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Volumn 45, Issue 25, 2006, Pages 7750-7762

Influencing cellular transformation by modulating the rates of GTP hydrolysis by Cdc42

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; COMPUTER ARCHITECTURE; HYDROLYSIS; SIGNALING;

EID: 33746933848     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060365h     Document Type: Article
Times cited : (28)

References (46)
  • 2
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon, N., and Hall, A. (1997) Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton, Curr. Opin. Cell Biol. 9, 86-92.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 3
    • 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
  • 4
    • 0033007293 scopus 로고    scopus 로고
    • Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity
    • Johnson, D. I. (1999) Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity, Microbiol. Mol. Biol. Rev. 63, 54-105.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 54-105
    • Johnson, D.I.1
  • 5
    • 0035375053 scopus 로고    scopus 로고
    • Cdc42 is a substrate for caspases and influences Fas-induced apoptosis
    • Tu, S., and Cerione, R. A. (2001) Cdc42 is a substrate for caspases and influences Fas-induced apoptosis, J. Biol. Chem. 276, 19656-19663.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19656-19663
    • Tu, S.1    Cerione, R.A.2
  • 6
    • 0028875683 scopus 로고
    • Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation
    • Bagrodia, S., Derijard, B., Davis, R. J., and Cerione, R. A. (1995) Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation, J. Biol. Chem. 270, 27995-27998.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27995-27998
    • Bagrodia, S.1    Derijard, B.2    Davis, R.J.3    Cerione, R.A.4
  • 7
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
    • Coso, O. A., Chiariello, M., Yu, J. C., Teramoto, H., Crespo, P., Xu, N., Miki, T., and Gutkind, J. S. (1995) The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway, Cell 81, 1137-1146.
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.C.3    Teramoto, H.4    Crespo, P.5    Xu, N.6    Miki, T.7    Gutkind, J.S.8
  • 8
    • 0029070887 scopus 로고
    • Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
    • Minden, A., Lin, A., Claret, F. X., Abo, A., and Karin, M. (1995) Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs, Cell 81, 1147-1157.
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Lin, A.2    Claret, F.X.3    Abo, A.4    Karin, M.5
  • 9
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • Olson, M. F., Ashworth, A., and Hall, A. (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
  • 10
    • 0028820587 scopus 로고
    • Rho family GTPases regulate p38 mitogen-activated protein kinase through the down-stream mediator Pak1
    • Zhang, S., Han, J., Sells, M. A., Chernoff, J., Knaus, U. G., Ulevitch, R. J., and Bokoch, G. M. (1995) Rho family GTPases regulate p38 mitogen-activated protein kinase through the down-stream mediator Pak1, J. Biol. Chem. 270, 23934-23936.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23934-23936
    • Zhang, S.1    Han, J.2    Sells, M.A.3    Chernoff, J.4    Knaus, U.G.5    Ulevitch, R.J.6    Bokoch, G.M.7
  • 11
    • 0035907377 scopus 로고    scopus 로고
    • The Cdc42 target ACK2 directly interacts with clathrin and influences clathrin assembly
    • Yang, W., Lo, C. G., Dispenza, T., and Cerione, R. A. (2001) The Cdc42 target ACK2 directly interacts with clathrin and influences clathrin assembly, J. Biol. Chem. 276, 17468-17473.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17468-17473
    • Yang, W.1    Lo, C.G.2    Dispenza, T.3    Cerione, R.A.4
  • 12
    • 0033126052 scopus 로고    scopus 로고
    • Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
    • Kroschewski, R., Hall, A., and Mellman, I. (1999) Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells, Nat. Cell Biol. 1, 8-13.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 8-13
    • Kroschewski, R.1    Hall, A.2    Mellman, I.3
  • 13
    • 0035341316 scopus 로고    scopus 로고
    • Cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network
    • Musch, A., Cohen, D., Kreitzer, G., and Rodriguez-Boulan, E. (2001) cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network, EMBO J. 20, 2171-2179.
