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Volumn 157, Issue 5, 2015, Pages 285-299

Ral GTPases: Crucial mediators of exocytosis and tumourigenesis

Author keywords

exocyst; exocytosis; Ral; Ras; tumourigenesis

Indexed keywords

CYCLIN D1; EXOCYST; FILAMIN; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATASE RAL; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; NUCLEIC ACID BINDING PROTEIN; PHOSPHOLIPASE D; PROTEIN; PROTEIN KINASE C ETA; RLIP76 PROTEIN; STRESS ACTIVATED PROTEIN KINASE; UNCLASSIFIED DRUG; RAL PROTEIN;

EID: 84941110929     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvv029     Document Type: Article
Times cited : (58)

References (140)
  • 1
    • 0022779153 scopus 로고
    • The ral gene: A new ras related gene isolated by the use of a synthetic probe
    • Chardin, P. and Tavitian, A. (1986) The ral gene: A new ras related gene isolated by the use of a synthetic probe. EMBO J. 5, 2203-2208
    • (1986) EMBO J. , vol.5 , pp. 2203-2208
    • Chardin, P.1    Tavitian, A.2
  • 2
    • 0024412469 scopus 로고
    • Coding sequences of human ralA and ralB cDNAs
    • Chardin, P. and Tavitian, A. (1989) Coding sequences of human ralA and ralB cDNAs. Nucleic Acids Res. 17, 4380
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4380
    • Chardin, P.1    Tavitian, A.2
  • 4
    • 36048968159 scopus 로고    scopus 로고
    • Geranylgeranyltransferase i inhibitors target RalB to inhibit anchorage-dependent growth and induce apoptosis and RalA to inhibit anchorage-independent growth
    • Falsetti, S.C., Wang, D.A., Peng, H., Carrico, D., Cox, A.D., Der, C.J., Hamilton, A.D., and Sebti, S.M. (2007) Geranylgeranyltransferase I inhibitors target RalB to inhibit anchorage-dependent growth and induce apoptosis and RalA to inhibit anchorage-independent growth. Mol. Cell. Biol. 27, 8003-8014
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8003-8014
    • Falsetti, S.C.1    Wang, D.A.2    Peng, H.3    Carrico, D.4    Cox, A.D.5    Der, C.J.6    Hamilton, A.D.7    Sebti, S.M.8
  • 5
    • 84875246715 scopus 로고    scopus 로고
    • Identification of a novel prenyl and palmitoyl modification at the CaaX motif of Cdc42 that regulates RhoGDI binding
    • Nishimura, A. and Linder, M.E. (2013) Identification of a novel prenyl and palmitoyl modification at the CaaX motif of Cdc42 that regulates RhoGDI binding. Mol. Cell. Biol. 33, 1417-1429
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 1417-1429
    • Nishimura, A.1    Linder, M.E.2
  • 6
    • 0025861485 scopus 로고
    • A family of ras-like GTP-binding proteins expressed in electromotor neurons
    • Ngsee, J.K., Elferink, L.A., and Scheller, R.H. (1991) A family of ras-like GTP-binding proteins expressed in electromotor neurons. J. Biol. Chem. 266, 2675-2680
    • (1991) J. Biol. Chem. , vol.266 , pp. 2675-2680
    • Ngsee, J.K.1    Elferink, L.A.2    Scheller, R.H.3
  • 7
    • 0030570831 scopus 로고    scopus 로고
    • Association of Ral GTP-binding protein with human platelet dense granules
    • Mark, B.L., Jilkina, O., and Bhullar, R.P. (1996) Association of Ral GTP-binding protein with human platelet dense granules. Biochem. Biophy. Res. Commun. 225, 40-46
    • (1996) Biochem. Biophy. Res. Commun. , vol.225 , pp. 40-46
    • Mark, B.L.1    Jilkina, O.2    Bhullar, R.P.3
  • 8
    • 33846011880 scopus 로고    scopus 로고
    • RalA-exocyst-dependent recycling endosome trafficking is required for the completion of cytokinesis
    • Chen, X.W., Inoue, M., Hsu, S.C., and Saltiel, A.R. (2006) RalA-exocyst-dependent recycling endosome trafficking is required for the completion of cytokinesis. J. Biol. Chem. 281, 38609-38616
    • (2006) J. Biol. Chem. , vol.281 , pp. 38609-38616
    • Chen, X.W.1    Inoue, M.2    Hsu, S.C.3    Saltiel, A.R.4
  • 9
    • 0027518574 scopus 로고
    • Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase
    • Albright, C.F., Giddings, B.W., Liu, J., Vito, M., and Weinberg, R.A. (1993) Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase. EMBO J. 12, 339-347
    • (1993) EMBO J. , vol.12 , pp. 339-347
    • Albright, C.F.1    Giddings, B.W.2    Liu, J.3    Vito, M.4    Weinberg, R.A.5
  • 10
    • 0033545328 scopus 로고    scopus 로고
    • Plasma membrane recruitment of RalGDS is critical for Ras-dependent Ral activation
    • Matsubara, K., Kishida, S., Matsuura, Y., Kitayama, H., Noda, M., and Kikuchi, A. (1999) Plasma membrane recruitment of RalGDS is critical for Ras-dependent Ral activation. Oncogene 18, 1303-1312
