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Volumn 288, Issue 6, 2013, Pages 4486-4500

Deciphering the molecular and functional basis of Dbl family proteins: A novel systematic approach toward classification of selective activation of the Rho family proteins

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; B-CELL LYMPHOMA; CARDIO-VASCULAR DISEASE; CATALYTIC EFFICIENCIES; CELL POLARITY; CELLULAR PROCESS; FUNCTIONAL BASIS; FUNCTIONAL PROPERTIES; GUANINE NUCLEOTIDE EXCHANGE FACTORS; META-ANALYSIS; NUCLEOTIDE EXCHANGE; PROTEIN FAMILY; RHO FAMILY; RHO PROTEINS; SELECTIVE ACTIVATION; SUBSTRATE SELECTIVITY; VASCULAR SMOOTH MUSCLE CELLS;

EID: 84873676027     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.429746     Document Type: Article
Times cited : (87)

References (91)
  • 1
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville, S., and Hall, A. (2002) Rho GTPases in cell biology. Nature 420, 629-635
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 2
    • 33748994545 scopus 로고    scopus 로고
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • Ridley, A. J. (2006) Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking. Trends Cell Biol. 16, 522-529
    • (2006) Trends Cell Biol. , vol.16 , pp. 522-529
    • Ridley, A.J.1
  • 3
    • 0034574572 scopus 로고    scopus 로고
    • Rho GTPases in neuronal morphogenesis
    • Luo, L. (2000) Rho GTPases in neuronal morphogenesis. Nat. Rev. Neu-rosci. 1, 173-180
    • (2000) Nat. Rev. Neu-rosci. , vol.1 , pp. 173-180
    • Luo, L.1
  • 4
    • 33750935902 scopus 로고    scopus 로고
    • Regulators of Rho GTPases in neuronal development
    • Watabe-Uchida, M., Govek, E. E., and Van Aelst, L. (2006) Regulators of Rho GTPases in neuronal development. Neurosci. 26, 10633-10635
    • (2006) Neurosci. , vol.26 , pp. 10633-10635
    • Watabe-Uchida, M.1    Govek, E.E.2    Van Aelst, L.3
  • 5
    • 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 Harbor Perspect. Biol. 2, a001818
    • (2010) Cold Spring Harbor Perspect. Biol. , vol.2
    • Hall, A.1    Lalli, G.2
  • 7
    • 0036191304 scopus 로고    scopus 로고
    • Rho GTPases in transformation and metastasis
    • Jaffe, A. B., and Hall, A. (2002) Rho GTPases in transformation and metastasis. Adv. Cancer Res. 84, 57-80
    • (2002) Adv. Cancer Res. , vol.84 , pp. 57-80
    • Jaffe, A.B.1    Hall, A.2
  • 8
    • 2342418629 scopus 로고    scopus 로고
    • Rho-family GTPases. It's not only Rac and Rho (and i like it)
    • Wennerberg, K., and Der, C. J. (2004) Rho-family GTPases. It's not only Rac and Rho (and I like it). Cell Sei. 117, 1301-1312
    • (2004) Cell Sei. , vol.117 , pp. 1301-1312
    • Wennerberg, K.1    Der, C.J.2
  • 9
    • 79959393264 scopus 로고    scopus 로고
    • Structure-function relationships of the G domain, a canonical switch motif
    • Wittinghofer, A., and Vetter, I. R. (2011) Structure-function relationships of the G domain, a canonical switch motif. Annu. Rev. Biochem. 80, 943-971
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 943-971
    • Wittinghofer, A.1    Vetter, I.R.2
  • 10
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and D'Souza-Schorey, C. (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
  • 11
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter, I. R., and Wittinghofer, A. (2001) The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 12
    • 0036644975 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors for Rho GTPases. Turning on the switch
    • Schmidt, A., and Hall, A. (2002) Guanine nucleotide exchange factors for Rho GTPases. Turning on the switch. Genes Dev. 16, 1587-1609