    • (2001) EMBO J. , vol.20 , pp. 2171-2179
    • Musch, A.1    Cohen, D.2    Kreitzer, G.3    Rodriguez-Boulan, E.4
  • 14
    • 0036179523 scopus 로고    scopus 로고
    • Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbpl
    • Fucini, R. V., Chen, J. L., Sharma, C., Kessels, M. M., and Stamnes, M. (2002) Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbpl, Mol. Biol. Cell 13, 621-631.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 621-631
    • Fucini, R.V.1    Chen, J.L.2    Sharma, C.3    Kessels, M.M.4    Stamnes, M.5
  • 16
    • 0001264854 scopus 로고    scopus 로고
    • The gamma-subunit of the coatomer complex binds Cdc42 to mediate transformation
    • Wu, W. J., Erickson, J. W., Lin, R., and Cerione, R. A. (2000) The gamma-subunit of the coatomer complex binds Cdc42 to mediate transformation, Nature 405, 800-804.
    • (2000) Nature , vol.405 , pp. 800-804
    • Wu, W.J.1    Erickson, J.W.2    Lin, R.3    Cerione, R.A.4
  • 17
    • 1442274703 scopus 로고    scopus 로고
    • Cdc42: New roads to travel
    • Cerione, R. A. (2004) Cdc42: New roads to travel, Trends Cell Biol. 14, 127-132.
    • (2004) Trends Cell Biol. , vol.14 , pp. 127-132
    • Cerione, R.A.1
  • 19
    • 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
  • 20
    • 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
  • 21
    • 0025073547 scopus 로고
    • Molecular cloning and characterization of a novel type of regulatory protein (GDI) for the rho proteins, ras p21-like small GTP-binding proteins
    • Fukumoto, Y., Kaibuchi, K., Hori, Y., Fujioka, H., Araki, S., Ueda, T., Kikuchi, A., and Takai, Y. (1990) Molecular cloning and characterization of a novel type of regulatory protein (GDI) for the rho proteins, ras p21-like small GTP-binding proteins, Oncogene 5, 1321-1328.
    • (1990) Oncogene , vol.5 , pp. 1321-1328
    • Fukumoto, Y.1    Kaibuchi, K.2    Hori, Y.3    Fujioka, H.4    Araki, S.5    Ueda, T.6    Kikuchi, A.7    Takai, Y.8
  • 22
    • 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
  • 23
    • 0031260578 scopus 로고    scopus 로고
    • A novel Cdc42Hs mutant induces cellular transformation
    • Lin, R., Bagrodia, S., Cerione, R., and Manor, D. (1997) A novel Cdc42Hs mutant induces cellular transformation, Curr. Biol. 7, 794-797.
    • (1997) Curr. Biol. , vol.7 , pp. 794-797
    • Lin, R.1    Bagrodia, S.2    Cerione, R.3    Manor, D.4
  • 24
    • 0033551698 scopus 로고    scopus 로고
    • Specific contributions of the small GTPases Rho, Rac, and Cdc42 to Dbl transformation
    • Lin, R., Cerione, R. A., and Manor, D. (1999) Specific contributions of the small GTPases Rho, Rac, and Cdc42 to Dbl transformation, J. Biol. Chem. 274, 23633-23641.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23633-23641
    • Lin, R.1    Cerione, R.A.2    Manor, D.3
  • 25
    • 0037108090 scopus 로고    scopus 로고
    • Antiapoptotic Cdc42 mutants are potent activators of cellular transformation
    • Tu, S. S., Wu, W. J., Yang, W., Nolbant, P., Hahn, K., and Cerione, R. A. (2002) Antiapoptotic Cdc42 mutants are potent activators of cellular transformation, Biochemistry 41, 12350-12358.
    • (2002) Biochemistry , vol.41 , pp. 12350-12358
    • Tu, S.S.1    Wu, W.J.2    Yang, W.3    Nolbant, P.4    Hahn, K.5    Cerione, R.A.6
  • 26
    • 0031762533 scopus 로고    scopus 로고
    • Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP
    • Nassar, N., Hoffman, G. R., Manor, D., Clardy, J. C., and Cerione, R. A. (1998) Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP, Nat. Struct. Biol. 5, 1047-1052.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1047-1052
    • Nassar, N.1    Hoffman, G.R.2    Manor, D.3    Clardy, J.C.4    Cerione, R.A.5
  • 27
    • 0037207097 scopus 로고    scopus 로고
    • Understanding the catalytic mechanism of GTPase-activating proteins: Demonstration of the importance of switch domain stabilization in the stimulation of GTP hydrolysis
    • Fidyk, N. J., and Cerione, R. A. (2002) Understanding the catalytic mechanism of GTPase-activating proteins: Demonstration of the importance of switch domain stabilization in the stimulation of GTP hydrolysis, Biochemistry 41, 15644-15653.
