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Volumn 34, Issue 2, 2009, Pages 223-233

Structural Insights into Formation of an Active Signaling Complex between Rac and Phospholipase C Gamma 2

Author keywords

SIGNALING

Indexed keywords

EPIDERMAL GROWTH FACTOR; GUANOSINE DIPHOSPHATE; PHOSPHOLIPASE C GAMMA2; PLECKSTRIN; RAC2 PROTEIN;

EID: 64749102105     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2009.02.023     Document Type: Article
Times cited : (64)

References (39)
  • 1
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop A.L., and 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
  • 2
    • 34249018367 scopus 로고    scopus 로고
    • GEFs and GAPs: critical elements in the control of small G proteins
    • Bos J.L., Rehmann H., and Wittinghofer A. GEFs and GAPs: critical elements in the control of small G proteins. Cell 129 (2007) 865-877
    • (2007) Cell , vol.129 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 4
    • 34247175312 scopus 로고    scopus 로고
    • GTP-binding proteins of the Rho/Rac family: regulation, effectors and functions in vivo
    • Bustelo X.R., Sauzeau V., and Berenjeno I.M. GTP-binding proteins of the Rho/Rac family: regulation, effectors and functions in vivo. Bioessays 29 (2007) 356-370
    • (2007) Bioessays , vol.29 , pp. 356-370
    • Bustelo, X.R.1    Sauzeau, V.2    Berenjeno, I.M.3
  • 5
    • 1842301722 scopus 로고    scopus 로고
    • Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPgammaS
    • Cherfils J., Menetrey J., Le Bras G., Janoueix-Lerosey I., de Gunzburg J., Garel J.R., and Auzat I. Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPgammaS. EMBO J. 16 (1997) 5582-5591
    • (1997) EMBO J. , vol.16 , pp. 5582-5591
    • Cherfils, J.1    Menetrey, J.2    Le Bras, G.3    Janoueix-Lerosey, I.4    de Gunzburg, J.5    Garel, J.R.6    Auzat, I.7
  • 6
    • 11144219896 scopus 로고    scopus 로고
    • Always look on the bright site of Rho: structural implications for a conserved intermolecular interface
    • Dvorsky R., and Ahmadian M.R. Always look on the bright site of Rho: structural implications for a conserved intermolecular interface. EMBO Rep. 5 (2004) 1130-1136
    • (2004) EMBO Rep. , vol.5 , pp. 1130-1136
    • Dvorsky, R.1    Ahmadian, M.R.2
  • 7
    • 0037416217 scopus 로고    scopus 로고
    • Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6
    • Garrard S.M., Capaldo C.T., Gao L., Rosen M.K., Macara I.G., and Tomchick D.R. Structure of Cdc42 in a complex with the GTPase-binding domain of the cell polarity protein, Par6. EMBO J. 22 (2003) 1125-1133
    • (2003) EMBO J. , vol.22 , pp. 1125-1133
    • Garrard, S.M.1    Capaldo, C.T.2    Gao, L.3    Rosen, M.K.4    Macara, I.G.5    Tomchick, D.R.6
  • 8
    • 0037308836 scopus 로고    scopus 로고
    • Ras-effector interactions: after one decade
    • Herrmann C. Ras-effector interactions: after one decade. Curr. Opin. Struct. Biol. 13 (2003) 122-129
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 122-129
    • Herrmann, C.1
  • 9
    • 0029913467 scopus 로고    scopus 로고
    • Differential interaction of the Ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor
    • Herrmann C., Horn G., Spaargaren M., and Wittinghofer A. Differential interaction of the Ras family GTP-binding proteins H-Ras, Rap1A, and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor. J. Biol. Chem. 271 (1996) 6794-6800
    • (1996) J. Biol. Chem. , vol.271 , pp. 6794-6800
    • Herrmann, C.1    Horn, G.2    Spaargaren, M.3    Wittinghofer, A.4
  • 11
    • 0037474209 scopus 로고    scopus 로고
    • Specificity and structural requirements of phospholipase C-beta stimulation by Rho GTPases versus G protein beta/gamma dimers
