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Volumn 9, Issue 2-4, 1998, Pages 167-196

The Role Of G Proteins In Insulin Signalling

Author keywords

G proteins; glucose uptake; insulin; membrane traffic

Indexed keywords

GLUCOSE TRANSPORTER; GUANINE NUCLEOTIDE BINDING PROTEIN; INSULIN; INSULIN RECEPTOR; INSULIN RECEPTOR SUBSTRATE 1; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOLIPASE D; PROTEIN TYROSINE KINASE; RAB PROTEIN; RHO FACTOR;

EID: 0032463762     PISSN: 07926855     EISSN: 21910286     Source Type: Journal    
DOI: 10.1515/JBCPP.1998.9.2-4.167     Document Type: Article
Times cited : (13)

References (159)
  • 1
    • 0001489445 scopus 로고
    • Tyrosine-specific protein kinase activity is associated with purified insulin receptor
    • Kasuga, M., Fujita-Yamaguchi, Y., Blithe, D., Kahn, CR. Tyrosine-specific protein kinase activity is associated with purified insulin receptor. Proc Natl Acad Sci USA 1983; 80: 2137–2141.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 2137-2141
    • Kasuga, M.1    Fujita-Yamaguchi, Y.2    Blithe, D.3    Kahn, C.R.4
  • 2
    • 0020065416 scopus 로고
    • Insulin stimulates the phosphorylation of the 95000 dalton subunit of its own receptor
    • Kasuga, M., Karlsson, FA., Kahn, CR. Insulin stimulates the phosphorylation of the 95000 dalton subunit of its own receptor. Science 1982; 215: 185–187.
    • (1982) Science , vol.215 , pp. 185-187
    • Kasuga, M.1    Karlsson, F.A.2    Kahn, C.R.3
  • 3
    • 0020417020 scopus 로고
    • Insulin activates a tyrosine-specific protein kinase in extracts of 3T3-L1 adipocytes and human placenta
    • Petruzzelli, LM., Gangaly, S., Smith, CR., Cobb, MH., Rubin, CS., Rosen, OM. Insulin activates a tyrosine-specific protein kinase in extracts of 3T3-L1 adipocytes and human placenta. Proc Natl Acad Sci USA 1982; 79: 6792–6796.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 6792-6796
    • Petruzzelli, L.M.1    Gangaly, S.2    Smith, C.R.3    Cobb, M.H.4    Rubin, C.S.5    Rosen, O.M.6
  • 4
    • 0020420363 scopus 로고
    • Insulin-stimulated tyrosine phosphorylation of the insulin receptor in detergent extracts of human placental membranes
    • Avruch, J., Nemenoff, RA., Blackshear, PJ., Pierce, MW., Osathanondh, R. Insulin-stimulated tyrosine phosphorylation of the insulin receptor in detergent extracts of human placental membranes. J Biol Chem 1982; 257: 15162–15166.
    • (1982) J Biol Chem , vol.257 , pp. 15162-15166
    • Avruch, J.1    Nemenoff, R.A.2    Blackshear, P.J.3    Pierce, M.W.4    Osathanondh, R.5
  • 5
    • 0025837881 scopus 로고
    • Purification and partial sequence analysis of ppl85, the major cellular substrate of the insulin receptor
    • Rothenberg, PL., Lane, WS., Karasik, A., Backer, J., White, M., Kahn, CR. Purification and partial sequence analysis of ppl85, the major cellular substrate of the insulin receptor. J Biol Chem 1991; 266: 8302–8311.
    • (1991) J Biol Chem , vol.266 , pp. 8302-8311
    • Rothenberg, P.L.1    Lane, W.S.2    Karasik, A.3    Backer, J.4    White, M.5    Kahn, C.R.6
  • 8
    • 0027164156 scopus 로고
    • Human skeletal muscle insulin receptor substrate-1. Characterization of the cDNA, gene, and chromosomal localization
    • Araki, E. Sun, XJ., Haag, BL. 3rd, Chuang, LM. Zhang, Y., Yang-Feng, TL., White, MF., Kahn, CR. Human skeletal muscle insulin receptor substrate-1. Characterization of the cDNA, gene, and chromosomal localization. Diabetes 1993; 42: 1041–1054.
    • (1993) Diabetes , vol.42 , pp. 1041-1054
    • Araki, E.1    Sun, X.J.2    Haag, B.L.3    Chuang, L.M.4    Zhang, Y.5    Yang-Feng, T.L.6    White, M.F.7    Kahn, C.R.8
  • 9
    • 0028904053 scopus 로고
    • Insulin action and the insulin signaling network
    • Cheatham, B., Kahn, CR. Insulin action and the insulin signaling network. Endocr Rev 1995; 16: 117–142.
    • (1995) Endocr Rev , vol.16 , pp. 117-142
    • Cheatham, B.1    Kahn, C.R.2
  • 10
    • 0028810236 scopus 로고
    • 4PS/insulin receptor substrate (IRS)-2 is the alternative substrate of the insulin receptor in IRS-1-deficient mice
    • Patti, ME., Sun, XJ., Bruening, JC., Araki, E., Lipes, MA., White, MF., Kahn, CR. 4PS/insulin receptor substrate (IRS)-2 is the alternative substrate of the insulin receptor in IRS-1-deficient mice. J Biol Chem 1995; 270: 24670–24673.
    • (1995) J Biol Chem , vol.270 , pp. 24670-24673
    • Patti, M.E.1    Sun, X.J.2    Bruening, J.C.3    Araki, E.4    Lipes, M.A.5    White, M.F.6    Kahn, C.R.7
  • 12
    • 0030995946 scopus 로고    scopus 로고
    • The 60-kDa phosphotyrosine protein in insulin-treated adipocytes is a new member of the Insulin Receptor Substrate Family
    • Lavan, BE., Lane, WS., Lienhard, GE. The 60-kDa phosphotyrosine protein in insulin-treated adipocytes is a new member of the Insulin Receptor Substrate Family. J Biol Chem 1997; 272: 11439–11443.
    • (1997) J Biol Chem , vol.272 , pp. 11439-11443
    • Lavan, B.E.1    Lane, W.S.2    Lienhard, G.E.3
  • 13
    • 0030848782 scopus 로고    scopus 로고
    • A novel 160-kDa phosphotyrosine protein in insulin-treated embryonic kidney cells is a new member of the insulin receptor substrate family
    • Lavan, BE., Fantin, VR., Chang, ET., Lane, WS., Keller, SR. Lienhard, GE. A novel 160-kDa phosphotyrosine protein in insulin-treated embryonic kidney cells is a new member of the insulin receptor substrate family. J Biol Chem 1997; 272: 21403–21407.
    • (1997) J Biol Chem , vol.272 , pp. 21403-21407
    • Lavan, B.E.1    Fantin, V.R.2    Chang, E.T.3    Lane, W.S.4    Keller, S.R.5    Lienhard, G.E.6
  • 15
    • 0030028790 scopus 로고    scopus 로고
    • A Grb2-associated docking protein in EGF- and insulin-receptor signalling
    • Holgado-Madruga, M., Emlet, DR., Moscatello, DK., Godwin, AK., Wong, AJ. A Grb2-associated docking protein in EGF- and insulin-receptor signalling. Nature 1996; 379: 550–564.
    • (1996) Nature , vol.379 , pp. 550-564
    • Holgado-Madruga, M.1    Emlet, D.R.2    Moscatello, D.K.3    Godwin, A.K.4    Wong, A.J.5
  • 17
    • 0024245612 scopus 로고
    • Characterization of insulin-stimulated microtubule-associated protein kinase. Rapid isolation and stabilization of a novel serine/threonine kinase from 3T3-L1 cells
    • Ray, LB., Sturgill, TW. Characterization of insulin-stimulated microtubule-associated protein kinase. Rapid isolation and stabilization of a novel serine/threonine kinase from 3T3-L1 cells. J Biol Chem 1988; 263: 12721–12727.
    • (1988) J Biol Chem , vol.263 , pp. 12721-12727
    • Ray, L.B.1    Sturgill, T.W.2
  • 19
    • 0026775083 scopus 로고
    • Sequential activation of MAP kinase activator, MAP kinases, and S6 peptide kinase in intact rat liver following insulin injection
    • Tobe, K., Kadowaki, T., Hara, K., Gotoh, Y., Kosako, H., Matsuda, S., Tamemoto, H., Ueki, K., Akanuma, Y., Nishida, E. Sequential activation of MAP kinase activator, MAP kinases, and S6 peptide kinase in intact rat liver following insulin injection. J Biol Chem 1992; 267: 21089–21097.
    • (1992) J Biol Chem , vol.267 , pp. 21089-21097
    • Tobe, K.1    Kadowaki, T.2    Hara, K.3    Gotoh, Y.4    Kosako, H.5    Matsuda, S.6    Tamemoto, H.7    Ueki, K.8    Akanuma, Y.9    Nishida, E.10
  • 20
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering, BM., Coffer, PJ. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 1995; 376: 599–602.
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.M.1    Coffer, P.J.2
  • 22
    • 0022349019 scopus 로고
    • Action of insulin modulated by pertussis toxin in rat adipocytes
    • Goren, HJ., Northup, JK., Hollenberg, MD. Action of insulin modulated by pertussis toxin in rat adipocytes. Can J Physiol Pharmacol 1985; 63: 1017–1022.