    • (2002) Biochemistry , vol.41 , pp. 15644-15653
    • Fidyk, N.J.1    Cerione, R.A.2
  • 28
    • 0020674810 scopus 로고
    • New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes
    • Hiratsuka, T. (1983) New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes, Biochim. Biophys. Acta 742, 496-508.
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 496-508
    • Hiratsuka, T.1
  • 29
    • 0027944055 scopus 로고
    • Investigation of the GTP-binding/GTPase cycle of Cdc42Hs using fluorescence spectroscopy
    • Leonard, D. A., Evans, T., Hart, M., Cerione, R. A., and Manor, D. (1994) Investigation of the GTP-binding/GTPase cycle of Cdc42Hs using fluorescence spectroscopy, Biochemistry 33, 12323-12328.
    • (1994) Biochemistry , vol.33 , pp. 12323-12328
    • Leonard, D.A.1    Evans, T.2    Hart, M.3    Cerione, R.A.4    Manor, D.5
  • 30
    • 20744453511 scopus 로고    scopus 로고
    • Cdc42 and Ras cooperate to mediate cellular transformation by intersectin-L
    • Wang, J. B., Wu, W. J., and Cerione, R. A. (2005) Cdc42 and Ras cooperate to mediate cellular transformation by intersectin-L, J. Biol. Chem. 280, 22883-22891.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22883-22891
    • Wang, J.B.1    Wu, W.J.2    Cerione, R.A.3
  • 32
    • 0026349335 scopus 로고
    • Is there a rate-limiting step before GTP cleavage by H-ras p21?
    • Rensland, H., Lautwein, A., Wittinghofer, A., and Goody, R. S. (1991) Is there a rate-limiting step before GTP cleavage by H-ras p21? Biochemistry 30, 11181-11185.
    • (1991) Biochemistry , vol.30 , pp. 11181-11185
    • Rensland, H.1    Lautwein, A.2    Wittinghofer, A.3    Goody, R.S.4
  • 33
    • 0027297116 scopus 로고
    • Mechanism of GTP hydrolysis by p21N-ras catalyzed by GAP: Studies with a fluorescent GTP analogue
    • Moore, K. J., Webb, M. R., and Eccleston, J. F. (1993) Mechanism of GTP hydrolysis by p21N-ras catalyzed by GAP: Studies with a fluorescent GTP analogue, Biochemistry 32, 7451-7459.
    • (1993) Biochemistry , vol.32 , pp. 7451-7459
    • Moore, K.J.1    Webb, M.R.2    Eccleston, J.F.3
  • 34
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • Burbelo, P. D., Drechsel, D., and Hall, A. (1995) A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases, J. Biol. Chem. 270, 29071-29074.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29071-29074
    • Burbelo, P.D.1    Drechsel, D.2    Hall, A.3
  • 35
    • 0030779042 scopus 로고    scopus 로고
    • Cloning and characterization of a novel Cdc42-associated tyrosine kinase, ACK-2, from bovine brain
    • Yang, W., and Cerione, R. A. (1997) Cloning and characterization of a novel Cdc42-associated tyrosine kinase, ACK-2, from bovine brain, J. Biol. Chem. 272, 24819-24824.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24819-24824
    • Yang, W.1    Cerione, R.A.2
  • 37
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
    • Kozma, R., Ahmed, S., Best, A., and Lim, L. (1995) The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts, Mol. Cell. Biol. 15, 1942-1952.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1942-1952
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 38
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D., and Hall, A. (1995) Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia, Cell 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 39
    • 0032568850 scopus 로고    scopus 로고
    • Biochemical studies of the mechanism of action of the Cdc42-GTPase-activating protein
    • Leonard, D. A., Lin, R., Cerione, R. A., and Manor, D. (1998) Biochemical studies of the mechanism of action of the Cdc42-GTPase-activating protein, J. Biol. Chem. 273, 16210-16215.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16210-16215
    • Leonard, D.A.1    Lin, R.2    Cerione, R.A.3    Manor, D.4
  • 40
    • 0141426629 scopus 로고    scopus 로고
    • Activated Cdc42 sequesters c-Cbl and prevents EGF receptor degradation
    • Wu, W. J., Tu, S., and Cerione, R. A. (2003) Activated Cdc42 sequesters c-Cbl and prevents EGF receptor degradation, Cell 114, 715-725.