    • (1999) Oncogene , vol.18 , pp. 1303-1312
    • Matsubara, K.1    Kishida, S.2    Matsuura, Y.3    Kitayama, H.4    Noda, M.5    Kikuchi, A.6
  • 11
    • 0027986765 scopus 로고
    • RalGDS family members interact with the effector loop of ras p21
    • Kikuchi, A., Demo, S.D., Ye, Z.H., Chen, Y.W., and Williams, L.T. (1994) ralGDS family members interact with the effector loop of ras p21. Mol. Cell. Biol. 14, 7483-7491
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7483-7491
    • Kikuchi, A.1    Demo, S.D.2    Ye, Z.H.3    Chen, Y.W.4    Williams, L.T.5
  • 14
    • 0034282408 scopus 로고    scopus 로고
    • A novel RalGEF-like protein, RGL3, as a candidate effector for rit and Ras
    • Shao, H. and Andres, D.A. (2000) A novel RalGEF-like protein, RGL3, as a candidate effector for rit and Ras. J. Biol. Chem. 275, 26914-26924
    • (2000) J. Biol. Chem. , vol.275 , pp. 26914-26924
    • Shao, H.1    Andres, D.A.2
  • 19
    • 42349101312 scopus 로고    scopus 로고
    • RalGDS couples growth factor signaling to Akt activation
    • Hao, Y., Wong, R., and Feig, L.A. (2008) RalGDS couples growth factor signaling to Akt activation. Mol. Cell. Biol. 28, 2851-2859
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 2851-2859
    • Hao, Y.1    Wong, R.2    Feig, L.A.3
  • 21
    • 0035081259 scopus 로고    scopus 로고
    • Regulation of Ras signaling specificity by protein kinase C
    • Rusanescu, G., Gotoh, T., Tian, X., and Feig, L.A. (2001) Regulation of Ras signaling specificity by protein kinase C. Mol. Cell. Biol. 21, 2650-2658
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2650-2658
    • Rusanescu, G.1    Gotoh, T.2    Tian, X.3    Feig, L.A.4
  • 22
    • 0034713356 scopus 로고    scopus 로고
    • The Rgr oncogene (homologous to RalGDS) induces transformation and gene expression by activating Ras, Ral and Rho mediated pathways
    • Hernandez-Munoz, I., Malumbres, M., Leonardi, P., and Pellicer, A. (2000) The Rgr oncogene (homologous to RalGDS) induces transformation and gene expression by activating Ras, Ral and Rho mediated pathways. Oncogene 19, 2745-2757
    • (2000) Oncogene , vol.19 , pp. 2745-2757
    • Hernandez-Munoz, I.1    Malumbres, M.2    Leonardi, P.3    Pellicer, A.4
  • 24
    • 80052055746 scopus 로고    scopus 로고
    • The human Rgr oncogene is overexpressed in T-cell malignancies and induces transformation by acting as a GEF for Ras and Ral
    • Osei-Sarfo, K., Martello, L., Ibrahim, S., and Pellicer, A. (2011) The human Rgr oncogene is overexpressed in T-cell malignancies and induces transformation by acting as a GEF for Ras and Ral. Oncogene 30, 3661-3671
    • (2011) Oncogene , vol.30 , pp. 3661-3671
    • Osei-Sarfo, K.1    Martello, L.2    Ibrahim, S.3    Pellicer, A.4
  • 25
    • 0034607989 scopus 로고    scopus 로고
    • Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral
    • Rebhun, J.F., Chen, H., and Quilliam, L.A. (2000) Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral. J. Biol. Chem. 275, 13406-13410
    • (2000) J. Biol. Chem. , vol.275 , pp. 13406-13410
    • Rebhun, J.F.1    Chen, H.2    Quilliam, L.A.3
  • 27
    • 34249985839 scopus 로고    scopus 로고
    • Functional analysis of RalGPS2, a murine guanine nucleotide exchange factor for RalA GTPase
    • Ceriani, M., Scandiuzzi, C., Amigoni, L., Tisi, R., Berruti, G., and Martegani, E. (2007) Functional analysis of RalGPS2, a murine guanine nucleotide exchange factor for RalA GTPase. Exp. Cell Res. 313, 2293-2307
    • (2007) Exp. Cell Res. , vol.313 , pp. 2293-2307
    • Ceriani, M.1    Scandiuzzi, C.2    Amigoni, L.3    Tisi, R.4    Berruti, G.5    Martegani, E.6
  • 28
    • 0025912628 scopus 로고
    • Characterization of a GTPase-activating protein for the Ras-related Ral protein
    • Emkey, R., Freedman, S., and Feig, L.A. (1991) Characterization of a GTPase-activating protein for the Ras-related Ral protein. J. Biol. Chem. 266, 9703-9706
    • (1991) J. Biol. Chem. , vol.266 , pp. 9703-9706
    • Emkey, R.1    Freedman, S.2    Feig, L.A.3
  • 30
    • 33747078270 scopus 로고    scopus 로고
    • Adipocytes contain a novel complex similar to the tuberous sclerosis complex
    • Gridley, S., Chavez, J.A., Lane, W.S., and Lienhard, G.E. (2006) Adipocytes contain a novel complex similar to the tuberous sclerosis complex. Cell. Signal. 18, 1626-1632