    • (2002) Genes Dev. , vol.16 , pp. 1587-1609
    • Schmidt, A.1    Hall, A.2
  • 13
    • 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. (2004) Always look on the bright site of Rho. Structural implications for a conserved intermolecular interface. EMBORep. 5, 1130-1136
    • (2004) EMBORep. , vol.5 , pp. 1130-1136
    • Dvorsky, R.1    Ahmadian, M.R.2
  • 14
    • 13444252631 scopus 로고    scopus 로고
    • GEF means go. Turning on RHO GTPases with guanine nucleotide-exchange factors
    • Rossman, K. L., Der, C. J., and Sondek, J. (2005) GEF means go. Turning on RHO GTPases with guanine nucleotide-exchange factors. Nat. Rev. Mol. Cell Biol. 6, 167-180
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 167-180
    • Rossman, K.L.1    Der, C.J.2    Sondek, J.3
  • 15
    • 0037213689 scopus 로고    scopus 로고
    • Rho GTPase-activating proteins in cell regulation
    • Moon, S. Y., and Zheng, Y. (2003) Rho GTPase-activating proteins in cell regulation. Trends Cell Biol. 13, 13-22
    • (2003) Trends Cell Biol. , vol.13 , pp. 13-22
    • Moon, S.Y.1    Zheng, Y.2
  • 17
    • 77449149247 scopus 로고    scopus 로고
    • Snapshots form a big picture of guanine nucleotide exchange
    • Rittinger, K. (2009) Snapshots form a big picture of guanine nucleotide exchange. Sei. Signal. 2, pe63
    • (2009) Sei. Signal. , vol.2
    • Rittinger, K.1
  • 19
    • 0942279704 scopus 로고    scopus 로고
    • Structural elements, mechanism, and evolutionary convergence of Rho protein-guanine nucleotide exchange factor complexes
    • Erickson, J. W., and Cerione, R. A. (2004) Structural elements, mechanism, and evolutionary convergence of Rho protein-guanine nucleotide exchange factor complexes. Biochemistry 43, 837-842
    • (2004) Biochemistry , vol.43 , pp. 837-842
    • Erickson, J.W.1    Cerione, R.A.2
  • 20
    • 16244413928 scopus 로고    scopus 로고
    • Larger than Dbl. New structural insights into RhoA activation
    • Rossman, K. L., and Sondek, J. (2005) Larger than Dbl. New structural insights into RhoA activation. Trends Biochem. Sei. 30, 163-165
    • (2005) Trends Biochem. Sei. , vol.30 , pp. 163-165
    • Rossman, K.L.1    Sondek, J.2
  • 21
    • 74549193568 scopus 로고    scopus 로고
    • Structure and function of heterotrimeric G protein-regulated Rho guanine nucleotide exchange factors
    • Aittaleb, M., Boguth, C. A., and Tesmer, J. J. (2010) Structure and function of heterotrimeric G protein-regulated Rho guanine nucleotide exchange factors. Mol. Pharmacol. 77, 111-125
    • (2010) Mol. Pharmacol. , vol.77 , pp. 111-125
    • Aittaleb, M.1    Boguth, C.A.2    Tesmer, J.J.3
  • 22
    • 0035668525 scopus 로고    scopus 로고
    • Dbl family guanine nucleotide exchange factors
    • Zheng, Y. (2001) Dbl family guanine nucleotide exchange factors. Trends Biochem. Sei. 26, 724-732
    • (2001) Trends Biochem. Sei. , vol.26 , pp. 724-732
    • Zheng, Y.1
  • 23
    • 79952047916 scopus 로고    scopus 로고
    • Rho-guanine nucleotide exchange factors during development. Force is nothing without control
    • Mulinari, S., and Hacker, U. (2010) Rho-guanine nucleotide exchange factors during development. Force is nothing without control. Small GTPases 1, 28-43
    • (2010) Small GTPases , vol.1 , pp. 28-43
    • Mulinari, S.1    Hacker, U.2
  • 25
    • 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. (2007) GEFs and GAPs. Critical elements in the control of small G proteins. Cell 129, 865-877
    • (2007) Cell , vol.129 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 26
    • 78649487698 scopus 로고    scopus 로고
    • Ras superfamily GEFs and GAPs. Validated and tractable targets for cancer therapy?