    • Illenberger D., Walliser C., Nurnberg B., Diaz Lorente M., and Gierschik P. Specificity and structural requirements of phospholipase C-beta stimulation by Rho GTPases versus G protein beta/gamma dimers. J. Biol. Chem. 278 (2003) 3006-3014
    • (2003) J. Biol. Chem. , vol.278 , pp. 3006-3014
    • Illenberger, D.1    Walliser, C.2    Nurnberg, B.3    Diaz Lorente, M.4    Gierschik, P.5
  • 12
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: biochemistry and biology
    • Jaffe A.B., and Hall A. Rho GTPases: biochemistry and biology. Annu. Rev. Cell Dev. Biol. 21 (2005) 247-269
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 14
    • 21844443829 scopus 로고    scopus 로고
    • Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase
    • Jin R., Junutula J.R., Matern H.T., Ervin K.E., Scheller R.H., and Brunger A.T. Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase. EMBO J. 24 (2005) 2064-2074
    • (2005) EMBO J. , vol.24 , pp. 2064-2074
    • Jin, R.1    Junutula, J.R.2    Matern, H.T.3    Ervin, K.E.4    Scheller, R.H.5    Brunger, A.T.6
  • 15
    • 33644840483 scopus 로고    scopus 로고
    • New insights into the families of PLC enzymes: looking back and going forward
    • Katan M. New insights into the families of PLC enzymes: looking back and going forward. Biochem. J. 391 (2005) e7-e9
    • (2005) Biochem. J. , vol.391
    • Katan, M.1
  • 16
    • 27544475993 scopus 로고    scopus 로고
    • Rac3-mediated transformation requires multiple effector pathways
    • Keller P.J., Gable C.M., Wing M.R., and Cox A.D. Rac3-mediated transformation requires multiple effector pathways. Cancer Res. 65 (2005) 9883-9890
    • (2005) Cancer Res. , vol.65 , pp. 9883-9890
    • Keller, P.J.1    Gable, C.M.2    Wing, M.R.3    Cox, A.D.4
  • 17
    • 50649096663 scopus 로고    scopus 로고
    • Analyzing protein interaction networks using structural information
    • Kiel C., Beltrao P., and Serrano L. Analyzing protein interaction networks using structural information. Annu. Rev. Biochem. 77 (2008) 415-441
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 415-441
    • Kiel, C.1    Beltrao, P.2    Serrano, L.3
  • 18
    • 8744219635 scopus 로고    scopus 로고
    • Pleckstrin homology domains: not just for phosphoinositides
    • Lemmon M.A. Pleckstrin homology domains: not just for phosphoinositides. Biochem. Soc. Trans. 32 (2004) 707-711
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 707-711
    • Lemmon, M.A.1
  • 19
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins
    • Milburn M.V., Tong L., deVos A.M., Brunger A., Yamaizumi Z., Nishimura S., and Kim S.H. Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins. Science 247 (1990) 939-945
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Tong, L.2    deVos, A.M.3    Brunger, A.4    Yamaizumi, Z.5    Nishimura, S.6    Kim, S.H.7
  • 20
    • 0029024547 scopus 로고
    • Isolation of protein prenyltransferases from bovine brain and baculovirus expression system
    • Moomaw J.F., Zhang F.L., and Casey P.J. Isolation of protein prenyltransferases from bovine brain and baculovirus expression system. Methods Enzymol. 250 (1995) 12-21
    • (1995) Methods Enzymol. , vol.250 , pp. 12-21
    • Moomaw, J.F.1    Zhang, F.L.2    Casey, P.J.3
  • 22
    • 0029107760 scopus 로고
    • The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue
    • Nassar N., Horn G., Herrmann C., Scherer A., McCormick F., and Wittinghofer A. The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature 375 (1995) 554-560
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Scherer, A.4    McCormick, F.5    Wittinghofer, A.6
  • 23
    • 0027132717 scopus 로고