    • (2006) Cell. Signal. , vol.18 , pp. 1626-1632
    • Gridley, S.1    Chavez, J.A.2    Lane, W.S.3    Lienhard, G.E.4
  • 31
    • 78651085682 scopus 로고    scopus 로고
    • A Ral GAP complex links PI 3-kinase/Akt signaling to RalA activation in insulin action
    • Chen, X.W., Leto, D., Xiong, T., Yu, G., Cheng, A., Decker, S., and Saltiel, A.R. (2011) A Ral GAP complex links PI 3-kinase/Akt signaling to RalA activation in insulin action. Mol. Biol. Cell 22, 141-152
    • (2011) Mol. Biol. Cell , vol.22 , pp. 141-152
    • Chen, X.W.1    Leto, D.2    Xiong, T.3    Yu, G.4    Cheng, A.5    Decker, S.6    Saltiel, A.R.7
  • 33
    • 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
  • 34
  • 35
    • 41949114173 scopus 로고    scopus 로고
    • The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues
    • Scrima, A., Thomas, C., Deaconescu, D., and Wittinghofer, A. (2008) The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues. EMBO J. 27, 1145-1153
    • (2008) EMBO J. , vol.27 , pp. 1145-1153
    • Scrima, A.1    Thomas, C.2    Deaconescu, D.3    Wittinghofer, A.4
  • 37
  • 39
    • 3042796979 scopus 로고    scopus 로고
    • GAP control: Regulating the regulators of small GTPases
    • Bernards, A. and Settleman, J. (2004) GAP control: regulating the regulators of small GTPases. Trends Cell Biol. 14, 377-385
    • (2004) Trends Cell Biol. , vol.14 , pp. 377-385
    • Bernards, A.1    Settleman, J.2
  • 40
    • 0035839569 scopus 로고    scopus 로고
    • The brain exocyst complex interacts with RalA in a GTP-dependent manner: Identification of a novel mammalian Sec3 gene and a second Sec15 gene
    • Brymora, A., Valova, V.A., Larsen, M.R., Roufogalis, B.D., and Robinson, P.J. (2001) The brain exocyst complex interacts with RalA in a GTP-dependent manner: identification of a novel mammalian Sec3 gene and a second Sec15 gene. J. Biol. Chem. 276, 29792-29797
    • (2001) J. Biol. Chem. , vol.276 , pp. 29792-29797
    • Brymora, A.1    Valova, V.A.2    Larsen, M.R.3    Roufogalis, B.D.4    Robinson, P.J.5
  • 42
    • 0036141434 scopus 로고    scopus 로고
    • The exocyst complex binds the small GTPase RalA to mediate filopodia formation
    • Sugihara, K., Asano, S., Tanaka, K., Iwamatsu, A., Okawa, K., and Ohta, Y. (2002) The exocyst complex binds the small GTPase RalA to mediate filopodia formation. Nat. Cell Biol. 4, 73-78
    • (2002) Nat. Cell Biol. , vol.4 , pp. 73-78
    • Sugihara, K.1    Asano, S.2    Tanaka, K.3    Iwamatsu, A.4    Okawa, K.5    Ohta, Y.6
  • 43
    • 0038602702 scopus 로고    scopus 로고
    • Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex
    • Fukai, S., Matern, H.T., Jagath, J.R., Scheller, R.H., and Brunger, A.T. (2003) Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex. EMBO J. 22, 3267-3278
    • (2003) EMBO J. , vol.22 , pp. 3267-3278
    • Fukai, S.1    Matern, H.T.2    Jagath, J.R.3    Scheller, R.H.4    Brunger, A.T.5
  • 44
    • 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. (2005) Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase. EMBO J. 24, 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
  • 46
    • 2442586577 scopus 로고    scopus 로고
    • RalA-exocyst interaction mediates GTP-dependent exocytosis
    • Wang, L., Li, G., and Sugita, S. (2004) RalA-exocyst interaction mediates GTP-dependent exocytosis. J. Biol. Chem. 279, 19875-19881
    • (2004) J. Biol. Chem. , vol.279 , pp. 19875-19881
    • Wang, L.1    Li, G.2    Sugita, S.3
  • 49
    • 0032872821 scopus 로고    scopus 로고
    • Small GTP-binding protein RalA associates with Weibel-Palade bodies in endothelial cells
    • de Leeuw, H.P., Wijers-Koster, P.M., van Mourik, J.A., and Voorberg, J. (1999) Small GTP-binding protein RalA associates with Weibel-Palade bodies in endothelial cells. Thromb Haemost. 82, 1177-1181
    • (1999) Thromb Haemost. , vol.82 , pp. 1177-1181
    • De Leeuw, H.P.1    Wijers-Koster, P.M.2    Van Mourik, J.A.3    Voorberg, J.4
  • 52
    • 21844459500 scopus 로고    scopus 로고
    • Mammalian exocyst complex is required for the docking step of insulin vesicle exocytosis
    • Tsuboi, T., Ravier, M.A., Xie, H., Ewart, M.A., Gould, G.W., Baldwin, S.A., and Rutter, G.A. (2005) Mammalian exocyst complex is required for the docking step of insulin vesicle exocytosis. J. Biol. Chem. 280, 25565-25570
    • (2005) J. Biol. Chem. , vol.280 , pp. 25565-25570
    • Tsuboi, T.1    Ravier, M.A.2    Xie, H.3    Ewart, M.A.4    Gould, G.W.5    Baldwin, S.A.6    Rutter, G.A.7