    • Vigil, D., Cherfils, J., Rossman, K. L., and Der, C. J. (2010) Ras superfamily GEFs and GAPs. Validated and tractable targets for cancer therapy? Nat. Rev. Cancer 10, 842-857
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 842-857
    • Vigil, D.1    Cherfils, J.2    Rossman, K.L.3    Der, C.J.4
  • 28
    • 0037138364 scopus 로고    scopus 로고
    • Signaling to the Rho GTPases. Networking with the DH domain
    • Hoffman, G. R., and Cerione, R. A. (2002) Signaling to the Rho GTPases. Networking with the DH domain. FEBS Lett. 513, 85-91
    • (2002) FEBS Lett. , vol.513 , pp. 85-91
    • Hoffman, G.R.1    Cerione, R.A.2
  • 29
    • 79955968406 scopus 로고    scopus 로고
    • Mechanistic insights into specificity, activity, and regulatory elements of the regulator of G-protein signaling (RGS)-containing Rho-specific guanine nucleotide exchange factors (GEFs) pi 15, PDZ-RhoGEF (PRG), and leukemia-associated RhoGEF (LARG)
    • Jaiswal, M., Gremer, L., Dvorsky, R., Haeusler, L. C, Cirstea, I. C, Uhlen-brock, K., and Ahmadian, M. R. (2011) Mechanistic insights into specificity, activity, and regulatory elements of the regulator of G-protein signaling (RGS)-containing Rho-specific guanine nucleotide exchange factors (GEFs) pi 15, PDZ-RhoGEF (PRG), and leukemia-associated RhoGEF (LARG). Biol. Chem. 286, 18202-18212
    • (2011) Biol. Chem. , vol.286 , pp. 18202-18212
    • Jaiswal, M.1    Gremer, L.2    Dvorsky, R.3    Haeusler, L.C.4    Cirstea, I.C.5    Uhlen-Brock, K.6    Ahmadian, M.R.7
  • 30
    • 84865650467 scopus 로고    scopus 로고
    • Regulation of the DH-PH tandem of guanine nucleotide exchange factor for Rho GTPases by phosphoinositides.ylt/v
    • Viaud, J., Gaits-Iacovoni, F., and Payrastre, B. (2012) Regulation of the DH-PH tandem of guanine nucleotide exchange factor for Rho GTPases by phosphoinositides.ylt/v. Biol. Regul. 52, 303-314
    • (2012) Biol. Regul. , vol.52 , pp. 303-314
    • Viaud, J.1    Gaits-Iacovoni, F.2    Payrastre, B.3
  • 33
    • 26944450513 scopus 로고    scopus 로고
    • An electrostatic steering mechanism of Cdc42 recognition by Wiskott-Aldrich syndrome proteins
    • Hemsath, L., Dvorsky, R., Fiegen, D., Carlier, M. F., and Ahmadian, M. R. (2005) An electrostatic steering mechanism of Cdc42 recognition by Wiskott-Aldrich syndrome proteins. Mol. Cell 20, 313-324
    • (2005) Mol. Cell , vol.20 , pp. 313-324
    • Hemsath, L.1    Dvorsky, R.2    Fiegen, D.3    Carlier, M.F.4    Ahmadian, M.R.5
  • 34
    • 33845868501 scopus 로고    scopus 로고
    • Evolution of the Rho family of Ras-like GTPases in eukaryotes
    • Boureux, A., Vignal, E., Faure, S., and Fort, P. (2007) Evolution of the Rho family of Ras-like GTPases in eukaryotes. Mol. Biol. Evol. 24, 203-216
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 203-216
    • Boureux, A.1    Vignal, E.2    Faure, S.3    Fort, P.4
  • 35
    • 0035800854 scopus 로고    scopus 로고
    • Identification of potential mechanisms for regulation of pll5 RhoGEF through analysis of endogenous and mutant forms of the exchange factor
    • Wells, C D., Gutowski, S., Bollag, G., and Sternweis, P. C. (2001) Identification of potential mechanisms for regulation of pll5 RhoGEF through analysis of endogenous and mutant forms of the exchange factor. J. Biol. Chem. 276, 28897-28905
    • (2001) J. Biol. Chem. , vol.276 , pp. 28897-28905
    • Wells, C.D.1    Gutowski, S.2    Bollag, G.3    Sternweis, P.C.4
  • 36
    • 0030451173 scopus 로고    scopus 로고
    • The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-specific guanine-nucleotide exchange factor
    • Zheng, Y., Fischer, D. J., Santos, M. F., Tigyi, G., Pasteris, N. G., Gorski, J. L., and Xu, Y. (1996) The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-specific guanine-nucleotide exchange factor. Biol. Chem. 271, 33169-33172
    • (1996) Biol. Chem. , vol.271 , pp. 33169-33172
    • Zheng, Y.1    Fischer, D.J.2    Santos, M.F.3    Tigyi, G.4    Pasteris, N.G.5    Gorski, J.L.6    Xu, Y.7
  • 37
    • 65849408332 scopus 로고    scopus 로고
    • RhoBTB3. A Rho GTPase-family ATPase required for endosome to Golgi transport
    • Espinosa, E. J., Calero, M., Sridevi, IC, and Pfeffer, S. R. (2009) RhoBTB3. A Rho GTPase-family 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, I.C.3    Pfeffer, S.R.4
  • 39
    • 0036150120 scopus 로고    scopus 로고
    • The hematopoiesis-specific GTP-binding protein RhoH is GTPase-deficient and modulates activities of other Rho GTPases by an inhibitory function
    • Li, X., Bu, X., Lu, B., Avraham, H., Flavell, R. A., and Lim, B. (2002) The hematopoiesis-specific GTP-binding protein RhoH is GTPase-deficient and modulates activities of other Rho GTPases by an inhibitory function. Mol. Cell. Biol. 22, 1158-1171
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1158-1171
    • Li, X.1    Bu, X.2    Lu, B.3    Avraham, H.4    Flavell, R.A.5    Lim, B.6
  • 40
    • 25444476956 scopus 로고    scopus 로고
    • RhoH GTPase. A key regulator of hematopoietic cell proliferation and apoptosis?