    • (1985) Can J Physiol Pharmacol , vol.63 , pp. 1017-1022
    • Goren, H.J.1    Northup, J.K.2    Hollenberg, M.D.3
  • 23
    • 0023937363 scopus 로고
    • Pertussis toxin treatment attenuates some effects of insulin in BC3H-1 murine myocytes
    • Luttrell, L., Hewlett, E., Romero, G., Rogol, A. Pertussis toxin treatment attenuates some effects of insulin in BC3H-1 murine myocytes. J Biol Chem 1988; 263: 6134–6142.
    • (1988) J Biol Chem , vol.263 , pp. 6134-6142
    • Luttrell, L.1    Hewlett, E.2    Romero, G.3    Rogol, A.4
  • 24
    • 0025026471 scopus 로고
    • A pertussis toxin sensitive G-protein mediates insulin action in murine BC3H1 myocytes
    • Luttrell, LM., Kilgour, E., Larner, J., Romero, G. A pertussis toxin sensitive G-protein mediates insulin action in murine BC3H1 myocytes. J Biol Chem 1990; 265: 16873–16879.
    • (1990) J Biol Chem , vol.265 , pp. 16873-16879
    • Luttrell, L.M.1    Kilgour, E.2    Larner, J.3    Romero, G.4
  • 25
    • 0025153039 scopus 로고
    • Pertussis toxin catalyzed ADP-ribosylation of a 41 kDa G-protein impairs insulin-stimulated glucose metabolism in BC3H-1 myocytes
    • Moises, RS., Heidenreich, KA. Pertussis toxin catalyzed ADP-ribosylation of a 41 kDa G-protein impairs insulin-stimulated glucose metabolism in BC3H-1 myocytes. J Cell Physiol 1990; 144: 538–545.
    • (1990) J Cell Physiol , vol.144 , pp. 538-545
    • Moises, R.S.1    Heidenreich, K.A.2
  • 26
    • 0024294407 scopus 로고
    • The phosphat-idylinositol-glycan anchors of membrane proteins: Potential precursors of insulin mediators
    • Romero, G., Luttrell, L., Rogol, A., Zeller, K., Hewlett, E., Larner, J. The phosphat-idylinositol-glycan anchors of membrane proteins: Potential precursors of insulin mediators. Science 1988; 240: 509–511.
    • (1988) Science , vol.240 , pp. 509-511
    • Romero, G.1    Luttrell, L.2    Rogol, A.3    Zeller, K.4    Hewlett, E.5    Larner, J.6
  • 27
    • 0025082688 scopus 로고
    • Insulin activates glycerol-3-phosphate acyltransferase (de novo phosphatidic acid synthesis) through a phospholipid-derived mediator. Apparent involvement of Gi alpha and activation of a phospholipase C
    • Vila, MC., Milligan, G., Standaert, ML., Farese, RV. Insulin activates glycerol-3-phosphate acyltransferase (de novo phosphatidic acid synthesis) through a phospholipid-derived mediator. Apparent involvement of Gi alpha and activation of a phospholipase C. Biochemistry 1990; 29: 8735–8740.
    • (1990) Biochemistry , vol.29 , pp. 8735-8740
    • Vila, M.C.1    Milligan, G.2    Standaert, M.L.3    Farese, R.V.4
  • 28
    • 0020959271 scopus 로고
    • Insulin exerts actions through a distinct species of guanine nucleotide regulatory protein: inhibition of adenylate cyclase
    • Heyworth, CM., Houslay, MD. Insulin exerts actions through a distinct species of guanine nucleotide regulatory protein: inhibition of adenylate cyclase. Biochem J 1983; 214: 547–552.
    • (1983) Biochem J , vol.214 , pp. 547-552
    • Heyworth, C.M.1    Houslay, M.D.2
  • 29
    • 0027401974 scopus 로고
    • The role of inositolglycan mediators in the modulation of steroidogenesis by insulin and insulin-like growth factor 1
    • Romero, G., Garmey, J., Veldhuis, J. The role of inositolglycan mediators in the modulation of steroidogenesis by insulin and insulin-like growth factor 1. Endocrinology 1993; 132: 1561–1568.
    • (1993) Endocrinology , vol.132 , pp. 1561-1568
    • Romero, G.1    Garmey, J.2    Veldhuis, J.3
  • 30
    • 0027129815 scopus 로고
    • The generation of inositolglycan mediators from rat liver plasma membranes: the role of guanine nucleotide binding proteins
    • Kilgour, E., Larner, J., Romero, G. The generation of inositolglycan mediators from rat liver plasma membranes: the role of guanine nucleotide binding proteins. Biochem Biophys Res Comm 1992; 186: 1151–1157.
    • (1992) Biochem Biophys Res Comm , vol.186 , pp. 1151-1157
    • Kilgour, E.1    Larner, J.2    Romero, G.3
  • 31
    • 0025695118 scopus 로고
    • G-protein-mediated regulation of the insulin-responsive glucose transporter in isolated cardiac myocytes
    • Eckel, J. Gerlach-Eskuchen, E. Reinauer, H. G-protein-mediated regulation of the insulin-responsive glucose transporter in isolated cardiac myocytes. Biochem J 1990; 272: 691–696.
    • (1990) Biochem J , vol.272 , pp. 691-696
    • Eckel, J.1    Gerlach-Eskuchen, E.2    Reinauer, H.3
  • 32
    • 0023708658 scopus 로고
    • Insulin inhibits pertussis toxin-catalyzed ADP-ribosylation of G-proteins. Evidence for a novel interaction between insulin receptors and G-proteins
    • Rothenberg, PL., Kahn, CR. Insulin inhibits pertussis toxin-catalyzed ADP-ribosylation of G-proteins. Evidence for a novel interaction between insulin receptors and G-proteins. J Biol Chem 1988; 263: 15546–15552.
    • (1988) J Biol Chem , vol.263 , pp. 15546-15552
    • Rothenberg, P.L.1    Kahn, C.R.2
  • 35
    • 0025063738 scopus 로고
    • Insulin receptor function is inhibited by guanosine 5'-[Y-thio]triphosphate (GTP[S])
    • Davis, HW., McDonald, JM. Insulin receptor function is inhibited by guanosine 5'-[Y-thio]triphosphate (GTP[S]). Biochem J 1990; 270: 401–407.
    • (1990) Biochem J , vol.270 , pp. 401-407
    • Davis, H.W.1    McDonald, J.M.2
  • 36
    • 0025685604 scopus 로고
    • Insulin activates guanosine 5'-[Y-thio] triphosphate (GTPYS) binding to a novel GTP-binding protein, GIR, from human placenta
    • Srivastava, SK., Singh, US. Insulin activates guanosine 5'-[Y-thio] triphosphate (GTPYS) binding to a novel GTP-binding protein, GIR, from human placenta. Biochem Biophys Res Comm 1990; 173: 501–506.
    • (1990) Biochem Biophys Res Comm , vol.173 , pp. 501-506
    • Srivastava, S.K.1    Singh, U.S.2
  • 37
    • 0023252211 scopus 로고
    • Insulin stimulates a novel GTPase activity in human platelets
    • Gawler, D., Houslay, MD. Insulin stimulates a novel GTPase activity in human platelets. FEBS Lett 1987; 216: 94–98.
    • (1987) FEBS Lett , vol.216 , pp. 94-98
    • Gawler, D.1    Houslay, M.D.2
  • 38
    • 0025186824 scopus 로고
    • Effect of GTP gamma S on insulin binding and tyrosine phosphorylation in liver membranes and L6 muscle cells
    • Burdett, E., Mills, GB., Klip, A. Effect of GTP gamma S on insulin binding and tyrosine phosphorylation in liver membranes and L6 muscle cells. Am J Physiol 1990; 258: C99-C108.
    • (1990) Am J Physiol , vol.258
    • Burdett, E.1    Mills, G.B.2    Klip, A.3
  • 39
    • 0028258162 scopus 로고
    • Guanosine 5'-(Yma-thio) triphosphate (GTPS) inhibits phosphorylation of insulin receptor and a novel GTP-binding protein, Gir, from human placenta
    • Srivastava, SK., Varma, TK., Sinha, AC., Singh, US. Guanosine 5'-(Yma-thio) triphosphate (GTPS) inhibits phosphorylation of insulin receptor and a novel GTP-binding protein, Gir, from human placenta. FEBS Lett 1994; 340: 124–128.
    • (1994) FEBS Lett , vol.340 , pp. 124-128
    • Srivastava, S.K.1    Varma, T.K.2    Sinha, A.C.3    Singh, U.S.4
  • 40
    • 0026467250 scopus 로고
    • Identification, partial purification, and characterization of two guanosine triphosphate-binding proteins associated with insulin receptors
    • Jo, H., Cha, BY., Davis, HW., McDonald, JM. Identification, partial purification, and characterization of two guanosine triphosphate-binding proteins associated with insulin receptors. Endocrinology 1992; 131: 2855–2862.