  • 53
    • 44449125651 scopus 로고    scopus 로고
    • Involvement of Exoc3l, a protein structurally related to the exocyst subunit Sec6, in insulin secretion
    • Saito, T., Shibasaki, T., and Seino, S. (2008) Involvement of Exoc3l, a protein structurally related to the exocyst subunit Sec6, in insulin secretion. Biomed. Res 29, 85-91
    • (2008) Biomed. Res , vol.29 , pp. 85-91
    • Saito, T.1    Shibasaki, T.2    Seino, S.3
  • 54
    • 49649090688 scopus 로고    scopus 로고
    • The RalA GTPase is a central regulator of insulin exocytosis from pancreatic islet beta cells
    • Lopez, J.A., Kwan, E.P., Xie, L., He, Y., James, D.E., and Gaisano, H.Y. (2008) The RalA GTPase is a central regulator of insulin exocytosis from pancreatic islet beta cells. J. Biol. Chem. 283, 17939-17945
    • (2008) J. Biol. Chem. , vol.283 , pp. 17939-17945
    • Lopez, J.A.1    Kwan, E.P.2    Xie, L.3    He, Y.4    James, D.E.5    Gaisano, H.Y.6
  • 55
    • 34548188298 scopus 로고    scopus 로고
    • Activation of RalA is required for insulin-stimulated Glut4 trafficking to the plasma membrane via the exocyst and the motor protein Myo1c
    • Chen, X.W., Leto, D., Chiang, S.H., Wang, Q., and Saltiel, A.R. (2007) Activation of RalA is required for insulin-stimulated Glut4 trafficking to the plasma membrane via the exocyst and the motor protein Myo1c. Dev. Cell 13, 391-404
    • (2007) Dev. Cell , vol.13 , pp. 391-404
    • Chen, X.W.1    Leto, D.2    Chiang, S.H.3    Wang, Q.4    Saltiel, A.R.5
  • 57
    • 79953189734 scopus 로고    scopus 로고
    • Control of secondary granule release in neutrophils by Ral GTPase
    • Chen, C.X., Soto, I., Guo, Y.L., and Liu, Y. (2011) Control of secondary granule release in neutrophils by Ral GTPase. J. Biol. Chem. 286, 11724-11733
    • (2011) J. Biol. Chem. , vol.286 , pp. 11724-11733
    • Chen, C.X.1    Soto, I.2    Guo, Y.L.3    Liu, Y.4
  • 59
    • 33646123087 scopus 로고    scopus 로고
    • Dual role of the exocyst in AMPA receptor targeting and insertion into the postsynaptic membrane
    • Gerges, N.Z., Backos, D.S., Rupasinghe, C.N., Spaller, M.R., and Esteban, J.A. (2006) Dual role of the exocyst in AMPA receptor targeting and insertion into the postsynaptic membrane. EMBO J. 25, 1623-1634
    • (2006) EMBO J. , vol.25 , pp. 1623-1634
    • Gerges, N.Z.1    Backos, D.S.2    Rupasinghe, C.N.3    Spaller, M.R.4    Esteban, J.A.5
  • 61
    • 0036178046 scopus 로고    scopus 로고
    • Ral-GTPase influences the regulation of the readily releasable pool of synaptic vesicles
    • Polzin, A., Shipitsin, M., Goi, T., Feig, L.A., and Turner, T.J. (2002) Ral-GTPase influences the regulation of the readily releasable pool of synaptic vesicles. Mol. Cell. Biol. 22, 1714-1722
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1714-1722
    • Polzin, A.1    Shipitsin, M.2    Goi, T.3    Feig, L.A.4    Turner, T.J.5
  • 62
    • 0032577562 scopus 로고    scopus 로고
    • Sec6/8 complex is recruited to cellcell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells
    • Grindstaff, K.K., Yeaman, C., Anandasabapathy, N., Hsu, S.C., Rodriguez-Boulan, E., Scheller, R.H., and Nelson, W.J. (1998) Sec6/8 complex is recruited to cellcell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells. Cell 93, 731-740
    • (1998) Cell , vol.93 , pp. 731-740
    • Grindstaff, K.K.1    Yeaman, C.2    Anandasabapathy, N.3    Hsu, S.C.4    Rodriguez-Boulan, E.5    Scheller, R.H.6    Nelson, W.J.7
  • 63
    • 2942711520 scopus 로고    scopus 로고
    • RalA but not RalB enhances polarized delivery of membrane proteins to the basolateral surface of epithelial cells
    • Shipitsin, M. and Feig, L.A. (2004) RalA but not RalB enhances polarized delivery of membrane proteins to the basolateral surface of epithelial cells. Mol. Cell. Biol. 24, 5746-5756
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5746-5756
    • Shipitsin, M.1    Feig, L.A.2
  • 68
    • 2542476025 scopus 로고    scopus 로고
    • RalA activation at nascent lamellipodia of epidermal growth factor-stimulated Cos7 cells and migrating Madin-Darby canine kidney cells
    • Takaya, A., Ohba, Y., Kurokawa, K., and Matsuda, M. (2004) RalA activation at nascent lamellipodia of epidermal growth factor-stimulated Cos7 cells and migrating Madin-Darby canine kidney cells. Mol. Biol. Cell 15, 2549-2557
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2549-2557
