메뉴 건너뛰기




Volumn 71, Issue 15, 2014, Pages 2775-2785

The IQGAP-related protein DGAP1 mediates signaling to the actin cytoskeleton as an effector and a sequestrator of Rac1 GTPases

Author keywords

Cell migration; Cell polarization; Dictyostelium; Rac; Rho GTPases; Scaffold proteins

Indexed keywords

PROTEIN DGAP1; RAC1 PROTEIN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84904278338     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-014-1606-3     Document Type: Review
Times cited : (8)

References (94)
  • 1
    • 0025254559 scopus 로고
    • Transduction of receptor signal into modulation of effector activity by G proteins: The first 20 years or so
    • Birnbaumer L (1990) Transduction of receptor signal into modulation of effector activity by G proteins: the first 20 years or so. FASEB J 4:3178-3188
    • (1990) FASEB J , vol.4 , pp. 3178-3188
    • Birnbaumer, L.1
  • 2
    • 0015071225 scopus 로고
    • Isolation of a calcium-sequestering protein from sarcoplasmic reticulum
    • MacLennan DH, Wong PT (1971) Isolation of a calcium-sequestering protein from sarcoplasmic reticulum. Proc Natl Acad Sci USA 68:1231-1235
    • (1971) Proc Natl Acad Sci USA , vol.68 , pp. 1231-1235
    • MacLennan, D.H.1    Wong, P.T.2
  • 3
    • 0032971134 scopus 로고    scopus 로고
    • Actin binding proteins that change extent and rate of actin monomer-polymer distribution by different mechanisms
    • Weber A (1999) Actin binding proteins that change extent and rate of actin monomer-polymer distribution by different mechanisms. Mol Cell Biochem 190:67-74
    • (1999) Mol Cell Biochem , vol.190 , pp. 67-74
    • Weber, A.1
  • 4
    • 56949098506 scopus 로고    scopus 로고
    • Molecular titration and ultrasensitivity in regulatory networks
    • Buchler NE, Louis M (2008) Molecular titration and ultrasensitivity in regulatory networks. J Mol Biol 384:1106-1119
    • (2008) J Mol Biol , vol.384 , pp. 1106-1119
    • Buchler, N.E.1    Louis, M.2
  • 5
    • 0026708551 scopus 로고
    • Interaction of thymosin beta 4 with muscle and platelet actin: Implications for actin sequestration in resting platelets
    • Weber A, Nachmias VT, Pennise CR, Pring M, Safer D (1992) Interaction of thymosin beta 4 with muscle and platelet actin: implications for actin sequestration in resting platelets. Biochemistry 31:6179-6185
    • (1992) Biochemistry , vol.31 , pp. 6179-6185
    • Weber, A.1    Nachmias, V.T.2    Pennise, C.R.3    Pring, M.4    Safer, D.5
  • 6
    • 0026725418 scopus 로고
    • Effects of profilin and profilactin on actin structure and function in living cells
    • Cao LG, Babcock GG, Rubenstein PA, Wang YL (1992) Effects of profilin and profilactin on actin structure and function in living cells. J Cell Biol 117:1023-1029
    • (1992) J Cell Biol , vol.117 , pp. 1023-1029
    • Cao, L.G.1    Babcock, G.G.2    Rubenstein, P.A.3    Wang, Y.L.4
  • 9
    • 34247175312 scopus 로고    scopus 로고
    • GTP-binding proteins of the Rho/Rac family: Regulation, effectors and functions in vivo
    • DOI 10.1002/bies.20558
    • Bustelo XR, Sauzeau V, Berenjeno IM (2007) GTP-binding proteins of the Rho/Rac family: regulation, effectors and functions in vivo. Bioessays 29:356-370 (Pubitemid 46597867)