    • (1992) Endocrinology , vol.131 , pp. 2855-2862
    • Jo, H.1    Cha, B.Y.2    Davis, H.W.3    McDonald, J.M.4
  • 42
    • 0027185664 scopus 로고
    • An insulin receptor peptide (1135-1156) stimulates guanosine 5'-[γ-thio]triphosphate binding to the 67 kDa G-protein associated with the insulin receptor
    • Jo, H., Radding, W., Anantharamaiah, GM., McDonald, JM. An insulin receptor peptide (1135-1156) stimulates guanosine 5'-[γ-thio]triphosphate binding to the 67 kDa G-protein associated with the insulin receptor. Biochem J 1993; 294: 19–24.
    • (1993) Biochem J , vol.294 , pp. 19-24
    • Jo, H.1    Radding, W.2    Anantharamaiah, G.M.3    McDonald, J.M.4
  • 45
    • 0025932251 scopus 로고
    • Two dominant inhibitory mutants of p21ras interfere with insulin-induced gene expression
    • Medema, RH., Wubbolts, R. Bos, JL. Two dominant inhibitory mutants of p21ras interfere with insulin-induced gene expression. Mol Cell Biol 1991; 11: 5963–5967.
    • (1991) Mol Cell Biol , vol.11 , pp. 5963-5967
    • Medema, R.H.1    Wubbolts, R.2    Bos, J.L.3
  • 46
    • 0027529827 scopus 로고
    • Ras activation by insulin and epidermal growth factor through enhanced exchange of guanine nucleotides on p21ras
    • Medema, RH., de Vries-Smits, AM., van der Zon, GC., Maassen, JA., Bos, JL. Ras activation by insulin and epidermal growth factor through enhanced exchange of guanine nucleotides on p21ras. Mol Cell Biol 1993; 13: 155–162.
    • (1993) Mol Cell Biol , vol.13 , pp. 155-162
    • Medema, R.H.1    de Vries-Smits, A.M.2    van der Zon, G.C.3    Maassen, J.A.4    Bos, J.L.5
  • 47
  • 48
    • 0027257212 scopus 로고
    • Insulin activates p21Ras and guanine nucleotide releasing factor in cells expressing wild type and mutant insulin receptors
    • Draznin, B. Chang, L., Leitner, JW., Takata, Y. Olefsky, JM. Insulin activates p21Ras and guanine nucleotide releasing factor in cells expressing wild type and mutant insulin receptors. J Biol Chem 1993; 268: 19998–20001.
    • (1993) J Biol Chem , vol.268 , pp. 19998-20001
    • Draznin, B.1    Chang, L.2    Leitner, J.W.3    Takata, Y.4    Olefsky, J.M.5
  • 49
    • 0027264112 scopus 로고
    • Activation of the mitogen-activated protein kinase pathway in Triton X-100 disrupted NIH-3T3 cells by p21 ras and in vitro by plasma membranes from NIH 3T3 cells
    • Dent, P., Wu, J., Romero, G., Vincent, LA., Castle, D. Sturgill, TW. Activation of the mitogen-activated protein kinase pathway in Triton X-100 disrupted NIH-3T3 cells by p21 ras and in vitro by plasma membranes from NIH 3T3 cells. Mol Biol Cell 1993; 4: 483–493.
    • (1993) Mol Biol Cell , vol.4 , pp. 483-493
    • Dent, P.1    Wu, J.2    Romero, G.3    Vincent, L.A.4    Castle, D.5    Sturgill, T.W.6
  • 50
    • 0026608238 scopus 로고
    • The son of sevenless gene product: a putative activator of Ras
    • Bonfni, L., Karlovich, CA., Dasgupta, C. Banerjee, U. The son of sevenless gene product: a putative activator of Ras. Science 1992; 255: 603–606.
    • (1992) Science , vol.255 , pp. 603-606
    • Bonfni, L.1    Karlovich, C.A.2    Dasgupta, C.3    Banerjee, U.4
  • 51
    • 0027404990 scopus 로고
    • An SH3-SH2-SH3 protein is required for p21Rasl activation and binds to sevenless and Sos proteins in vitro
    • Simon, MA., Dodson, GS., Rubin, GM. An SH3-SH2-SH3 protein is required for p21Rasl activation and binds to sevenless and Sos proteins in vitro. Cell 1993; 73: 169–177.
    • (1993) Cell , vol.73 , pp. 169-177
    • Simon, M.A.1    Dodson, G.S.2    Rubin, G.M.3
  • 53
    • 0027153103 scopus 로고
    • Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor
    • Buday, L., Downward, J. Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor. Cell 1993; 73: 611–620.
    • (1993) Cell , vol.73 , pp. 611-620
    • Buday, L.1    Downward, J.2
  • 55
    • 0027312272 scopus 로고
    • Guanine-nucelotide-releasing factor mSos1 binds to Grb2 and links receptor tyrosine kinases to ras signalling
    • Li, N., Batzer, A., Daly, R., Yajnik, V., Skolnik, E., Chardin, P., Bar-Sagi, B., Margolis, B., Schlessinger, J. Guanine-nucelotide-releasing factor mSos1 binds to Grb2 and links receptor tyrosine kinases to ras signalling. Nature 1993; 363: 85–88.
    • (1993) Nature , vol.363 , pp. 85-88
    • Li, N.1    Batzer, A.2    Daly, R.3    Yajnik, V.4    Skolnik, E.5    Chardin, P.6    Bar-Sagi, B.7    Margolis, B.8    Schlessinger, J.9
  • 56
    • 0027910431 scopus 로고
    • Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
    • Egan, SE., Giddings, BW., Brooks, MW., Buday, L., Sizeland, AM., Weinberg, RA. Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature 1993; 363: 45–51.
    • (1993) Nature , vol.363 , pp. 45-51
    • Egan, S.E.1    Giddings, B.W.2    Brooks, M.W.3    Buday, L.4    Sizeland, A.M.5    Weinberg, R.A.6
  • 59
    • 0028341446 scopus 로고
    • Shc is the predominant signaling molecule coupling insulin receptors to activation of guanine nucleotide releasing factor and p21ras-GTP formation
    • Sasaoka, T., Draznin, B., Leitner, JW., Langlois, WJ., Olefsky, JM. Shc is the predominant signaling molecule coupling insulin receptors to activation of guanine nucleotide releasing factor and p21ras-GTP formation. J Biol Chem 1994; 269: 10734–10738.
    • (1994) J Biol Chem , vol.269 , pp. 10734-10738
    • Sasaoka, T.1    Draznin, B.2    Leitner, J.W.3    Langlois, W.J.4    Olefsky, J.M.5
  • 61
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine kinase Raf
    • Vojtek, AB., Hollenberg, SM., Cooper, JA. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 1993; 74: 205–214.
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 62
    • 0027935756 scopus 로고
    • Interaction of Ras and Raf in intact mammalian cells upon extracellular stimulation
    • Hallberg, B., Rayter, SI., Downward, J. Interaction of Ras and Raf in intact mammalian cells upon extracellular stimulation. J Biol Chem 1994; 269: 3913–3916.
    • (1994) J Biol Chem , vol.269 , pp. 3913-3916
    • Hallberg, B.1    Rayter, S.I.2    Downward, J.3
  • 63
    • 0023013903 scopus 로고
    • Insulin-like growth factors, insulin, and epidermal growth factor cause rapid cytoskeletal reorganization in KB cells. Clarification of the roles of type I insulin-like growth factor receptors and insulin receptors
    • Kadowaki, T., Koyasu, S., Nishida, E., Sakai, H., Takaku, F., Yahara, I., Kasuga, M. Insulin-like growth factors, insulin, and epidermal growth factor cause rapid cytoskeletal reorganization in KB cells. Clarification of the roles of type I insulin-like growth factor receptors and insulin receptors. J Biol Chem 1986; 261: 16141–16147.
    • (1986) J Biol Chem , vol.261 , pp. 16141-16147
    • Kadowaki, T.1    Koyasu, S.2    Nishida, E.3    Sakai, H.4    Takaku, F.5    Yahara, I.6    Kasuga, M.7
  • 64
    • 0028258943 scopus 로고
    • rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor- and 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling in KB cells
    • Nishiyama, T., Sasaki, T., Takaishi, K., Kato, M., Yaku, H., Araki, K., Matsuura, Y., Takai, Y. rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor- and 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling in KB cells. Mol Cell Biol 1994; 14: 2447–2456.
    • (1994) Mol Cell Biol , vol.14 , pp. 2447-2456
    • Nishiyama, T.1    Sasaki, T.2    Takaishi, K.3    Kato, M.4    Yaku, H.5    Araki, K.6    Matsuura, Y.7    Takai, Y.8
  • 65
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, AJ., Hall, A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 1992; 70: 389–399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 66
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, AJ., Paterson, HF., Johnston, CL., Diekmann, D., Hall, A. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 1992; 70: 401–410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 67
    • 0025859983 scopus 로고
    • Insulin and nonhydrolyzable GTP analogs induce translocation of GLUT 4 to the plasma membrane in alpha-toxin-permeabilized rat adipose cells
    • Baldini, G., Hohman, R., Charron, MJ., Lodish, HF. Insulin and nonhydrolyzable GTP analogs induce translocation of GLUT 4 to the plasma membrane in alpha-toxin-permeabilized rat adipose cells. J Biol Chem 1991; 266: 4037–4040.
