pubitemid 38529655)
    • (2004) Genes and Development , vol.18 , Issue.8 , pp. 856-861
    • Wilkins, A.1    Ping, Q.2    Carpenter, C.L.3
  • 30
    • 65849408332 scopus 로고    scopus 로고
    • RhoBTB3: A Rho GTPasefamily ATPase required for endosome to Golgi transport
    • Espinosa, E.J., Calero, M., Sridevi, K., and Pfeffer, S.R. (2009) RhoBTB3: a Rho GTPasefamily ATPase required for endosome to Golgi transport. Cell 137, 938-948.
    • (2009) Cell , vol.137 , pp. 938-948
    • Espinosa, E.J.1    Calero, M.2    Sridevi, K.3    Pfeffer, S.R.4
  • 31
    • 0037341806 scopus 로고    scopus 로고
    • RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase
    • DOI 10.1038/ncb935
    • Gasman, S., Kalaidzidis, Y., and Zerial, M. (2003) RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase. Nat Cell Biol 5, 195-204. (Pubitemid 36322245)
    • (2003) Nature Cell Biology , vol.5 , Issue.3 , pp. 195-204
    • Gasman, S.1    Kalaidzidis, Y.2    Zerial, M.3
  • 32
    • 0037080330 scopus 로고    scopus 로고
    • Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor activity in semaphorin 3A-induced cytoskeletal collapse
    • Zanata, S.M., Hovatta, I., Rohm, B., and Puschel, A.W. (2002) Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor activity in Semaphorin 3A-induced cytoskeletal collapse. J Neurosci 22, 471-477. (Pubitemid 34049085)
    • (2002) Journal of Neuroscience , vol.22 , Issue.2 , pp. 471-477
    • Zanata, S.M.1    Hovatta, I.2    Rohm, B.3    Puschel, A.W.4
  • 33
    • 77957763767 scopus 로고    scopus 로고
    • RhoH modulates pre-TCR and TCR signalling by regulating LCK
    • Wang, H., Zeng, X., Fan, Z., and Lim, B. (2011) RhoH modulates pre-TCR and TCR signalling by regulating LCK. Cell Signal 23, 249-258.
    • (2011) Cell Signal , vol.23 , pp. 249-258
    • Wang, H.1    Zeng, X.2    Fan, Z.3    Lim, B.4
  • 35
    • 33750121336 scopus 로고    scopus 로고
    • RhoH GTPase recruits and activates Zap70 required for T cell receptor signaling and thymocyte development
    • DOI 10.1038/ni1396, PII NI1396
    • Gu, Y., Chae, H.D., Siefring, J.E., Jasti, A.C., Hildeman, D.A., and Williams, D.A. (2006) RhoH GTPase recruits and activates Zap70 required for T cell receptor signaling and thymocyte development. Nat Immunol 7, 1182-1190. (Pubitemid 44594314)
    • (2006) Nature Immunology , vol.7 , Issue.11 , pp. 1182-1190
    • Gu, Y.1    Chae, H.-D.2    Siefring, J.E.3    Jasti, A.C.4    Hildeman, D.A.5    Williams, D.A.6
  • 36
    • 77956633945 scopus 로고    scopus 로고
    • Regulation of the Rho family small GTPase Wrch-1/RhoU by C-terminal tyrosine phosphorylation requires Src
    • Alan, J.K., Berzat, A.C., Dewar, B.J., Graves, L.M., and Cox, A.D.(2010) Regulation of the Rho family small GTPase Wrch-1/RhoU by C-terminal tyrosine phosphorylation requires Src. Mol Cell Biol 30, 4324-4338.
    • (2010) Mol Cell Biol , vol.30 , pp. 4324-4338
    • Alan, J.K.1    Berzat, A.C.2    Dewar, B.J.3    Graves, L.M.4    Cox, A.D.5
  • 37
    • 77949801029 scopus 로고    scopus 로고
    • Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/ Milton complex
    • Misko, A., Jiang, S., Wegorzewska, I., Milbrandt, J., and Baloh, R.H. (2010) Mitofusin 2 is necessary for transport of axonal mitochondria and interacts with the Miro/ Milton complex. J Neurosci 30, 4232-4240.