    • (2007) BioEssays , vol.29 , Issue.4 , pp. 356-370
    • Bustelo, X.R.1    Sauzeau, V.2    Berenjeno, I.M.3
  • 10
    • 16644370412 scopus 로고    scopus 로고
    • Human RAS superfamily proteins and related GTPases
    • Colicelli J (2004) Human RAS superfamily proteins and related GTPases. Sci STKE 2004:RE13
    • (2004) Sci STKE , vol.2004
    • Colicelli, J.1
  • 11
    • 78649474147 scopus 로고    scopus 로고
    • Ras history: The saga continues
    • Cox AD, Der CJ (2010) Ras history: the saga continues. Small GTPases 1:2-27
    • (2010) Small GTPases , vol.1 , pp. 2-27
    • Cox, A.D.1    Der, C.J.2
  • 12
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: New insights into their functions from in vivo studies
    • Heasman SJ, Ridley AJ (2008) Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat Rev Mol Cell Biol 9:690-701
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 13
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • DOI 10.1042/0264-6021:3480241
    • Bishop AL, Hall A (2000) Rho GTPases and their effector proteins. Biochem J 348:241-255 (Pubitemid 30345195)
    • (2000) Biochemical Journal , vol.348 , Issue.2 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 14
    • 0035898686 scopus 로고    scopus 로고
    • Recruitment of cortexillin into the cleavage furrow is controlled by Rac1 and IQGAP-related proteins
    • DOI 10.1093/emboj/20.14.3705
    • Faix J, Weber I, Mintert U, Köhler J, Lottspeich F, Marriott G (2001) Recruitment of cortexillin into the cleavage furrow is controlled by Rac1 and IQGAP-related proteins. EMBO J 20:3705-3715 (Pubitemid 32691782)
    • (2001) EMBO Journal , vol.20 , Issue.14 , pp. 3705-3715
    • Faix, J.1    Weber, I.2    Mintert, U.3    Kohler, J.4    Lottspeich, F.5    Marriott, G.6
  • 15
    • 56749160113 scopus 로고    scopus 로고
    • Design principles of biochemical oscillators
    • Novák B, Tyson JJ (2008) Design principles of biochemical oscillators. Nat Rev Mol Cell Biol 9:981-991
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 981-991
    • Novák, B.1    Tyson, J.J.2
  • 17
    • 0043093686 scopus 로고    scopus 로고
    • IQGAP proteins are integral components of cytoskeletal regulation
    • DOI 10.1038/sj.embor.embor867
    • Briggs MW, Sacks DB (2003) IQGAP proteins are integral components of cytoskeletal regulation. EMBO Rep 4:571-574 (Pubitemid 36939947)
    • (2003) EMBO Reports , vol.4 , Issue.6 , pp. 571-574
    • Briggs, M.W.1    Sacks, D.B.2
  • 18
    • 35748946040 scopus 로고    scopus 로고
    • Get to grips: Steering local actin dynamics with IQGAPs
    • DOI 10.1038/sj.embor.7401089, PII 7401089
    • Brandt DT, Grosse R (2007) Get to grips: steering local actin dynamics with IQGAPs. EMBO Rep 8:1019-1023 (Pubitemid 350042336)
    • (2007) EMBO Reports , vol.8 , Issue.11 , pp. 1019-1023
    • Brandt, D.T.1    Grosse, R.2
  • 19
    • 84856219974 scopus 로고    scopus 로고
    • IQGAP1 and its binding proteins control diverse biological functions
    • White CD, Erdemir HH, Sacks DB (2012) IQGAP1 and its binding proteins control diverse biological functions. Cell Signal 24:826-834
    • (2012) Cell Signal , vol.24 , pp. 826-834
    • White, C.D.1    Erdemir, H.H.2    Sacks, D.B.3
  • 20
    • 84858329431 scopus 로고    scopus 로고