    • (1991) J Biol Chem , vol.266 , pp. 4037-4040
    • Baldini, G.1    Hohman, R.2    Charron, M.J.3    Lodish, H.F.4
  • 68
    • 0026773059 scopus 로고
    • Cloning of a Rab3 isotype predominantly expressed in adipocytes
    • Baldini, G., Hohl, T., Lin, HY., Lodish, HF. Cloning of a Rab3 isotype predominantly expressed in adipocytes. Proc Natl Acad Sci USA 1992; 89: 5049–5052.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5049-5052
    • Baldini, G.1    Hohl, T.2    Lin, H.Y.3    Lodish, H.F.4
  • 69
    • 0029018297 scopus 로고
    • Nonneuronal expression of Rab3A: induction during adipogenesis and association with different intracellular membranes than Rab3D
    • Baldini, G., Scherer, PE., Lodish, HF. Nonneuronal expression of Rab3A: induction during adipogenesis and association with different intracellular membranes than Rab3D. Proc Natl Acad Sci USA 1995; 92: 4284–4288.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4284-4288
    • Baldini, G.1    Scherer, P.E.2    Lodish, H.F.3
  • 70
    • 0027741390 scopus 로고
    • Rad: a member of the Ras family overexpressed in muscle of type II diabetic humans
    • Reynet, C., Kahn, CR. Rad: a member of the Ras family overexpressed in muscle of type II diabetic humans. Science 1993; 262: 1441–1444.
    • (1993) Science , vol.262 , pp. 1441-1444
    • Reynet, C.1    Kahn, C.R.2
  • 71
    • 0024287765 scopus 로고
    • Inhibition of yeast adenylate cyclase by antibodies to ras p21
    • Gibbs, JB., Marsico-Ahern, JD., Skolnick, EM. Sigal, IS. Inhibition of yeast adenylate cyclase by antibodies to ras p21. Biochem J 1988; 252: 289–292.
    • (1988) Biochem J , vol.252 , pp. 289-292
    • Gibbs, J.B.1    Marsico-Ahern, J.D.2    Skolnick, E.M.3    Sigal, I.S.4
  • 72
    • 0025965647 scopus 로고
    • Regulation of binding of rhoB p20 to membranes by its specific regulatory protein, GDP dissociation inhibitor
    • Isomura, M., Kikuchi, A., Ohga, N., Takai, Y. Regulation of binding of rhoB p20 to membranes by its specific regulatory protein, GDP dissociation inhibitor. Oncogene 1991; 6; 119–124.
    • (1991) Oncogene , vol.6 , pp. 119-124
    • Isomura, M.1    Kikuchi, A.2    Ohga, N.3    Takai, Y.4
  • 73
    • 0026713293 scopus 로고
    • The small GTP-binding proteins in the cytosol of insulin-secreting cells are complexed to GDP dissociation inhibitor proteins
    • Regazzi, R., Kikuchi, A., Takai, Y., Wollheim, CB. The small GTP-binding proteins in the cytosol of insulin-secreting cells are complexed to GDP dissociation inhibitor proteins. J Biol Chem 1992; 267: 17512–17519.
    • (1992) J Biol Chem , vol.267 , pp. 17512-17519
    • Regazzi, R.1    Kikuchi, A.2    Takai, Y.3    Wollheim, C.B.4
  • 74
    • 0027442667 scopus 로고
    • Biologically active lipids are regulators of Rac.GDI complexation
    • Chuang, TH., Bohl, BP., Bokoch, GM. Biologically active lipids are regulators of Rac.GDI complexation. J Biol Chem 1993; 268: 26206–26211.
    • (1993) J Biol Chem , vol.268 , pp. 26206-26211
    • Chuang, T.H.1    Bohl, B.P.2    Bokoch, G.M.3
  • 75
    • 0025906597 scopus 로고
    • Post-translational modifications of the C-terminal region of the rho protein are important for its interaction with membranes and the stimulatory and inhibitory GDP/GTP exchange proteins
    • Hori, Y., Kikuchi, A., Isomura, M. Katayama, M., Miura, Y., Fujioka, H., Kaibuchi, K. Takai, Y. Post-translational modifications of the C-terminal region of the rho protein are important for its interaction with membranes and the stimulatory and inhibitory GDP/GTP exchange proteins. Oncogene 1991; 6: 515–522.
    • (1991) Oncogene , vol.6 , pp. 515-522
    • Hori, Y.1    Kikuchi, A.2    Isomura, M.3    Katayama, M.4    Miura, Y.5    Fujioka, H.6    Kaibuchi, K.7    Takai, Y.8
  • 76
    • 0027052911 scopus 로고
    • Post-translational processing of rac p21s is important both for their interaction with the GDP/GTP exchange proteins and for their activation of NADPH oxidase
    • Ando, S., Kaibuchi, K., Sasaki, T. Hiraoka, K., Nishiyama, T., Mizuno, T., Asada, M. Nunoi, H., Matsuda, I., Matsuura, Y. Post-translational processing of rac p21s is important both for their interaction with the GDP/GTP exchange proteins and for their activation of NADPH oxidase. J Biol Chem 1992; 267: 25709–25713.
    • (1992) J Biol Chem , vol.267 , pp. 25709-25713
    • Ando, S.1    Kaibuchi, K.2    Sasaki, T.3    Hiraoka, K.4    Nishiyama, T.5    Mizuno, T.6    Asada, M.7    Nunoi, H.8    Matsuda, I.9    Matsuura, Y.10
  • 77
    • 0025731020 scopus 로고
    • Redistribution of ADP-ribosylation factor during stimulation of permeabilized cells with GTP analogues
    • Regazzi, R., Ullrich, S., Kahn, RA., Wollheim, CB. Redistribution of ADP-ribosylation factor during stimulation of permeabilized cells with GTP analogues. Biochem J 1991; 275: 639–644.
    • (1991) Biochem J , vol.275 , pp. 639-644
    • Regazzi, R.1    Ullrich, S.2    Kahn, R.A.3    Wollheim, C.B.4
  • 78
    • 0027153957 scopus 로고
    • Two distinct populations of ARF bound to Golgi membranes
    • Helms, JB., Palmer, DJ., Rothman, JE. Two distinct populations of ARF bound to Golgi membranes. J Cell Biol 1993; 121: 751–760.
    • (1993) J Cell Biol , vol.121 , pp. 751-760
    • Helms, J.B.1    Palmer, D.J.2    Rothman, J.E.3
  • 79
    • 0029807379 scopus 로고    scopus 로고
    • Structure and intracellular localization of mouse ADP-ribosylation factors type 1 to type 6 (ARF1-ARF6)
    • Hosaka, M., Toda, K., Takatsu, H., Torii, S., Murakami, K., Nakayama, K. Structure and intracellular localization of mouse ADP-ribosylation factors type 1 to type 6 (ARF1-ARF6). J Biochem 1996; 120: 813–819.
    • (1996) J Biochem , vol.120 , pp. 813-819
    • Hosaka, M.1    Toda, K.2    Takatsu, H.3    Torii, S.4    Murakami, K.5    Nakayama, K.6
  • 80
    • 0030893929 scopus 로고    scopus 로고
    • Activation and translocation of Rho (and ADP ribosylation factor) by insulin in rat adipocytes. Apparent involvement of phosphatidylinositol 3-kinase
    • Karnam, P., Standaert, ML., Galloway, L., Farese, RV. Activation and translocation of Rho (and ADP ribosylation factor) by insulin in rat adipocytes. Apparent involvement of phosphatidylinositol 3-kinase. J Biol Chem 1997; 272: 6136–6140.
    • (1997) J Biol Chem , vol.272 , pp. 6136-6140
    • Karnam, P.1    Standaert, M.L.2    Galloway, L.3    Farese, R.V.4
  • 81
    • 0031172192 scopus 로고    scopus 로고
    • ARF proteins mediate insulin-dependent activation of phospholipase D
    • Shome, K., Vasudevan, C., Romero, G. ARF proteins mediate insulin-dependent activation of phospholipase D. Curr Biol 1997; 7: 387–96.
    • (1997) Curr Biol , vol.7
    • Shome, K.1    Vasudevan, C.2    Romero, G.3
  • 82
    • 0026561901 scopus 로고
    • Brefeldin A: insights into the control of membrane traffic and organelle structure
    • Klausner, RD. Donaldson, JG., Lippincott-Schwartz, J. Brefeldin A: insights into the control of membrane traffic and organelle structure. J Cell Biol 1992; 116: 1071–1080.
    • (1992) J Cell Biol , vol.116 , pp. 1071-1080
    • Klausner, R.D.1    Donaldson, J.G.2    Lippincott-Schwartz, J.3
  • 83
    • 0026746713 scopus 로고
    • Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF
    • Helms, JB., Rothman, JE. Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF. Nature 1992; 360: 352–354.
    • (1992) Nature , vol.360 , pp. 352-354
    • Helms, J.B.1    Rothman, J.E.2
  • 84
    • 0026677375 scopus 로고
    • Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein
    • Donaldson, JG., Finazzi, D., Klausner, RD. Brefeldin A inhibits Golgi membrane-catalysed exchange of guanine nucleotide onto ARF protein. Nature 1992; 360: 350–352.
    • (1992) Nature , vol.360 , pp. 350-352
    • Donaldson, J.G.1    Finazzi, D.2    Klausner, R.D.3
  • 85
    • 0027193417 scopus 로고
    • Activation of ADP-ribosylation factor by Golgi membranes. Evidence for a brefeldin A- and proteasesensitive activating factor on Golgi membranes
    • Randazzo, PA., Yang, YM. Rulka, C., Kahn, RA. Activation of ADP-ribosylation factor by Golgi membranes. Evidence for a brefeldin A- and proteasesensitive activating factor on Golgi membranes. J Biol Chem 1993; 268: 9555–9563.