    • Takaya, A.1    Ohba, Y.2    Kurokawa, K.3    Matsuda, M.4
  • 69
    • 53349175462 scopus 로고    scopus 로고
    • Ral-regulated interaction between Sec5 and paxillin targets Exocyst to focal complexes during cell migration
    • Spiczka, K.S. and Yeaman, C. (2008) Ral-regulated interaction between Sec5 and paxillin targets Exocyst to focal complexes during cell migration. J. Cell Sci. 121, 2880-2891
    • (2008) J. Cell Sci. , vol.121 , pp. 2880-2891
    • Spiczka, K.S.1    Yeaman, C.2
  • 70
    • 26244439675 scopus 로고    scopus 로고
    • Centriolin anchoring of exocyst and SNARE complexes at the midbody is required for secretory-vesicle-mediated abscission
    • Gromley, A., Yeaman, C., Rosa, J., Redick, S., Chen, C.T., Mirabelle, S., Guha, M., Sillibourne, J., and Doxsey, S.J. (2005) Centriolin anchoring of exocyst and SNARE complexes at the midbody is required for secretory-vesicle-mediated abscission. Cell 123, 75-87
    • (2005) Cell , vol.123 , pp. 75-87
    • Gromley, A.1    Yeaman, C.2    Rosa, J.3    Redick, S.4    Chen, C.T.5    Mirabelle, S.6    Guha, M.7    Sillibourne, J.8    Doxsey, S.J.9
  • 71
    • 51949085937 scopus 로고    scopus 로고
    • Distinct roles of RalA and RalB in the progression of cytokinesis are supported by distinct RalGEFs
    • Cascone, I., Selimoglu, R., Ozdemir, C., Del Nery, E., Yeaman, C., White, M., and Camonis, J. (2008) Distinct roles of RalA and RalB in the progression of cytokinesis are supported by distinct RalGEFs. EMBO J. 27, 2375-2387
    • (2008) EMBO J. , vol.27 , pp. 2375-2387
    • Cascone, I.1    Selimoglu, R.2    Ozdemir, C.3    Del Nery, E.4    Yeaman, C.5    White, M.6    Camonis, J.7
  • 72
    • 33751538120 scopus 로고    scopus 로고
    • Exo70 interacts with the Arp2/3 complex and regulates cell migration
    • Zuo, X., Zhang, J., Zhang, Y., Hsu, S.C., Zhou, D., and Guo, W. (2006) Exo70 interacts with the Arp2/3 complex and regulates cell migration. Nat. Cell Biol. 8, 1383-1388
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1383-1388
    • Zuo, X.1    Zhang, J.2    Zhang, Y.3    Hsu, S.C.4    Zhou, D.5    Guo, W.6
  • 73
    • 28544437382 scopus 로고    scopus 로고
    • Ral GTPases regulate neurite branching through GAP-43 and the exocyst complex
    • Lalli, G. and Hall, A. (2005) Ral GTPases regulate neurite branching through GAP-43 and the exocyst complex. J. Cell Biol. 171, 857-869
    • (2005) J. Cell Biol. , vol.171 , pp. 857-869
    • Lalli, G.1    Hall, A.2
  • 74
    • 0029001797 scopus 로고
    • Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases
    • Cantor, S.B., Urano, T., and Feig, L.A. (1995) Identification and characterization of Ral-binding protein 1, a potential downstream target of Ral GTPases. Mol. Cell. Biol. 15, 4578-4584
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4578-4584
    • Cantor, S.B.1    Urano, T.2    Feig, L.A.3
  • 76
    • 0031465736 scopus 로고    scopus 로고
    • An Eps homology (EH) domain protein that binds to the Ral-GTPase target, RalBP1
    • Yamaguchi, A., Urano, T., Goi, T., and Feig, L.A. (1997) An Eps homology (EH) domain protein that binds to the Ral-GTPase target, RalBP1. J. Biol. Chem. 272, 31230-31234
    • (1997) J. Biol. Chem. , vol.272 , pp. 31230-31234
    • Yamaguchi, A.1    Urano, T.2    Goi, T.3    Feig, L.A.4
  • 77
    • 0031974491 scopus 로고    scopus 로고
    • Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral
    • Ikeda, M., Ishida, O., Hinoi, T., Kishida, S., and Kikuchi, A. (1998) Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral. J. Biol. Chem. 273, 814-821
    • (1998) J. Biol. Chem. , vol.273 , pp. 814-821
    • Ikeda, M.1    Ishida, O.2    Hinoi, T.3    Kishida, S.4    Kikuchi, A.5
  • 78
    • 0033592669 scopus 로고    scopus 로고
    • Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis
    • Morinaka, K., Koyama, S., Nakashima, S., Hinoi, T., Okawa, K., Iwamatsu, A., and Kikuchi, A. (1999) Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis. Oncogene 18, 5915-5922
    • (1999) Oncogene , vol.18 , pp. 5915-5922
    • Morinaka, K.1    Koyama, S.2    Nakashima, S.3    Hinoi, T.4    Okawa, K.5    Iwamatsu, A.6    Kikuchi, A.7
  • 79
    • 0033832942 scopus 로고    scopus 로고
    • RLIP76, an effector of the GTPase Ral, interacts with the AP2 complex: Involvement of the Ral pathway in receptor endocytosis