    • IQGAP family members in yeast, Dictyostelium, and mammalian cells
    • Shannon KB (2012) IQGAP family members in yeast, Dictyostelium, and mammalian cells. Int J Cell Biol 2012:1-14
    • (2012) Int J Cell Biol , vol.2012 , pp. 1-14
    • Shannon, K.B.1
  • 21
    • 33748276641 scopus 로고    scopus 로고
    • Rho GTPase signaling in Dictyostelium discoideum: Insights from the genome
    • DOI 10.1016/j.ejcb.2006.04.011, PII S0171933506000811, A special issue dedicated to Guenter Gerisch on the occasion of his 75th birthday
    • Vlahou G, Rivero F (2006) Rho GTPase signaling in Dictyostelium discoideum: insights from the genome. Eur J Cell Biol 85:947-959 (Pubitemid 44317600)
    • (2006) European Journal of Cell Biology , vol.85 , Issue.9-10 , pp. 947-959
    • Vlahou, G.1    Rivero, F.2
  • 22
    • 84858148138 scopus 로고    scopus 로고
    • A dual role for Rac1 GTPases in the regulation of cell motility
    • Filić V, Marinović M, Faix J, Weber I (2012) A dual role for Rac1 GTPases in the regulation of cell motility. J Cell Sci 125:387-398
    • (2012) J Cell Sci , vol.125 , pp. 387-398
    • Filić, V.1    Marinović, M.2    Faix, J.3    Weber, I.4
  • 23
    • 0034619847 scopus 로고    scopus 로고
    • IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling
    • DOI 10.1038/35047107
    • Miki H, Yamaguchi H, Suetsugu S, Takenawa T (2000) IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature 408:732-735 (Pubitemid 32015990)
    • (2000) Nature , vol.408 , Issue.6813 , pp. 732-735
    • Miki, H.1    Yamaguchi, H.2    Suetsugu, S.3    Takenawa, T.4
  • 24
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
    • Eden S, Rohatgi R, Podtelejnikov AV, Mann M, Kirschner MW (2002) Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature 418:790-793
    • (2002) Nature , vol.418 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 25
    • 16044367114 scopus 로고    scopus 로고
    • Cortexillins, major determinants of cell shape and size, are actin- bundling proteins with a parallel coiled-coil tail
    • DOI 10.1016/S0092-8674(00)80136-1
    • Faix J, Steinmetz M, Boves H, Kammerer RA, Lottspeich F, Mintert U, Murphy J, Stock A, Aebi U, Gerisch G (1996) Cortexillins, major determinants of cell shape and size, are actin-bundling proteins with a parallel coiled-coil tail. Cell 86:631-642 (Pubitemid 26299494)
    • (1996) Cell , vol.86 , Issue.4 , pp. 631-642
    • Faix, J.1    Steinmetz, M.2    Boves, H.3    Kammerer, R.A.4    Lottspeich, F.5    Mintert, U.6    Murphy, J.7    Stock, A.8    Aebi, U.9    Gerisch, G.10
  • 26
    • 0031768407 scopus 로고    scopus 로고
    • The IQGAP-related protein DGAP1 interacts with Rac and is involved in the modulation of the F-actin cytoskeleton and control of cell motility
    • Faix J, Clougherty C, Konzok A, Mintert U, Murphy J, Albrecht R, Mühlbauer B, Kuhlmann J (1998) The IQGAP-related protein DGAP1 interacts with Rac and is involved in the modulation of the F-actin cytoskeleton and control of cell motility. J Cell Sci 111:3059-3071 (Pubitemid 28517394)
    • (1998) Journal of Cell Science , vol.111 , Issue.20 , pp. 3059-3071
    • Faix, J.1    Clougherty, C.2    Konzok, A.3    Mintert, U.4    Murphy, J.5    Albrecht, R.6    Muhlbauer, B.7    Kuhlmann, J.8
  • 27