    • (1993) J Biol Chem , vol.268 , pp. 9555-9563
    • Randazzo, P.A.1    Yang, Y.M.2    Rulka, C.3    Kahn, R.A.4
  • 86
    • 0028023005 scopus 로고
    • Brefeldin A inhibits insulin-induced glucose transport stimulation and GLUT4 recruitment in rat adipocytes
    • Lachaal, M., Moronski, C., Liu, H., Jung, CY. Brefeldin A inhibits insulin-induced glucose transport stimulation and GLUT4 recruitment in rat adipocytes. J Biol Chem 1994; 269: 23689–23693.
    • (1994) J Biol Chem , vol.269 , pp. 23689-23693
    • Lachaal, M.1    Moronski, C.2    Liu, H.3    Jung, C.Y.4
  • 87
    • 0029609235 scopus 로고
    • The effects of brefeldin A on the glucose transport system in rat adipocytes. Implications regarding the intracellular locus of insulin-sensitive Glut4
    • Bao, S., Smith, RM., Jarett, L., Garvey, WT. The effects of brefeldin A on the glucose transport system in rat adipocytes. Implications regarding the intracellular locus of insulin-sensitive Glut4. J Biol Chem 1995; 270: 30199–30204.
    • (1995) J Biol Chem , vol.270 , pp. 30199-30204
    • Bao, S.1    Smith, R.M.2    Jarett, L.3    Garvey, W.T.4
  • 88
    • 0029886414 scopus 로고    scopus 로고
    • Insulin-induced GLUT4 recycling in rat adipose cells by a pathway insensitive to brefeldin A
    • Kono-Sugita, E., Satoh, S., Suzuki, Y., Egawa, M., Udaka, N., Ito, T., Sekihara, H. Insulin-induced GLUT4 recycling in rat adipose cells by a pathway insensitive to brefeldin A. Eur J Biochem 1996; 236: 1033–1037.
    • (1996) Eur J Biochem , vol.236 , pp. 1033-1037
    • Kono-Sugita, E.1    Satoh, S.2    Suzuki, Y.3    Egawa, M.4    Udaka, N.5    Ito, T.6    Sekihara, H.7
  • 89
    • 0028914182 scopus 로고
    • A regulatory role for ARF6 in receptor-mediated endocytosis
    • D'Souza-Schorey, C., Li, G., Colombo, MI., Stahl, PD. A regulatory role for ARF6 in receptor-mediated endocytosis. Science 1995; 267: 1175–1178.
    • (1995) Science , vol.267 , pp. 1175-1178
    • D'Souza-Schorey, C.1    Li, G.2    Colombo, M.I.3    Stahl, P.D.4
  • 90
    • 0032498526 scopus 로고    scopus 로고
    • ARF6 targets recycling vesicles to the plasma membrane: insights from an ultrastructural investigation
    • D'Souza-Schorey, C., van Donselaar, E., Hsu, VW., Yang, C., Stahl, PD., Peters, PJ. ARF6 targets recycling vesicles to the plasma membrane: insights from an ultrastructural investigation. J Cell Biol 1998; 140: 603–616.
    • (1998) J Cell Biol , vol.140 , pp. 603-616
    • D'Souza-Schorey, C.1    van Donselaar, E.2    Hsu, V.W.3    Yang, C.4    Stahl, P.D.5    Peters, P.J.6
  • 91
    • 0026632366 scopus 로고
    • Evidence for ADP-ribosylation factor (ARF) as a regulator of in vitro endosome-endosome fusion
    • Lenhard, JM., Kahn, RA., Stahl, PD. Evidence for ADP-ribosylation factor (ARF) as a regulator of in vitro endosome-endosome fusion. J Biol Chem 1992; 267: 13047–13052.
    • (1992) J Biol Chem , vol.267 , pp. 13047-13052
    • Lenhard, J.M.1    Kahn, R.A.2    Stahl, P.D.3
  • 92
    • 0028136853 scopus 로고
    • Heterotrimeric GTP-binding proteins (G proteins) and ADP-ribosylation factor (ARF) regulate priming of endosomal membranes for fusion
    • Lenhard, JM., Colombo, MI., Stahl, PD. Heterotrimeric GTP-binding proteins (G proteins) and ADP-ribosylation factor (ARF) regulate priming of endosomal membranes for fusion. Arch Biochem Biophys 1994; 312: 474–479.
    • (1994) Arch Biochem Biophys , vol.312 , pp. 474-479
    • Lenhard, J.M.1    Colombo, M.I.2    Stahl, P.D.3
  • 93
    • 0026001029 scopus 로고
    • ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein
    • Serafini, T., Orci, L., Amherdt, M., Brunner, M., Kahn, RA., Rothman, JE. ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. Cell 1991; 67: 239–253.
    • (1991) Cell , vol.67 , pp. 239-253
    • Serafini, T.1    Orci, L.2    Amherdt, M.3    Brunner, M.4    Kahn, R.A.5    Rothman, J.E.6
  • 94
  • 95
    • 0031802483 scopus 로고    scopus 로고
    • The distribution and translocation of the G protein ADP-ribosylation Factor 1 in live cells is determined by its GTPase activity
    • Vasudevan, C., Han, W., Tan, Y., Nie, Y., Li, D., Shome, K., Watkins, SC., Levitan, ES., Romero, G. The distribution and translocation of the G protein ADP-ribosylation Factor 1 in live cells is determined by its GTPase activity. J Cell Sci 1998; 111: 1277–1285.
    • (1998) J Cell Sci , vol.111 , pp. 1277-1285
    • Vasudevan, C.1    Han, W.2    Tan, Y.3    Nie, Y.4    Li, D.5    Shome, K.6    Watkins, S.C.7    Levitan, E.S.8    Romero, G.9
  • 96
    • 0024977517 scopus 로고
    • Identification of rho as a substrate for botulinum toxin C3-catalyzed ADP-ribosylation
    • Quilliam, LA., Lacal, JC., Bokoch, GM. Identification of rho as a substrate for botulinum toxin C3-catalyzed ADP-ribosylation. FEBS Lett 1989; 247: 221–226.
    • (1989) FEBS Lett , vol.247 , pp. 221-226
    • Quilliam, L.A.1    Lacal, J.C.2    Bokoch, G.M.3
  • 97
    • 0024449589 scopus 로고
    • The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells
    • Chardin, P., Boquet, P., Madaule, P., Popoff, MR., Rubin, EJ., Gill, DM. The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells. EMBO J 1989; 8: 1087–1092.
    • (1989) EMBO J , vol.8 , pp. 1087-1092
    • Chardin, P.1    Boquet, P.2    Madaule, P.3    Popoff, M.R.4    Rubin, E.J.5    Gill, D.M.6
  • 98
    • 0025195876 scopus 로고
    • Microinjection of recombinant p21rho induces rapid changes in cell morphology
    • Paterson, HF., Self, AJ., Garrett, MD. Just, I., Aktories, K. Hall, A. Microinjection of recombinant p21rho induces rapid changes in cell morphology. J Cell Biol 1990; 111: 1001–1007.
    • (1990) J Cell Biol , vol.111 , pp. 1001-1007
    • Paterson, H.F.1    Self, A.J.2    Garrett, M.D.3    Just, I.4    Aktories, K.5    Hall, A.6
  • 99
    • 0028021308 scopus 로고
    • Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho
    • Jalink, K., van Corven, EJ., Hengeveld, T., Morii, N., Narumiva, S., Moolenaar, WH. Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho. J Cell Biol 1994; 126: 801–810.
    • (1994) J Cell Biol , vol.126 , pp. 801-810
    • Jalink, K.1    van Corven, E.J.2    Hengeveld, T.3    Morii, N.4    Narumiva, S.5    Moolenaar, W.H.6
  • 100
    • 0032571395 scopus 로고    scopus 로고
    • The low molecular weight GTPase Rho regulates myofibril formation and organization in neonatal rat ventricular myocytes. Involvement of Rho kinase
    • Hoshijima, M., Sah, VP., Wang, Y., Chien, KR., Brown, JH. The low molecular weight GTPase Rho regulates myofibril formation and organization in neonatal rat ventricular myocytes. Involvement of Rho kinase. J Biol Chem 1998; 273: 7725–7730.
    • (1998) J Biol Chem , vol.273 , pp. 7725-7730
    • Hoshijima, M.1    Sah, V.P.2    Wang, Y.3    Chien, K.R.4    Brown, J.H.5
  • 102
    • 0030582707 scopus 로고    scopus 로고
    • Clostridium botulinum C3 exoenzyme stimulates GLUT4-mediated glucose transport, but not glycogen synthesis, in 3T3-L1 adipocytes- a potential role of rho?
    • van den Berghe, N., Barros, LF. van Mackelenbergh, MG., Krans, HM. Clostridium botulinum C3 exoenzyme stimulates GLUT4-mediated glucose transport, but not glycogen synthesis, in 3T3-L1 adipocytes- a potential role of rho? Biochem Biophys Res Comm 1996; 229: 430–439.