    • (2010) J Neurosci , vol.30 , pp. 4232-4240
    • Misko, A.1    Jiang, S.2    Wegorzewska, I.3    Milbrandt, J.4    Baloh, R.H.5
  • 38
    • 59449093560 scopus 로고    scopus 로고
    • The transforming Rho family GTPase Wrch-1 disrupts epithelial cell tight junctions and epithelial morphogenesis
    • Brady, D.C., Alan, J.K., Madigan, J.P., Fanning, A.S., and Cox, A.D. (2009) The transforming Rho family GTPase Wrch-1 disrupts epithelial cell tight junctions and epithelial morphogenesis. Mol Cell Biol 29, 1035-1049.
    • (2009) Mol Cell Biol , vol.29 , pp. 1035-1049
    • Brady, D.C.1    Alan, J.K.2    Madigan, J.P.3    Fanning, A.S.4    Cox, A.D.5
  • 39
    • 40749157168 scopus 로고    scopus 로고
    • The atypical Rho GTPase Wrch1 collaborates with the nonreceptor tyrosine kinases Pyk2 and Src in regulating cytoskeletal dynamics
    • Ruusala, A., and Aspenström, P. (2008) The atypical Rho GTPase Wrch1 collaborates with the nonreceptor tyrosine kinases Pyk2 and Src in regulating cytoskeletal dynamics. Mol Cell Biol 28, 1802-1814.
    • (2008) Mol Cell Biol , vol.28 , pp. 1802-1814
    • Ruusala, A.1    Aspenström, P.2
  • 40
    • 24044544231 scopus 로고    scopus 로고
    • Direct interaction of Rnd1 with FRS2β regulates Rnd1-induced down-regulation of RhoA activity and is involved in fibroblast growth factor-induced neurite outgrowth in PC12 cells
    • DOI 10.1074/jbc.M411356200
    • Harada, A., Katoh, H., and Negishi, M. (2005) Direct interaction of Rnd1 with FRS2 beta regulates Rnd1-induced down-regulation of RhoA activity and is involved in fibroblast growth factor-induced neurite outgrowth in PC12 cells. J Biol Chem 280, 18418-18424. (Pubitemid 41389091)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.18 , pp. 18418-18424
    • Harada, A.1    Katoh, H.2    Negishi, M.3
  • 41
    • 0342545998 scopus 로고    scopus 로고
    • Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family
    • DOI 10.1016/S0014-5793(99)01530-6, PII S0014579399015306
    • Vayssiere, B., Zalcman, G., Mahe, Y., Mirey, G., Ligensa, T., Weidner, K.M., Chardin, P., and Camonis, J. (2000) Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family. FEBS Lett 467, 91-96. (Pubitemid 30069549)
    • (2000) FEBS Letters , vol.467 , Issue.1 , pp. 91-96
    • Vayssiere, B.1    Zalcman, G.2    Mahe, Y.3    Mirey, G.4    Ligensa, T.5    Weidner, K.M.6    Chardin, P.7    Camonis, J.8
  • 43
    • 0038491273 scopus 로고    scopus 로고
    • Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells
    • DOI 10.1074/jbc.M303047200
    • Oinuma, I., Katoh, H., Harada, A., and Negishi, M. (2003) Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEFmediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells. J Biol Chem 278, 25671-25677. (Pubitemid 36835322)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 25671-25677
    • Oinuma, I.1    Katoh, H.2    Harada, A.3    Negishi, M.4
  • 44
    • 37549021146 scopus 로고    scopus 로고
    • Binding of Rac1, Rnd1, and RhoD to a novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain
    • Tong, Y., Chugha, P., Hota, P.K., Alviani, R.S., Li, M., Tempel, W., Shen, L., Park, H.W., and Buck, M. (2007) Binding of Rac1, Rnd1, and RhoD to a novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain. J Biol Chem 282, 37215-37224.