    • Gu, Y., Zheng, Y., and Williams, D. A. (2005) RhoH GTPase. A key regulator of hematopoietic cell proliferation and apoptosis? Cell Cycle 4, 201-202
    • (2005) Cell Cycle , vol.4 , pp. 201-202
    • Gu, Y.1    Zheng, Y.2    Williams, D.A.3
  • 41
    • 0037150122 scopus 로고    scopus 로고
    • Crystal structure of the core domain of RhoE/Rnd3. A constitutively activated small G protein
    • Garavini, H., Riento, IC, Phelan, J. P., McAlister, M. S., Ridley, A. J., and Keep, N. H. (2002) Crystal structure of the core domain of RhoE/Rnd3. A constitutively activated small G protein. Biochemistry 41, 6303-6310
    • (2002) Biochemistry , vol.41 , pp. 6303-6310
    • Garavini, H.1    Riento, I.C.2    Phelan, J.P.3    McAlister, M.S.4    Ridley, A.J.5    Keep, N.H.6
  • 43
    • 84866130598 scopus 로고    scopus 로고
    • The GTPase-deficient Rnd proteins are stabilized by their effectors
    • Goh, L. L., and Manser, E. (2012) The GTPase-deficient Rnd proteins are stabilized by their effectors. Biol. Chem. 287, 31311-31320
    • (2012) Biol. Chem. , vol.287 , pp. 31311-31320
    • Goh, L.L.1    Manser, E.2
  • 47
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE. Multiple sequence alignment with high accuracy and high throughput
    • Edgar, R. C. (2004) MUSCLE. Multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792-1797
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 49
    • 0037086652 scopus 로고    scopus 로고
    • A crystallographic view of interactions between Dbs and Cdc42. PH domain-assisted guanine nucleotide exchange
    • Rossman, IC L., Worthylake, D. IC, Snyder, J. T., Siderovski, D. P., Campbell, S. L., and Sondek, J. (2002) A crystallographic view of interactions between Dbs and Cdc42. PH domain-assisted guanine nucleotide exchange. EMBOJ. 21, 1315-1326
    • (2002) EMBOJ , vol.21 , pp. 1315-1326
    • Rossman, I.C.L.1    Worthylake, D.I.C.2    Snyder, J.T.3    Siderovski, D.P.4    Campbell, S.L.5    Sondek, J.6
  • 51
    • 8744317101 scopus 로고    scopus 로고
    • Structural determinants of RhoA binding and nucleotide exchange in leukemia-associated Rho guanine-nucleotide exchange factor
    • Kristelly, R., Gao, G., and Tesmer, J. J. (2004) Structural determinants of RhoA binding and nucleotide exchange in leukemia-associated Rho guanine-nucleotide exchange factor. Biol. Chem. 279, 47352-47362
    • (2004) Biol. Chem. , vol.279 , pp. 47352-47362
    • Kristelly, R.1    Gao, G.2    Tesmer, J.J.3
  • 52
    • 0021825489 scopus 로고
    • Isolation of a new human oncogene from a diffuse B-cell lymphoma
    • Eva, A., and Aaronson, S. A. (1985) Isolation of a new human oncogene from a diffuse B-cell lymphoma. Nature 316, 273-275
    • (1985) Nature , vol.316 , pp. 273-275
    • Eva, A.1    Aaronson, S.A.2
  • 54
    • 0030466893 scopus 로고    scopus 로고
    • Faciogenital dysplasia protein (FGD1) and Vav, two related proteins required for normal embryonic development, are upstream regulators of Rho GTPases
    • Olson, M. F., Pasteris, N. G., Gorski, I. L., and Hall, A. (1996) Faciogenital dysplasia protein (FGD1) and Vav, two related proteins required for normal embryonic development, are upstream regulators of Rho GTPases. Curr. Biol. 6, 1628-1633
    • (1996) Curr. Biol. , vol.6 , pp. 1628-1633
    • Olson, M.F.1    Pasteris, N.G.2    Gorski, I.L.3    Hall, A.4
  • 55
    • 33751271616 scopus 로고    scopus 로고