    • (1996) Biochem Biophys Res Comm , vol.229 , pp. 430-439
    • van den Berghe, N.1    Barros, L.F.2    van Mackelenbergh, M.G.3    Krans, H.M.4
  • 103
    • 0032571004 scopus 로고    scopus 로고
    • Comparative effects of GTPYS and insulin on the activation of Rho, phosphatidylinositol 3-kinase, and protein kinase N in rat adipocytes-Relationship to glucose transport
    • Standaert, M., Bandyopadhyay, G., Galloway, L., Ono, Y., Mukai, H., Farese, R. Comparative effects of GTPYS and insulin on the activation of Rho, phosphatidylinositol 3-kinase, and protein kinase N in rat adipocytes-Relationship to glucose transport. J Biol Chem 1998; 273: 7470–7477.
    • (1998) J Biol Chem , vol.273 , pp. 7470-7477
    • Standaert, M.1    Bandyopadhyay, G.2    Galloway, L.3    Ono, Y.4    Mukai, H.5    Farese, R.6
  • 104
    • 0030707535 scopus 로고    scopus 로고
    • Changes in the signalling status of the small GTP-binding proteins Rac and Rho do not influence insulin-stimulated hexose transport
    • Dorrestijn, J., Bos, JL., Van der Zon, GC., Maassen, JA. Changes in the signalling status of the small GTP-binding proteins Rac and Rho do not influence insulin-stimulated hexose transport. Exp Clin Endocrinol Diabetes 1997; 105: 254–262.
    • (1997) Exp Clin Endocrinol Diabetes , vol.105 , pp. 254-262
    • Dorrestijn, J.1    Bos, J.L.2    Van der Zon, G.C.3    Maassen, J.A.4
  • 105
    • 0031036483 scopus 로고    scopus 로고
    • Rab 3D in rat adipose cells and its overexpression in genetic obesity (Zucker fatty rat)
    • Guerre-Millo, M., Baldini, G., Lodish, HF., Lavau, M., Cushman, SW. Rab 3D in rat adipose cells and its overexpression in genetic obesity (Zucker fatty rat). Biochem J 1997; 321: 89–93.
    • (1997) Biochem J , vol.321 , pp. 89-93
    • Guerre-Millo, M.1    Baldini, G.2    Lodish, H.F.3    Lavau, M.4    Cushman, S.W.5
  • 106
    • 0028358976 scopus 로고
    • Insulin-induced translocation of the glucose transporter GLUT4 in cardiac muscle: studies on the role of small-molecular-mass GTP-binding proteins
    • Uphues, I., Kolter, T., Goud, B. Eckel, J. Insulin-induced translocation of the glucose transporter GLUT4 in cardiac muscle: studies on the role of small-molecular-mass GTP-binding proteins. Biochem J 1994; 301: 177–182
    • (1994) Biochem J , vol.301 , pp. 177-182
    • Uphues, I.1    Kolter, T.2    Goud, B.3    Eckel, J.4
  • 109
    • 0031007132 scopus 로고    scopus 로고
    • Association of cytosolic Rab4 with GDI isoforms in insulin-sensitive 3T3-L1 adipocytes
    • Shisheva, A., Czech, MP. Association of cytosolic Rab4 with GDI isoforms in insulin-sensitive 3T3-L1 adipocytes. Biochemistry 1997; 36: 6564–6570.
    • (1997) Biochemistry , vol.36 , pp. 6564-6570
    • Shisheva, A.1    Czech, M.P.2
  • 110
    • 0030908290 scopus 로고    scopus 로고
    • Insulin stimulates guanine nucleotide exchange on Rab4 via a wortmannin-sensitive signaling pathway in rat adipocytes
    • Shibata, H., Omata, W., Kojima, I. Insulin stimulates guanine nucleotide exchange on Rab4 via a wortmannin-sensitive signaling pathway in rat adipocytes. J Biol Chem 1997; 272; 14542–14546.
    • (1997) J Biol Chem , vol.272 , pp. 14542-14546
    • Shibata, H.1    Omata, W.2    Kojima, I.3
  • 111
    • 0030780582 scopus 로고    scopus 로고
    • The small guanosine triphosphate-binding protein Rab4 is involved in insulin-induced GLUT4 translocation and actin filament rearrangement in 3T3-L1 cells
    • Vollenweider, P., Martin, SS., Haruta, T., Morris, AJ., Nelson, JG., Cormont, M., Le Marchand-Brustel, Y., Rose, DW., Olefsky, JM. The small guanosine triphosphate-binding protein Rab4 is involved in insulin-induced GLUT4 translocation and actin filament rearrangement in 3T3-L1 cells. Endocrinology 1997; 138: 4941–4949.
    • (1997) Endocrinology , vol.138 , pp. 4941-4949
    • Vollenweider, P.1    Martin, S.S.2    Haruta, T.3    Morris, A.J.4    Nelson, J.G.5    Cormont, M.6    Le Marchand-Brustel, Y.7    Rose, D.W.8    Olefsky, J.M.9
  • 112
    • 0025784181 scopus 로고
    • Rab3 A attachment to the synaptic vesicle membrane mediated by a conserved polyisoprenylated carboxy-terminal sequence
    • Johnston, PA., Archer, BT. 3rd, Robinson, K., Mignery, GA., Jahn, R., Sudhof, TC. Rab3 A attachment to the synaptic vesicle membrane mediated by a conserved polyisoprenylated carboxy-terminal sequence. Neuron 1991; 7: 101–109.
    • (1991) Neuron , vol.7 , pp. 101-109
    • Johnston, P.A.1    Archer, B.T.2    Robinson, K.3    Mignery, G.A.4    Jahn, R.5    Sudhof, T.C.6
  • 113
    • 0025830577 scopus 로고
    • C terminus of the small GTP-binding protein smg p25A contains two geranylgeranylated cysteine residues and a methyl ester
    • Farnsworth, CC., Kawata, M., Yoshida, I., Takai, Y., Gelb, MH., Glomset, JA. C terminus of the small GTP-binding protein smg p25A contains two geranylgeranylated cysteine residues and a methyl ester. Proc Natl Acad Sci USA 1991; 88: 6196–6200.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 6196-6200
    • Farnsworth, C.C.1    Kawata, M.2    Yoshida, I.3    Takai, Y.4    Gelb, M.H.5    Glomset, J.A.6
  • 114
    • 0027180460 scopus 로고
    • Post-translational processing and membrane association of the two early endosome-associated rab GTP-binding proteins (rab4 and rab5)
    • Li, G., Stahl, PD. Post-translational processing and membrane association of the two early endosome-associated rab GTP-binding proteins (rab4 and rab5). Arch Biochem Biophys 1993; 304; 471–478.
    • (1993) Arch Biochem Biophys , vol.304 , pp. 471-478
    • Li, G.1    Stahl, P.D.2
  • 115
    • 0029984532 scopus 로고    scopus 로고
    • A synthetic peptide corresponding to the Rab4 hypervariable carboxyl-terminal domain inhibits insulin action on glucose transport in rat adipocytes
    • Shibata, H., Omata, W., Suzuki, Y., Tanaka, S., Kojima, I. A synthetic peptide corresponding to the Rab4 hypervariable carboxyl-terminal domain inhibits insulin action on glucose transport in rat adipocytes. J Biol Chem 1996; 271: 9704–9709.
    • (1996) J Biol Chem , vol.271 , pp. 9704-9709
    • Shibata, H.1    Omata, W.2    Suzuki, Y.3    Tanaka, S.4    Kojima, I.5
  • 116
    • 0030980279 scopus 로고    scopus 로고
    • The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion
    • Geppert, M., Goda, Y., Stevens, CF., Sudhof, TC. The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion. Nature 1997; 387: 810–814.
    • (1997) Nature , vol.387 , pp. 810-814
    • Geppert, M.1    Goda, Y.2    Stevens, C.F.3    Sudhof, T.C.4
  • 117
    • 0028168008 scopus 로고
    • A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles
    • Sogaard, M., Tani, K., Ye, RR., Geromanos, S., Tempst, P., Kirchhausen, T., Rothman, JE., Söllner, T. A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles. Cell 1994; 78: 937–948.
    • (1994) Cell , vol.78 , pp. 937-948
    • Sogaard, M.1    Tani, K.2    Ye, R.R.3    Geromanos, S.4    Tempst, P.5    Kirchhausen, T.6    Rothman, J.E.7    Söllner, T.8
  • 118
    • 0028791634 scopus 로고
    • Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion
    • Stenmark, H., Vitale, G., Ullrich, O., Zerial, M. Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion. Cell 1995; 83: 423–432.
    • (1995) Cell , vol.83 , pp. 423-432
    • Stenmark, H.1    Vitale, G.2    Ullrich, O.3    Zerial, M.4
  • 119
  • 120
    • 0031898897 scopus 로고    scopus 로고
    • Rab3 and synaptotagmin: The yin and yang of synaptic membrane fusion
    • Geppert, M., Sudhof, TC. Rab3 and synaptotagmin: The yin and yang of synaptic membrane fusion. Ann Rev Neurosci 1998; 21: 75–95.
    • (1998) Ann Rev Neurosci , vol.21 , pp. 75-95
    • Geppert, M.1    Sudhof, T.C.2
  • 121
    • 0029126327 scopus 로고
    • Rab GDP dissociation inhibitor: putting rab GTPases in the right place
    • Pfeffer, SR., Dirac-Svejstrup, AB., Soldati, T. Rab GDP dissociation inhibitor: putting rab GTPases in the right place. J Biol Chem 1995; 270: 17057–17059.