    • (2007) J Biol Chem , vol.282 , pp. 37215-37224
    • Tong, Y.1    Chugha, P.2    Hota, P.K.3    Alviani, R.S.4    Li, M.5    Tempel, W.6    Shen, L.7    Park, H.W.8    Buck, M.9
  • 45
    • 58649116718 scopus 로고    scopus 로고
    • Rnd1 regulates axon extension by enhancing the microtubule destabilizing activity of SCG10
    • Li, Y.H., Ghavampur, S., Bondallaz, P., Will, L., Grenningloh, G., and Puschel, A.W. (2009) Rnd1 regulates axon extension by enhancing the microtubule destabilizing activity of SCG10. J Biol Chem 284, 363-371.
    • (2009) J Biol Chem , vol.284 , pp. 363-371
    • Li, Y.H.1    Ghavampur, S.2    Bondallaz, P.3    Will, L.4    Grenningloh, G.5    Puschel, A.W.6
  • 49
    • 65449122789 scopus 로고    scopus 로고
    • Different requirement for Rnd GTPases of R-Ras GAP activity of Plexin-C1 and Plexin-D1
    • Uesugi, K., Oinuma, I., Katoh, H., and Negishi, M. (2009) Different requirement for Rnd GTPases of R-Ras GAP activity of Plexin-C1 and Plexin-D1. J Biol Chem 284, 6743-6751.
    • (2009) J Biol Chem , vol.284 , pp. 6743-6751
    • Uesugi, K.1    Oinuma, I.2    Katoh, H.3    Negishi, M.4
  • 50
    • 33744549035 scopus 로고    scopus 로고
    • Pragmin, a novel effector of Rnd2 GTPase, Stimulates RhoA activity
    • DOI 10.1074/jbc.M511314200
    • Tanaka, H., Katoh, H., and Negishi, M. (2006) Pragmin, a novel effector of Rnd2 GTPase, stimulates RhoA activity. J Biol Chem 281, 10355-10364. (Pubitemid 43864574)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.15 , pp. 10355-10364
    • Tanaka, H.1    Katoh, H.2    Negishi, M.3
  • 51
    • 0037160026 scopus 로고    scopus 로고
    • Rapostlin is a novel effector of Rnd2 GTPase inducing neurite branching
    • DOI 10.1074/jbc.M208090200
    • Fujita, H., Katoh, H., Ishikawa, Y., Mori, K., and Negishi, M. (2002) Rapostlin is a novel effector of Rnd2 GTPase inducing neurite branching. J Biol Chem 277, 45428-45434. (Pubitemid 36159151)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.47 , pp. 45428-45434
    • Fujita, H.1    Katoh, H.2    Ishikawa, Y.3    Mori, K.4    Negishi, M.5
  • 52
    • 0037101784 scopus 로고    scopus 로고
    • Vps4-A (vacuolar protein sorting 4-A) is a binding partner for a novel Rho family GTpase, Rnd2
    • DOI 10.1042/BJ20020062
    • Tanaka, H., Fujita, H., Katoh, H., Mori, K., and Negishi, M. (2002) Vps4-A (vacuolar protein sorting 4-A) is a binding partner for a novel Rho family GTPase, Rnd2. Biochem J 365, 349-353. (Pubitemid 36135307)
    • (2002) Biochemical Journal , vol.365 , Issue.2 , pp. 349-353
    • Tanaka, H.1    Fujita, H.2    Katoh, H.3    Mori, K.4    Negishi, M.5
  • 53
    • 0038655599 scopus 로고    scopus 로고
    • RhoE binds to ROCK I and inhibits downstream signaling
    • DOI 10.1128/MCB.23.12.4219-4229.2003
    • Riento, K., Guasch, R.M., Garg, R., Jin, B., and Ridley, A.J. (2003) RhoE binds to ROCK I and inhibits downstream signaling. Mol Cell Biol 23, 4219-4229. (Pubitemid 36666425)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.12 , pp. 4219-4229
    • Riento, K.1    Guasch, R.M.2    Garg, R.3    Jin, B.4    Ridley, A.J.5
  • 54
    • 77957878007 scopus 로고    scopus 로고
    • The RhoA GEF Syx is a target of Rnd3 and regulated via a Raf1-like ubiquitin-related domain
    • Goh, L. L., and Manser, E. (2010) The RhoA GEF Syx is a target of Rnd3 and regulated via a Raf1-like ubiquitin-related domain. PLoS One 5, e12409.
    • (2010) PLoS One , vol.5
    • Goh, L.L.1    Manser, E.2


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