    • Role of Rho GTPases and Rho-GEFs in the regulation of cell shape and integrity in fission yeast
    • Garcia, P., Tajadura, V., Garcia, I., and Sanchez, Y. (2006) Role of Rho GTPases and Rho-GEFs in the regulation of cell shape and integrity in fission yeast. Yeast 23, 1031-1043
    • (2006) Yeast , vol.23 , pp. 1031-1043
    • Garcia, P.1    Tajadura, V.2    Garcia, I.3    Sanchez, Y.4
  • 56
    • 0032541613 scopus 로고    scopus 로고
    • Rho family proteins and Ras transformation. The RHOad less traveled gets congested
    • Zohn, I.M., Campbell, S.L., Khosravi-Far, R., Rossman, K.L., and Der, C. J. (1998) Rho family proteins and Ras transformation. The RHOad less traveled gets congested. Oncogene 17, 1415-1438
    • (1998) Oncogene , vol.17 , pp. 1415-1438
    • Zohn, I.M.1    Campbell, S.L.2    Khosravi-Far, R.3    Rossman, K.L.4    Der, C.J.5
  • 57
    • 33845933351 scopus 로고    scopus 로고
    • The molecular basis of RhoA specificity in the guanine nucleotide exchange factor PDZ-RhoGEF
    • Oleksy, A., Opaliriski, L., Derewenda, U., Derewenda, Z. S., and Otlewski, J. (2006) The molecular basis of RhoA specificity in the guanine nucleotide exchange factor PDZ-RhoGEF. Biol. Chem. 281, 32891-32897
    • (2006) Biol. Chem. , vol.281 , pp. 32891-32897
    • Oleksy, A.1    Opaliriski, L.2    Derewenda, U.3    Derewenda, Z.S.4    Otlewski, J.5
  • 59
    • 0034619877 scopus 로고    scopus 로고
    • Crystal structure of Racl in complex with the guanine nucleotide exchange region of Tiaml
    • Worthylake, D. IC, Rossman, IC L., and Sondek, J. (2000) Crystal structure of Racl in complex with the guanine nucleotide exchange region of Tiaml. Natore 408, 682-688
    • (2000) Natore , vol.408 , pp. 682-688
    • Worthylake, D.I.C.1    Rossman, I.C.L.2    Sondek, J.3
  • 61
    • 25444486668 scopus 로고    scopus 로고
    • The Rac activator Tiaml controls tight junction biogenesis in keratinocytes through binding to and activation of the Par polarity complex
    • Mertens, A. E., Rygiel, T. P., Olivo, C, van der Kammen, R., and Collard, J. G. (2005) The Rac activator Tiaml controls tight junction biogenesis in keratinocytes through binding to and activation of the Par polarity complex. Cell Biol. 170, 1029-1037
    • (2005) Cell Biol. , vol.170 , pp. 1029-1037
    • Mertens, A.E.1    Rygiel, T.P.2    Olivo, C.3    Van Der Kammen, R.4    Collard, J.G.5
  • 62
    • 34848869140 scopus 로고    scopus 로고
    • The Par-Tiaml complex controls persistent migration by stabilizing microtubule-dependent front-rear polarity
    • Pegtel, D. M., Ellenbroek, S. I., Mertens, A. E., van der Kammen, R. A., de Rooij, J., and Collard, J. G. (2007) The Par-Tiaml complex controls persistent migration by stabilizing microtubule-dependent front-rear polarity. Curr. Biol. 17, 1623-1634
    • (2007) Curr. Biol. , vol.17 , pp. 1623-1634
    • Pegtel, D.M.1    Ellenbroek, S.I.2    Mertens, A.E.3    Van Der Kammen, R.A.4    De Rooij, J.5    Collard, J.G.6
  • 63
    • 33947283144 scopus 로고    scopus 로고
    • The Par polarity complex regulates Rapl-and chemokine-induced T cell polarization
    • Gérard, A., Mertens, A. E., van der Kammen, R. A., and Collard, J. G. (2007) The Par polarity complex regulates Rapl-and chemokine-induced T cell polarization. Cell Biol. 176, 863-875
    • (2007) Cell Biol. , vol.176 , pp. 863-875