    • Jullien-Flores, V., Mahe, Y., Mirey, G., Leprince, C., Meunier-Bisceuil, B., Sorkin, A., and Camonis, J.H. (2000) RLIP76, an effector of the GTPase Ral, interacts with the AP2 complex: involvement of the Ral pathway in receptor endocytosis. J. Cell Sci. 113 (Pt 16), 2837-2844
    • (2000) J. Cell Sci. , vol.113 , pp. 2837-2844
    • Jullien-Flores, V.1    Mahe, Y.2    Mirey, G.3    Leprince, C.4    Meunier-Bisceuil, B.5    Sorkin, A.6    Camonis, J.H.7
  • 81
    • 84867496141 scopus 로고    scopus 로고
    • RALBP1/RLIP76 depletion in mice suppresses tumor growth by inhibiting tumor neovascularization
    • Lee, S., Wurtzel, J.G., Singhal, S.S., Awasthi, S., and Goldfinger, L.E. (2012) RALBP1/RLIP76 depletion in mice suppresses tumor growth by inhibiting tumor neovascularization. Cancer Res. 72, 5165-5173
    • (2012) Cancer Res. , vol.72 , pp. 5165-5173
    • Lee, S.1    Wurtzel, J.G.2    Singhal, S.S.3    Awasthi, S.4    Goldfinger, L.E.5
  • 84
    • 0042023468 scopus 로고    scopus 로고
    • Transport of glutathione conjugates and chemotherapeutic drugs by RLIP76 (RALBP1): A novel link between G-protein and tyrosine kinase signaling and drug resistance
    • Awasthi, S., Singhal, S.S., Sharma, R., Zimniak, P., and Awasthi, Y.C. (2003) Transport of glutathione conjugates and chemotherapeutic drugs by RLIP76 (RALBP1): A novel link between G-protein and tyrosine kinase signaling and drug resistance. Int. J. Cancer 106, 635-646
    • (2003) Int. J. Cancer , vol.106 , pp. 635-646
    • Awasthi, S.1    Singhal, S.S.2    Sharma, R.3    Zimniak, P.4    Awasthi, Y.C.5
  • 86
    • 0028818914 scopus 로고
    • Involvement of Ral GTPase in v-Src-induced phospholipase D activation
    • Jiang, H., Luo, J.Q., Urano, T., Frankel, P., Lu, Z., Foster, D.A., and Feig, L.A. (1995) Involvement of Ral GTPase in v-Src-induced phospholipase D activation. Nature 378, 409-412
    • (1995) Nature , vol.378 , pp. 409-412
    • Jiang, H.1    Luo, J.Q.2    Urano, T.3    Frankel, P.4    Lu, Z.5    Foster, D.A.6    Feig, L.A.7
  • 89
    • 13244260780 scopus 로고    scopus 로고
    • RalA interacts with ZONAB in a cell density-dependent manner and regulates its transcriptional activity
    • Frankel, P., Aronheim, A., Kavanagh, E., Balda, M.S., Matter, K., Bunney, T.D., and Marshall, C.J. (2005) RalA interacts with ZONAB in a cell density-dependent manner and regulates its transcriptional activity. EMBO J. 24, 54-62
    • (2005) EMBO J. , vol.24 , pp. 54-62
    • Frankel, P.1    Aronheim, A.2    Kavanagh, E.3    Balda, M.S.4    Matter, K.5    Bunney, T.D.6    Marshall, C.J.7
  • 97
    • 84859778293 scopus 로고    scopus 로고
    • MTOR signaling in growth control and disease
    • Laplante, M. and Sabatini, D.M. (2012) mTOR signaling in growth control and disease. Cell 149, 274-293
    • (2012) Cell , vol.149 , pp. 274-293
    • Laplante, M.1    Sabatini, D.M.2
  • 98
    • 58049216316 scopus 로고    scopus 로고
    • RalA functions as an indispensable signal mediator for the nutrient-sensing system
    • Maehama, T., Tanaka, M., Nishina, H., Murakami, M., Kanaho, Y., and Hanada, K. (2008) RalA functions as an indispensable signal mediator for the nutrient-sensing system. J. Biol. Chem. 283, 35053-35059
    • (2008) J. Biol. Chem. , vol.283 , pp. 35053-35059
    • Maehama, T.1    Tanaka, M.2    Nishina, H.3    Murakami, M.4    Kanaho, Y.5    Hanada, K.6
  • 99
    • 84892853050 scopus 로고    scopus 로고
    • Ral and Rheb GTPase activating proteins integrate mTOR and GTPase signaling in aging, autophagy, and tumor cell invasion
    • Martin, T.D., Chen, X.W., Kaplan, R.E., Saltiel, A.R., Walker, C.L., Reiner, D.J., and Der, C.J. (2014) Ral and Rheb GTPase activating proteins integrate mTOR and GTPase signaling in aging, autophagy, and tumor cell invasion. Mol. Cell 53, 209-220
    • (2014) Mol. Cell , vol.53 , pp. 209-220
    • Martin, T.D.1    Chen, X.W.2    Kaplan, R.E.3    Saltiel, A.R.4    Walker, C.L.5    Reiner, D.J.6    Der, C.J.7
  • 100
    • 79960387847 scopus 로고    scopus 로고
    • Phospholipase D mediates nutrient input to mammalian target of rapamycin complex 1 (mTORC1)
    • Xu, L., Salloum, D., Medlin, P.S., Saqcena, M., Yellen, P., Perrella, B., and Foster, D.A. (2011) Phospholipase D mediates nutrient input to mammalian target of rapamycin complex 1 (mTORC1). J. Biol. Chem. 286, 25477-25486
    • (2011) J. Biol. Chem. , vol.286 , pp. 25477-25486
    • Xu, L.1    Salloum, D.2    Medlin, P.S.3    Saqcena, M.4    Yellen, P.5    Perrella, B.6    Foster, D.A.7
  • 103