    • The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S
    • Noel J.P., Hamm H.E., and Sigler P.B. The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S. Nature 366 (1993) 654-663
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 24
    • 46649087194 scopus 로고    scopus 로고
    • Effector proteins exert an important influence on the signaling-active state of the small GTPase Cdc42
    • Phillips M.J., Calero G., Chan B., Ramachandran S., and Cerione R.A. Effector proteins exert an important influence on the signaling-active state of the small GTPase Cdc42. J. Biol. Chem. 283 (2008) 14153-14164
    • (2008) J. Biol. Chem. , vol.283 , pp. 14153-14164
    • Phillips, M.J.1    Calero, G.2    Chan, B.3    Ramachandran, S.4    Cerione, R.A.5
  • 27
    • 0033779101 scopus 로고    scopus 로고
    • Structure, function, and control of phosphoinositide-specific phospholipase C
    • Rebecchi M.J., and Pentyala S.N. Structure, function, and control of phosphoinositide-specific phospholipase C. Physiol. Rev. 80 (2000) 1291-1335
    • (2000) Physiol. Rev. , vol.80 , pp. 1291-1335
    • Rebecchi, M.J.1    Pentyala, S.N.2
  • 28
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of phophoinositide-specific phospholipase C
    • Rhee S.-G. Regulation of phophoinositide-specific phospholipase C. Annu. Rev. Biochem. 70 (2001) 281-312
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 281-312
    • Rhee, S.-G.1
  • 29
    • 33748994545 scopus 로고    scopus 로고
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • Ridley A.J. Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking. Trends Cell Biol. 16 (2006) 522-529
    • (2006) Trends Cell Biol. , vol.16 , pp. 522-529
    • Ridley, A.J.1
  • 31
    • 12444279041 scopus 로고    scopus 로고
    • Signaling properties and expression in normal and tumor tissues of two phospholipase C epsilon splice variants
    • Sorli S.C., Bunney T.D., Sugden P.H., Paterson H.F., and Katan M. Signaling properties and expression in normal and tumor tissues of two phospholipase C epsilon splice variants. Oncogene 24 (2005) 90-100
    • (2005) Oncogene , vol.24 , pp. 90-100
    • Sorli, S.C.1    Bunney, T.D.2    Sugden, P.H.3    Paterson, H.F.4    Katan, M.5
  • 33
    • 0035837426 scopus 로고    scopus 로고
    • The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways
    • Tarricone C., Xiao B., Justin N., Walker P.A., Rittinger K., Gamblin S.J., and Smerdon S.J. The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. Nature 411 (2001) 215-219
    • (2001) Nature , vol.411 , pp. 215-219
    • Tarricone, C.1    Xiao, B.2    Justin, N.3    Walker, P.A.4    Rittinger, K.5    Gamblin, S.J.6    Smerdon, S.J.7
  • 34
    • 0029023942 scopus 로고
    • Rho family GTPases bind to phosphoinositide kinases
    • Tolias K.F., Cantley L.C., and Carpenter C.L. Rho family GTPases bind to phosphoinositide kinases. J. Biol. Chem. 270 (1995) 17656-17659
    • (1995) J. Biol. Chem. , vol.270 , pp. 17656-17659
    • Tolias, K.F.1    Cantley, L.C.2    Carpenter, C.L.3
  • 35
    • 0033522118 scopus 로고    scopus 로고
    • Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport
    • Vetter I.R., Nowak C., Nishimoto T., Kuhlmann J., and Wittinghofer A. Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport. Nature 398 (1999) 39-46
    • (1999) Nature , vol.398 , pp. 39-46
    • Vetter, I.R.1    Nowak, C.2    Nishimoto, T.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 36
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter I.R., and Wittinghofer A. The guanine nucleotide-binding switch in three dimensions. Science 294 (2001) 1299-1304
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2


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