    • Gérard, A.1    Mertens, A.E.2    Van Der Kammen, R.A.3    Collard, J.G.4
  • 66
    • 35748983198 scopus 로고    scopus 로고
    • Ga directly activates p63RhoGEF and Trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain
    • Rojas, R. J., Yohe, M. E., Gershburg, S., Kawano, T., Kozasa, T., and Sondek, J. (2007) Ga directly activates p63RhoGEF and Trio via a conserved extension of the Dbl homology-associated pleckstrin homology domain. Biol. Chem. 282, 29201-29210
    • (2007) Biol. Chem. , vol.282 , pp. 29201-29210
    • Rojas, R.J.1    Yohe, M.E.2    Gershburg, S.3    Kawano, T.4    Kozasa, T.5    Sondek, J.6
  • 67
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson, IC M., Lemmon, M. A., Schlessinger, J., and Sigler, P. B. (1995) Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 83, 1037-1046
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, I.C.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 69
    • 0030723206 scopus 로고    scopus 로고
    • Targeting of Tiaml to the plasma membrane requires the cooperative function of the N-terminal pleckstrin homology domain and an adjacent protein interaction domain
    • Stam, J. C, Sander, E. E., Michiels, F., van Leeuwen, F. N, Kain, H. E., van der Kammen, R. A., and Collard, J. G. (1997) Targeting of Tiaml to the plasma membrane requires the cooperative function of the N-terminal pleckstrin homology domain and an adjacent protein interaction domain. J. Biol. Chem. 272, 28447-28454
    • (1997) J. Biol. Chem. , vol.272 , pp. 28447-28454
    • Stam, J.C.1    Sander, E.E.2    Michiels, F.3    Van Leeuwen, F.N.4    Kain, H.E.5    Van Der Kammen, R.A.6    Collard, J.G.7
  • 74
    • 84855745889 scopus 로고    scopus 로고
    • CIIA functions as a molecular switch for the Racl-specific GEF activity of SOS1
    • Hwang, H. S., Hwang, S. G., Cho, I. H, Chae, I. S., Yoon, IC W., Cho, S. G., and Choi, E. J. (2011) CIIA functions as a molecular switch for the Racl-specific GEF activity of SOS1. Cell Biol. 195, 377-386
    • (2011) Cell Biol. , vol.195 , pp. 377-386
    • Hwang, H.S.1    Hwang, S.G.2    Cho, I.H.3    Chae, I.S.4    Yoon, I.C.W.5    Cho, S.G.6    Choi, E.J.7
  • 76
    • 22744432389 scopus 로고    scopus 로고
    • Scaffold proteins dictate Rho GTPase-signaling specificity
    • Marinissen, M. J., and Gutkind, J. S. (2005) Scaffold proteins dictate Rho GTPase-signaling specificity. Trends Biochem. Sei. 30, 423-426
    • (2005) Trends Biochem. Sei. , vol.30 , pp. 423-426
    • Marinissen, M.J.1    Gutkind, J.S.2
  • 77
    • 33845228037 scopus 로고    scopus 로고
    • Ccpgl, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs
    • Kostenko, E. V., Olabisi, O. O., Sahay, S., Rodriguez, P. L., and Whitehead, I. P. (2006) Ccpgl, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs. Mol. Cell. Biol. 26, 8964-8975
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8964-8975
    • Kostenko, E.V.1    Olabisi, O.O.2    Sahay, S.3    Rodriguez, P.L.4    Whitehead, I.P.5
  • 78
    • 33749240350 scopus 로고    scopus 로고
    • Coupling receptor tyrosine kinases to Rho GTPases-GEFs what's the link
    • Schiller, M. R. (2006) Coupling receptor tyrosine kinases to Rho GTPases-GEFs what's the link. Cell. Signal. 18, 1834-1843
    • (2006) Cell. Signal. , vol.18 , pp. 1834-1843
    • Schiller, M.R.1
  • 83
    • 70450222906 scopus 로고    scopus 로고