    • 4344646902 scopus 로고    scopus 로고
    • Species-and cell type-specific requirements for cellular transformation
    • Rangarajan, A., Hong, S.J., Gifford, A., and Weinberg, R.A. (2004) Species-and cell type-specific requirements for cellular transformation. Cancer Cell 6, 171-183
    • (2004) Cancer Cell , vol.6 , pp. 171-183
    • Rangarajan, A.1    Hong, S.J.2    Gifford, A.3    Weinberg, R.A.4
  • 105
    • 78651380816 scopus 로고    scopus 로고
    • Activation and involvement of Ral GTPases in colorectal cancer
    • Martin, T.D., Samuel, J.C., Routh, E.D., Der, C.J., and Yeh, J.J. (2011) Activation and involvement of Ral GTPases in colorectal cancer. Cancer Res. 71, 206-215
    • (2011) Cancer Res. , vol.71 , pp. 206-215
    • Martin, T.D.1    Samuel, J.C.2    Routh, E.D.3    Der, C.J.4    Yeh, J.J.5
  • 111
    • 0034899045 scopus 로고    scopus 로고
    • Signal pathways which promote invasion and metastasis: Critical and distinct contributions of extracellular signal-regulated kinase and Ral-specific guanine exchange factor pathways
    • Ward, Y., Wang, W., Woodhouse, E., Linnoila, I., Liotta, L., and Kelly, K. (2001) Signal pathways which promote invasion and metastasis: critical and distinct contributions of extracellular signal-regulated kinase and Ral-specific guanine exchange factor pathways. Mol. Cell. Biol. 21, 5958-5969
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5958-5969
    • Ward, Y.1    Wang, W.2    Woodhouse, E.3    Linnoila, I.4    Liotta, L.5    Kelly, K.6
  • 112
    • 35648970538 scopus 로고    scopus 로고
    • Activation of the RalGEF/Ral pathway promotes prostate cancer metastasis to bone
    • Yin, J., Pollock, C., Tracy, K., Chock, M., Martin, P., Oberst, M., and Kelly, K. (2007) Activation of the RalGEF/Ral pathway promotes prostate cancer metastasis to bone. Mol. Cell. Biol. 27, 7538-7550
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 7538-7550
    • Yin, J.1    Pollock, C.2    Tracy, K.3    Chock, M.4    Martin, P.5    Oberst, M.6    Kelly, K.7
  • 113
    • 33845448647 scopus 로고    scopus 로고
    • Divergent roles for RalA and RalB in malignant growth of human pancreatic carcinoma cells
    • Lim, K.H., O'Hayer, K., Adam, S.J., Kendall, S.D., Campbell, P.M., Der, C.J., and Counter, C.M. (2006) Divergent roles for RalA and RalB in malignant growth of human pancreatic carcinoma cells. Curr. Biol. 16, 2385-2394
    • (2006) Curr. Biol. , vol.16 , pp. 2385-2394
    • Lim, K.H.1    O'Hayer, K.2    Adam, S.J.3    Kendall, S.D.4    Campbell, P.M.5    Der, C.J.6    Counter, C.M.7
  • 115
    • 77249083257 scopus 로고    scopus 로고
    • Sec5 and Exo84 foster oncogenic ras-mediated tumorigenesis
    • Issaq, S.H., Lim, K.H., and Counter, C.M. (2010) Sec5 and Exo84 foster oncogenic ras-mediated tumorigenesis. Mol. Cancer Res. 8, 223-231
    • (2010) Mol. Cancer Res. , vol.8 , pp. 223-231
    • Issaq, S.H.1    Lim, K.H.2    Counter, C.M.3
  • 116
  • 117
    • 69949103110 scopus 로고    scopus 로고
    • The role of the exocyst in matrix metalloproteinase secretion and actin dynamics during tumor cell invadopodia formation
    • Liu, J., Yue, P., Artym, V.V., Mueller, S.C., and Guo, W. (2009) The role of the exocyst in matrix metalloproteinase secretion and actin dynamics during tumor cell invadopodia formation. Mol. Biol. Cell 20, 3763-3771
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3763-3771
    • Liu, J.1    Yue, P.2    Artym, V.V.3    Mueller, S.C.4    Guo, W.5
  • 122
    • 84909952634 scopus 로고    scopus 로고
    • Ral GTPase down-regulation stabilizes and reactivates p53 to inhibit malignant transformation
    • Tecleab, A., Zhang, X., and Sebti, S.M. (2014) Ral GTPase Down-regulation Stabilizes and Reactivates p53 to Inhibit Malignant Transformation. J. Biol. Chem. 289, 31296-31309
    • (2014) J. Biol. Chem. , vol.289 , pp. 31296-31309
    • Tecleab, A.1    Zhang, X.2    Sebti, S.M.3
  • 123
    • 78951475020 scopus 로고    scopus 로고
    • P53 and its mutants in tumor cell migration and invasion
    • Muller, P.A., Vousden, K.H., and Norman, J.C. (2011) p53 and its mutants in tumor cell migration and invasion. J. Cell Biol. 192, 209-218
    • (2011) J. Cell Biol. , vol.192 , pp. 209-218
    • Muller, P.A.1    Vousden, K.H.2    Norman, J.C.3
  • 124
    • 78049370949 scopus 로고    scopus 로고
    • Aberrant overexpression of the Rgl2 Ral small GTPase-specific guanine nucleotide exchange factor promotes pancreatic cancer growth through Ral-dependent and Ral-independent mechanisms