    • (2003) Cell , vol.114 , pp. 715-725
    • Wu, W.J.1    Tu, S.2    Cerione, R.A.3
  • 41
    • 0027958423 scopus 로고
    • Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product
    • Hart, M. J., Eva, A., Zangrilli, D., Aaronson, S. A., Evans, T., Cerione, R. A., and Zheng, Y. (1994) Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product, J. Biol. Chem. 269, 62-65.
    • (1994) J. Biol. Chem. , vol.269 , pp. 62-65
    • Hart, M.J.1    Eva, A.2    Zangrilli, D.3    Aaronson, S.A.4    Evans, T.5    Cerione, R.A.6    Zheng, Y.7
  • 42
    • 0027369641 scopus 로고
    • Cloning and expression of a human CDC42 GTPase-activating protein reveals a functional SH3-binding domain
    • Barfod, E. T., Zheng, Y., Kuang, W. J., Hart, M. J., Evans, T., Cerione, R. A., and Ashkenazi, A. (1993) Cloning and expression of a human CDC42 GTPase-activating protein reveals a functional SH3-binding domain, J. Biol. Chem. 268, 26059-26062.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26059-26062
    • Barfod, E.T.1    Zheng, Y.2    Kuang, W.J.3    Hart, M.J.4    Evans, T.5    Cerione, R.A.6    Ashkenazi, A.7
  • 43
    • 0037855764 scopus 로고    scopus 로고
    • Deleted in liver cancer (DLC) 2 encodes a RhoGAP protein with growth suppressor function and is underexpressed in hepatocellular carcinoma
    • Ching, Y. P., Wong, C. M., Chan, S. F., Leung, T. H., Ng, D. C., Jin, D. Y., and Ng, I. O. (2003) Deleted in liver cancer (DLC) 2 encodes a RhoGAP protein with growth suppressor function and is underexpressed in hepatocellular carcinoma, J. Biol. Chem. 278, 10824-10830.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10824-10830
    • Ching, Y.P.1    Wong, C.M.2    Chan, S.F.3    Leung, T.H.4    Ng, D.C.5    Jin, D.Y.6    Ng, I.O.7
  • 44
    • 3242699514 scopus 로고    scopus 로고
    • Overexpression of Rho A, Rac1, and Cdc42 GTPases is associated with progression in testicular cancer
    • Kamai, T., Yamanishi, T., Shirataki, H., Takagi, K., Asami, H., Ito, Y., and Yoshida, K. (2004) Overexpression of Rho A, Rac1, and Cdc42 GTPases is associated with progression in testicular cancer, Clin. Cancer Res. 10, 4799-4805.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 4799-4805
    • Kamai, T.1    Yamanishi, T.2    Shirataki, H.3    Takagi, K.4    Asami, H.5    Ito, Y.6    Yoshida, K.7
  • 45
    • 0037048326 scopus 로고    scopus 로고
    • Rho GTPases in human breast tumours: Expression and mutation analyses and correlation with clinical parameters
    • Fritz, G., Brachetti, C., Bahlmann, F., Schmidt, M., and Kaina, B. (2002) Rho GTPases in human breast tumours: Expression and mutation analyses and correlation with clinical parameters, Br. J. Cancer 87, 635-644.
    • (2002) Br. J. Cancer , vol.87 , pp. 635-644
    • Fritz, G.1    Brachetti, C.2    Bahlmann, F.3    Schmidt, M.4    Kaina, B.5


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