    • Rif proteins take to the RhoD. Rho GTPases at the crossroads of actin dynamics and membrane trafficking
    • Gad, A. IC, and Aspenström, P. (2010) Rif proteins take to the RhoD. Rho GTPases at the crossroads of actin dynamics and membrane trafficking. Cell. Signal. 22, 183-189
    • (2010) Cell. Signal. , vol.22 , pp. 183-189
    • Gad, A.I.C.1    Aspenström, P.2
  • 84
    • 0028801195 scopus 로고
    • The kinetic mechanism of Ran-nucleotide exchange catalyzed by RCC1
    • Klebe, C, Prinz, H., Wittinghofer, A., and Goody, R. S. (1995) The kinetic mechanism of Ran-nucleotide exchange catalyzed by RCC1. Biochemistry 34, 12543-12552
    • (1995) Biochemistry , vol.34 , pp. 12543-12552
    • Klebe, C.1    Prinz, H.2    Wittinghofer, A.3    Goody, R.S.4
  • 86
    • 0032546533 scopus 로고    scopus 로고
    • Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25Mm
    • Lenzen, C, Cool, R. H., Prinz, H., Kuhlmann, J., and Wittinghofer, A. (1998) Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25Mm. Biochemistry 37, 7420-7430
    • (1998) Biochemistry , vol.37 , pp. 7420-7430
    • Lenzen, C.1    Cool, R.H.2    Prinz, H.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 87
    • 0034687081 scopus 로고    scopus 로고
    • Mechanism of nucleotide release from Rho by the GDP dissociation stimulator protein
    • Hutchinson, J. P., and Eccleston, J. F. (2000) Mechanism of nucleotide release from Rho by the GDP dissociation stimulator protein. Biochemistry 39, 11348-11359
    • (2000) Biochemistry , vol.39 , pp. 11348-11359
    • Hutchinson, J.P.1    Eccleston, J.F.2
  • 88
    • 33846028702 scopus 로고    scopus 로고
    • Sec2 is a highly efficient exchange factor for the Rab protein Sec4
    • Itzen, A., Rak, A., and Goody, R. S. (2007) Sec2 is a highly efficient exchange factor for the Rab protein Sec4. Mol. Biol. 365, 1359-1367
    • (2007) Mol. Biol. , vol.365 , pp. 1359-1367
    • Itzen, A.1    Rak, A.2    Goody, R.S.3
  • 89
    • 33846027894 scopus 로고    scopus 로고
    • Structural evidence for a common intermediate in small G protein-GEF reactions
    • Thomas, C, Fricke, I., Scrima, A., Berken, A., and Wittinghofer, A. (2007) Structural evidence for a common intermediate in small G protein-GEF reactions. Mol. Cell 25, 141-149
    • (2007) Mol. Cell , vol.25 , pp. 141-149
    • Thomas, C.1    Fricke, I.2    Scrima, A.3    Berken, A.4    Wittinghofer, A.5
  • 90
    • 0037604662 scopus 로고    scopus 로고
    • Dynamic and coordinated expression profile of dbl-family guanine nucleotide exchange factors in the developing mouse brain
    • Yoshizawa, M., Sone, M., Matsuo, N., Nagase, T., Ohara, O., Nabeshima, Y., and Hoshino, M. (2003) Dynamic and coordinated expression profile of dbl-family guanine nucleotide exchange factors in the developing mouse brain. Gene Expr. Patterns 3, 375-381
    • (2003) Gene Expr. Patterns , vol.3 , pp. 375-381
    • Yoshizawa, M.1    Sone, M.2    Matsuo, N.3    Nagase, T.4    Ohara, O.5    Nabeshima, Y.6    Hoshino, M.7
  • 91
    • 77954257799 scopus 로고    scopus 로고
    • Con-Surf 2010. Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy, H, Erez, E., Martz, E., Pupko, T., and Ben-Tal, N. (2010) Con-Surf 2010. Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. 38, W529-W533
    • (2010) Nucleic Acids Res. , vol.38
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5


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