    • Vigil, D., Martin, T.D., Williams, F., Yeh, J.J., Campbell, S.L., and Der, C.J. (2010) Aberrant overexpression of the Rgl2 Ral small GTPase-specific guanine nucleotide exchange factor promotes pancreatic cancer growth through Ral-dependent and Ral-independent mechanisms. J. Biol. Chem. 285, 34729-34740
    • (2010) J. Biol. Chem. , vol.285 , pp. 34729-34740
    • Vigil, D.1    Martin, T.D.2    Williams, F.3    Yeh, J.J.4    Campbell, S.L.5    Der, C.J.6
  • 125
    • 20444475352 scopus 로고    scopus 로고
    • Downregulation of human DAB2IP gene expression mediated by polycomb Ezh2 complex and histone deacetylase in prostate cancer
    • Chen, H., Tu, S.W., and Hsieh, J.T. (2005) Downregulation of human DAB2IP gene expression mediated by polycomb Ezh2 complex and histone deacetylase in prostate cancer. J. Biol. Chem. 280, 22437-22444
    • (2005) J. Biol. Chem. , vol.280 , pp. 22437-22444
    • Chen, H.1    Tu, S.W.2    Hsieh, J.T.3
  • 127
    • 20144373746 scopus 로고    scopus 로고
    • Identification of V23RalA-Ser194 as a critical mediator for Aurora-A-induced cellular motility and transformation by small pool expression screening
    • Wu, J.C., Chen, T.Y., Yu, C.T., Tsai, S.J., Hsu, J.M., Tang, M.J., Chou, C.K., Lin, W.J., Yuan, C.J., and Huang, C.Y. (2005) Identification of V23RalA-Ser194 as a critical mediator for Aurora-A-induced cellular motility and transformation by small pool expression screening. J. Biol. Chem. 280, 9013-9022
    • (2005) J. Biol. Chem. , vol.280 , pp. 9013-9022
    • Wu, J.C.1    Chen, T.Y.2    Yu, C.T.3    Tsai, S.J.4    Hsu, J.M.5    Tang, M.J.6    Chou, C.K.7    Lin, W.J.8    Yuan, C.J.9    Huang, C.Y.10
  • 130
    • 84862084695 scopus 로고    scopus 로고
    • Phosphorylation by protein kinase Calpha regulates RalB small GTPase protein activation, subcellular localization, and effector utilization
    • Martin, T.D., Mitin, N., Cox, A.D., Yeh, J.J., and Der, C.J. (2012) Phosphorylation by protein kinase Calpha regulates RalB small GTPase protein activation, subcellular localization, and effector utilization. J. Biol. Chem. 287, 14827-14836
    • (2012) J. Biol. Chem. , vol.287 , pp. 14827-14836
    • Martin, T.D.1    Mitin, N.2    Cox, A.D.3    Yeh, J.J.4    Der, C.J.5
  • 131
    • 78449292864 scopus 로고    scopus 로고
    • Phosphorylation of RalB is important for bladder cancer cell growth and metastasis
    • Wang, H., Owens, C., Chandra, N., Conaway, M.R., Brautigan, D.L., and Theodorescu, D. (2010) Phosphorylation of RalB is important for bladder cancer cell growth and metastasis. Cancer Res. 70, 8760-8769
    • (2010) Cancer Res. , vol.70 , pp. 8760-8769
    • Wang, H.1    Owens, C.2    Chandra, N.3    Conaway, M.R.4    Brautigan, D.L.5    Theodorescu, D.6
  • 132
    • 84868593574 scopus 로고    scopus 로고
    • Genetic deletion of RALA and RALB small GTPases reveals redundant functions in development and tumorigenesis
    • Peschard, P., McCarthy, A., Leblanc-Dominguez, V., Yeo, M., Guichard, S., Stamp, G., and Marshall, C.J. (2012) Genetic deletion of RALA and RALB small GTPases reveals redundant functions in development and tumorigenesis. Curr. Biol. 22, 2063-2068
    • (2012) Curr. Biol. , vol.22 , pp. 2063-2068
    • Peschard, P.1    McCarthy, A.2    Leblanc-Dominguez, V.3    Yeo, M.4    Guichard, S.5    Stamp, G.6    Marshall, C.J.7
  • 134
    • 0030774573 scopus 로고    scopus 로고
    • The geranylgeranyltransferase-I inhibitor GGTI-298 arrests human tumor cells in G0/G1 and induces p21(WAF1/CIP1/SDI1) in a p53-independent manner
    • Vogt, A., Sun, J., Qian, Y., Hamilton, A.D., and Sebti, S.M. (1997) The geranylgeranyltransferase-I inhibitor GGTI-298 arrests human tumor cells in G0/G1 and induces p21(WAF1/CIP1/SDI1) in a p53-independent manner. J. Biol. Chem. 272, 27224-27229
    • (1997) J. Biol. Chem. , vol.272 , pp. 27224-27229
    • Vogt, A.1    Sun, J.2    Qian, Y.3    Hamilton, A.D.4    Sebti, S.M.5
  • 138
    • 84888639050 scopus 로고    scopus 로고
    • K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions
    • Ostrem, J.M., Peters, U., Sos, M.L., Wells, J.A., and Shokat, K.M. (2013) K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions. Nature 503, 548-551
    • (2013) Nature , vol.503 , pp. 548-551
    • Ostrem, J.M.1    Peters, U.2    Sos, M.L.3    Wells, J.A.4    Shokat, K.M.5


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