    • (1995) J Biol Chem , vol.270 , pp. 17057-17059
    • Pfeffer, S.R.1    Dirac-Svejstrup, A.B.2    Soldati, T.3
  • 122
    • 0029051343 scopus 로고
    • A GDP/GTP exchange-stimulatory activity for the Rab5-RabGDI complex on clathrin-coated vesicles from bovine brain
    • Horiuchi, H., Giner, A., Hoflack, B., Zerial, M. A GDP/GTP exchange-stimulatory activity for the Rab5-RabGDI complex on clathrin-coated vesicles from bovine brain. J Biol Chem 1995; 270: 11257–11262.
    • (1995) J Biol Chem , vol.270 , pp. 11257-11262
    • Horiuchi, H.1    Giner, A.2    Hoflack, B.3    Zerial, M.4
  • 123
    • 0027979639 scopus 로고
    • Rab4 is phosphorylated by the insulin-activated extracellular-signal-regulated kinase ERK1
    • Cormont, M., Tanti, JF., Zahraoui, A., Van Obberghen, E., Le Marchand-Brustel, Y. Rab4 is phosphorylated by the insulin-activated extracellular-signal-regulated kinase ERK1. Eur J Biochem 1994; 219: 1081–1085.
    • (1994) Eur J Biochem , vol.219 , pp. 1081-1085
    • Cormont, M.1    Tanti, J.F.2    Zahraoui, A.3    Van Obberghen, E.4    Le Marchand-Brustel, Y.5
  • 125
    • 0029973135 scopus 로고    scopus 로고
    • Activated phosphatidylinositol 3-kinase is sufficient to mediate actin rearrangement and GLUT4 translocation in 3T3-L1 adipocytes
    • Martin, SS., Haruta, T., Morris, AJ., Klippel, A., Williams, LT., Olefsky, JM. Activated phosphatidylinositol 3-kinase is sufficient to mediate actin rearrangement and GLUT4 translocation in 3T3-L1 adipocytes. J Biol Chem 1996; 271: 17605–17608.
    • (1996) J Biol Chem , vol.271 , pp. 17605-17608
    • Martin, S.S.1    Haruta, T.2    Morris, A.J.3    Klippel, A.4    Williams, L.T.5    Olefsky, J.M.6
  • 126
    • 0030054398 scopus 로고    scopus 로고
    • Overexpression of catalytic subunit p110alpha of phosphatidylinositol 3-kinase increases glucose transport activity with translocation of glucose transporters in 3T3-L1 adipocytes
    • Katagiri, H., Asano, T., Ishihara, H., Inukai, K., Shibasaki, Y., Kikuchi, M., Yazaki, Y., Oka, Y. Overexpression of catalytic subunit p110alpha of phosphatidylinositol 3-kinase increases glucose transport activity with translocation of glucose transporters in 3T3-L1 adipocytes. J Biol Chem 1996; 271: 16987–16990.
    • (1996) J Biol Chem , vol.271 , pp. 16987-16990
    • Katagiri, H.1    Asano, T.2    Ishihara, H.3    Inukai, K.4    Shibasaki, Y.5    Kikuchi, M.6    Yazaki, Y.7    Oka, Y.8
  • 127
    • 0031022582 scopus 로고    scopus 로고
    • Differential effects of constitutively active phosphatidylinositol 3-kinase on glucose transport, glycogen synthase activity, and DNA synthesis in 3T3-L1 adipocytes
    • Frevert, EU., Kahn, BB. Differential effects of constitutively active phosphatidylinositol 3-kinase on glucose transport, glycogen synthase activity, and DNA synthesis in 3T3-L1 adipocytes. Mol Cell Biol 1997; 17: 190–198.
    • (1997) Mol Cell Biol , vol.17 , pp. 190-198
    • Frevert, E.U.1    Kahn, B.B.2
  • 129
    • 0027142022 scopus 로고
    • ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity
    • Brown, HA., Gutowski, S., Moomaw, CR., Slaughter, C., Stemweis, PC. ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell 1993; 75: 1137–1144.
    • (1993) Cell , vol.75 , pp. 1137-1144
    • Brown, H.A.1    Gutowski, S.2    Moomaw, C.R.3    Slaughter, C.4    Stemweis, P.C.5
  • 130
    • 0027999909 scopus 로고
    • Activation of rat liver phospholipase D by the small GTP-binding protein RhoA
    • Malcolm, KC., Ross, AH., Qiu, RG., Symons, M., Exton, JH. Activation of rat liver phospholipase D by the small GTP-binding protein RhoA. J Biol Chem 1994; 269: 25951–25954.
    • (1994) J Biol Chem , vol.269 , pp. 25951-25954
    • Malcolm, K.C.1    Ross, A.H.2    Qiu, R.G.3    Symons, M.4    Exton, J.H.5
  • 131
    • 0029020350 scopus 로고
    • Resolved phospholipase D activity is modulated by cytosolic factors other than Arf
    • Singer, WD., Brown, HA. Bokoch, GM. Sternweis, PC. Resolved phospholipase D activity is modulated by cytosolic factors other than Arf. J Biol Chem 1995; 270: 14944–14950.
    • (1995) J Biol Chem , vol.270 , pp. 14944-14950
    • Singer, W.D.1    Brown, H.A.2    Bokoch, G.M.3    Sternweis, P.C.4
  • 132
    • 0029564902 scopus 로고
    • Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family
    • Hammond, SM., Altshuller, YM., Sung, TC., Rudge, SA., Kristine Rose, K., Engebrecht, J., Morris, AJ., Frohman, MA. Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. J Biol Chem 1995; 270: 29640–29643.
    • (1995) J Biol Chem , vol.270 , pp. 29640-29643
    • Hammond, S.M.1    Altshuller, Y.M.2    Sung, T.C.3    Rudge, S.A.4    Kristine Rose, K.5    Engebrecht, J.6    Morris, A.J.7    Frohman, M.A.8
  • 134
    • 16844366239 scopus 로고    scopus 로고
    • Evidence for Rho-mediated agonist stimulation of phospholipase D in Rat1 fibroblasts. Effects of Clostridium botulinum C3 transferase
    • Malcolm, KC., Elliott, CM., Exton, JH. Evidence for Rho-mediated agonist stimulation of phospholipase D in Rat1 fibroblasts. Effects of Clostridium botulinum C3 transferase. J Biol; Chem 1996; 271: 13135–13139.
    • (1996) J Biol; Chem , vol.271 , pp. 13135-13139
    • Malcolm, K.C.1    Elliott, C.M.2    Exton, J.H.3
  • 135
    • 0031019308 scopus 로고    scopus 로고
    • Role of Rho family proteins in phospholipase D activation by growth factors
    • Hess, JH., Ross, AH., Qiu, RG., Symons, M., Exton, JH. Role of Rho family proteins in phospholipase D activation by growth factors. J Biol Chem 1997; 272: 1615–1620.
    • (1997) J Biol Chem , vol.272 , pp. 1615-1620
    • Hess, J.H.1    Ross, A.H.2    Qiu, R.G.3    Symons, M.4    Exton, J.H.5
  • 136
    • 0028233378 scopus 로고
    • Identification, partial purification, and characterization of a novel phospholipid-dependent and fatty acid-activated protein kinase from human platelets
    • Khan, WA., Blobe, GC., Richards, AL., Hannun, YA. Identification, partial purification, and characterization of a novel phospholipid-dependent and fatty acid-activated protein kinase from human platelets. J Biol Chem 1994; 269: 9729–9735.
    • (1994) J Biol Chem , vol.269 , pp. 9729-9735
    • Khan, W.A.1    Blobe, G.C.2    Richards, A.L.3    Hannun, Y.A.4
  • 137
    • 0028567280 scopus 로고
    • Phosphatidic acid activation of protein kinase C-Ç overexpressed in COS cells: comparison with other protein kinase C isotypes and other acidic lipids
    • Limatola, C., Schaap, D., Moolenaar, WH., van Blitterswijk, WJ. Phosphatidic acid activation of protein kinase C-Ç overexpressed in COS cells: comparison with other protein kinase C isotypes and other acidic lipids. Biochem J 1994; 304: 1001–1008.
    • (1994) Biochem J , vol.304 , pp. 1001-1008
    • Limatola, C.1    Schaap, D.2    Moolenaar, W.H.3    van Blitterswijk, W.J.4
  • 138
    • 0030950647 scopus 로고    scopus 로고
    • Phosphatidic acid-mediated phosphorylation of the NADPH oxidase component p47-phox. Evidence that phosphatidic acid may activate a novel protein kinase
    • Waite, KA., Wallin, R., Qualliotine-Mann, D., McPhail, LC. Phosphatidic acid-mediated phosphorylation of the NADPH oxidase component p47-phox. Evidence that phosphatidic acid may activate a novel protein kinase. J Biol Chem 1997; 272: 15569–15578.
    • (1997) J Biol Chem , vol.272 , pp. 15569-15578
    • Waite, K.A.1    Wallin, R.2    Qualliotine-Mann, D.3    McPhail, L.C.4
  • 139
    • 0029032202 scopus 로고
    • Lysophosphatidic acid: a multifunctional phospholipid messenger
    • Moolenar, WH. Lysophosphatidic acid: a multifunctional phospholipid messenger. J Biol Chem 1995; 270: 12949–12952.
    • (1995) J Biol Chem , vol.270 , pp. 12949-12952
    • Moolenar, W.H.1
  • 141
    • 0021227676 scopus 로고
    • The role of protein kinase C in cell surface signal transduction and tumour promotion
    • Nishizuka, Y. The role of protein kinase C in cell surface signal transduction and tumour promotion. Nature 1984; 308: 693–698.
    • (1984) Nature , vol.308 , pp. 693-698
    • Nishizuka, Y.1
  • 142
    • 0030987070 scopus 로고    scopus 로고
    • Regulation of protein kinase C
    • Newton, AC. Regulation of protein kinase C. Curr Opin Cell Biol 1997; 9: 161–167.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 161-167
    • Newton, A.C.1
  • 143
    • 0029935339 scopus 로고    scopus 로고
    • Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoyl-phorbol-13-acetate-stimulated Madin-Darbv canine kidney cells
    • Ghosh, S., Strum, JC., Sciorra, VA., Daniel, L., Bell, RM. Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoyl-phorbol-13-acetate-stimulated Madin-Darbv canine kidney cells. J Biol Chem 1996; 271: 8472–8480.
    • (1996) J Biol Chem , vol.271 , pp. 8472-8480
    • Ghosh, S.1    Strum, J.C.2    Sciorra, V.A.3    Daniel, L.4    Bell, R.M.5
  • 144
    • 13044297218 scopus 로고    scopus 로고
    • Insulin-induced Raf-1 translocation to intracellular compartments
    • Rizzo, MA., Vasudevan, C., Watkins, S., Romero, G. Insulin-induced Raf-1 translocation to intracellular compartments. Mol Biol Cell 1997; 8: 129a.
    • (1997) Mol Biol Cell , vol.8
    • Rizzo, M.A.1    Vasudevan, C.2    Watkins, S.3    Romero, G.4
  • 145
    • 0032499031 scopus 로고    scopus 로고
    • Insulin-dependent translocation of arno to the plasma membrane of adipocytes requires phosphatidyl-inositol 3-kinase
    • Venkateswarlu, K., Oatey, PB., Tavare, JM., Cullen, PJ. Insulin-dependent translocation of arno to the plasma membrane of adipocytes requires phosphatidyl-inositol 3-kinase. Curr Biol 1998; 8: 463–466.
    • (1998) Curr Biol , vol.8 , pp. 463-466
    • Venkateswarlu, K.1    Oatey, P.B.2    Tavare, J.M.3    Cullen, P.J.4
  • 147
    • 0032488847 scopus 로고    scopus 로고
    • Structure of the guanine nucleotide exchange factor Sec7 domain of human arno and analysis of the interaction with ARF GTPase
    • Mossessova, E., Gulbis, JM., Goldberg, J. Structure of the guanine nucleotide exchange factor Sec7 domain of human arno and analysis of the interaction with ARF GTPase. Cell 1998; 92: 415–423.
    • (1998) Cell , vol.92 , pp. 415-423
    • Mossessova, E.1    Gulbis, J.M.2    Goldberg, J.3
  • 148
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., D'Souza-Schorey, C. Rho GTPases and signaling networks. Gene Develop 1997; 11: 2295–2322.
    • (1997) Gene Develop , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 149
    • 0030293886 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase signals activate a selective subset of Rac/Rho-dependent effector pathways
    • Reif, K., Nobes, CD., Thomas, G., Hall, A., Cantrell, DA. Phosphatidylinositol 3-kinase signals activate a selective subset of Rac/Rho-dependent effector pathways. Curr Biol 1996; 6: 1445–1455.
    • (1996) Curr Biol , vol.6 , pp. 1445-1455
    • Reif, K.1    Nobes, C.D.2    Thomas, G.3    Hall, A.4    Cantrell, D.A.5
  • 150
    • 0028928447 scopus 로고
    • Insulin-dependent tyrosine phosphorylation of the vav protooncogene product in cells of hematopoietic origin
    • Uddin, S., Katzav, S., White, MF., Platanias, LC. Insulin-dependent tyrosine phosphorylation of the vav protooncogene product in cells of hematopoietic origin. J Biol Chem 1995; 270: 7712–7716.
    • (1995) J Biol Chem , vol.270 , pp. 7712-7716
    • Uddin, S.1    Katzav, S.2    White, M.F.3    Platanias, L.C.4
  • 151
    • 0028137073 scopus 로고
    • Gem: an induced, immediate early protein belonging to the Ras family
    • Maguire, J., Santoro, T., Jensen, P., Siebenlist, U., Yewdell, J., Kelly, K. Gem: an induced, immediate early protein belonging to the Ras family. Science 1994; 265: 241–244.
    • (1994) Science , vol.265 , pp. 241-244
    • Maguire, J.1    Santoro, T.2    Jensen, P.3    Siebenlist, U.4    Yewdell, J.5    Kelly, K.6
  • 152
    • 0029619704 scopus 로고
    • Kir, a novel Ras-family G-protein, induces invasive pseudohyphal growth in Saccharomyces cerevisiae
    • Dorm, D., Cohen, L., Del Villar, K., Poullet, P., Mohr, R., Whiteway, M., Witte, O., Tamanoim, F. Kir, a novel Ras-family G-protein, induces invasive pseudohyphal growth in Saccharomyces cerevisiae. Oncogene 1995; 11: 2267–2271.
    • (1995) Oncogene , vol.11 , pp. 2267-2271
    • Dorm, D.1    Cohen, L.2    Del Villar, K.3    Poullet, P.4    Mohr, R.5    Whiteway, M.6    Witte, O.7    Tamanoim, F.8
  • 153
    • 0030803793 scopus 로고    scopus 로고
    • Rem is a new member of the Rad- and Gem/Kir Ras-related GTP-binding protein family repressed by lipopolysaccharide stimulation
    • Finlin, BS., Andres, DA. Rem is a new member of the Rad- and Gem/Kir Ras-related GTP-binding protein family repressed by lipopolysaccharide stimulation. J Biol Chem 1997; 272: 21982–21988.
    • (1997) J Biol Chem , vol.272 , pp. 21982-21988
    • Finlin, B.S.1    Andres, D.A.2
  • 154
    • 0030595132 scopus 로고    scopus 로고
    • Overexpression of Rad inhibits glucose uptake in cultured muscle and fat cells
    • Moyers, JS., Bilan, PJ., Reynet, C., Kahn, CR. Overexpression of Rad inhibits glucose uptake in cultured muscle and fat cells. J Biol Chem 1996; 271: 23111–23116.
    • (1996) J Biol Chem , vol.271 , pp. 23111-23116
    • Moyers, J.S.1    Bilan, P.J.2    Reynet, C.3    Kahn, C.R.4
  • 156
    • 0030910312 scopus 로고    scopus 로고
    • Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II
    • Moyers, JS., Bilan, PJ., Zhu, J., Kahn, CR. Rad and Rad-related GTPases interact with calmodulin and calmodulin-dependent protein kinase II. J Biol Chem 1997; 272: 11832–11839.
    • (1997) J Biol Chem , vol.272 , pp. 11832-11839
    • Moyers, J.S.1    Bilan, P.J.2    Zhu, J.3    Kahn, C.R.4
  • 157
    • 0029670787 scopus 로고    scopus 로고
    • Rad, a novel Ras-related GTPase, interacts with skeletal muscle beta-tropomyosin
    • Zhu, J., Bilan, PJ., Moyers, JS., Antonetti, DA., Kahn, CR. Rad, a novel Ras-related GTPase, interacts with skeletal muscle beta-tropomyosin. J Biol Chem 1996; 271: 768–773.
    • (1996) J Biol Chem , vol.271 , pp. 768-773
    • Zhu, J.1    Bilan, P.J.2    Moyers, J.S.3    Antonetti, D.A.4    Kahn, C.R.5
  • 158
    • 0031040840 scopus 로고    scopus 로고
    • Muscle Rad expression and human metabolism: potential role of the novel Ras-related GTPase in energy expenditure and body composition
    • Garvey, WT., Maianu, L., Kennedy, A., Wallace, P., Ganaway, E., Hamacher, LL., Yarnall, DP., Lenhard, JM., Burns, DK. Muscle Rad expression and human metabolism: potential role of the novel Ras-related GTPase in energy expenditure and body composition. Diabetes 1997; 46: 444–450.
    • (1997) Diabetes , vol.46 , pp. 444-450
    • Garvey, W.T.1    Maianu, L.2    Kennedy, A.3    Wallace, P.4    Ganaway, E.5    Hamacher, L.L.6    Yarnall, D.P.7    Lenhard, J.M.8    Burns, D.K.9
  • 159
    • 0030667190 scopus 로고    scopus 로고
    • Insulin and epidermal growth factor stimulate a conformational change in Rap1 and dissociation of the CrkII-C3G complex
    • Okada, S., Pessin, JE. Insulin and epidermal growth factor stimulate a conformational change in Rap1 and dissociation of the CrkII-C3G complex. J Biol Chem 1997; 272: 28179–28182.
    • (1997) J Biol Chem , vol.272 , pp. 28179-28182
    • Okada, S.1    Pessin, J.E.2


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