    • 0030574044 scopus 로고    scopus 로고
    • DGAP1, a homologue of rasGTPase activating proteins that controls growth, cytokinesis, and development in Dictyostelium discoideum
    • DOI 10.1016/0014-5793(96)00963-5
    • Faix J, Dittrich W (1996) DGAP1, a homologue of rasGT-Pase activating proteins that controls growth, cytokinesis, and development in Dictyostelium discoideum. FEBS Lett 394: 251-257 (Pubitemid 26341453)
    • (1996) FEBS Letters , vol.394 , Issue.3 , pp. 251-257
    • Faix, J.1    Dittrich, W.2
  • 28
    • 1642446043 scopus 로고    scopus 로고
    • p-41-Arc subunit of human Arp2/3 complex is a p21-activated kinase-1-interacting substrate
    • DOI 10.1038/sj.embor.7400079
    • Vadlamudi RK, Li F, Barnes CJ, Bagheri-Yarmand R, Kumar R (2004) p41-Arc subunit of human Arp2/3 complex is a p21-activated kinase-1-interacting substrate. EMBO Rep 5:154-160 (Pubitemid 38401194)
    • (2004) EMBO Reports , vol.5 , Issue.2 , pp. 154-160
    • Vadlamudi, R.K.1    Li, F.2    Barnes, C.J.3    Bagheri-Yarmand, R.4    Kumar, R.5
  • 31
    • 16244411349 scopus 로고    scopus 로고
    • Calcium signalling in growth cone migration
    • Bolsover SR (2005) Calcium signalling in growth cone migration. Cell Calcium 37:395-402
    • (2005) Cell Calcium , vol.37 , pp. 395-402
    • Bolsover, S.R.1
  • 32
    • 34547957429 scopus 로고    scopus 로고
    • 2+ signaling events
    • DOI 10.1016/j.ceca.2007.02.010, PII S0143416007000462
    • Niggli E, Shirokova N (2007) A guide to sparkology: the taxonomy of elementary cellular Ca2+ signaling events. Cell Calcium 42:379-387 (Pubitemid 47263999)
    • (2007) Cell Calcium , vol.42 , Issue.4-5 , pp. 379-387
    • Niggli, E.1    Shirokova, N.2
  • 36
    • 1242298534 scopus 로고    scopus 로고
    • Chemotaxis: Signalling modules join hands at front and tail
    • DOI 10.1038/sj.embor.7400051
    • Postma M, Bosgraaf L, Loovers HM, Van Haastert PJM (2004) Chemotaxis: signalling modules join hands at front and tail. EMBO Rep 5:35-40 (Pubitemid 38228525)
    • (2004) EMBO Reports , vol.5 , Issue.1 , pp. 35-40
    • Postma, M.1    Bosgraaf, L.2    Loovers, H.M.3    Van Haastert, P.J.M.4
  • 38
    • 0035833255 scopus 로고    scopus 로고
    • Myosin II dynamics and cortical flow during contractile ring formation in Dictyostelium cells
    • Yumura S (2001) Myosin II dynamics and cortical flow during contractile ring formation in Dictyostelium cells. J Cell Biol 154:137-146
    • (2001) J Cell Biol , vol.154 , pp. 137-146
    • Yumura, S.1
  • 43
    • 0037044862 scopus 로고    scopus 로고
    • Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography
    • DOI 10.1126/science.1076184
    • Medalia O, Weber I, Frangakis AS, Nicastro D, Gerisch G, Baumeister W (2002) Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography. Science 298:1209-1213 (Pubitemid 35285482)
    • (2002) Science , vol.298 , Issue.5596 , pp. 1209-1213
    • Medalia, O.1    Weber, I.2    Frangakis, A.S.3    Nicastro, D.4    Gerisch, G.5    Baumeister, W.6
  • 44
    • 77951977342 scopus 로고    scopus 로고
    • Electron tomography reveals unbranched networks of actin filaments in lamellipodia
    • Urban E, Jacob S, Nemethova M, Resch GP, Small JV (2010) Electron tomography reveals unbranched networks of actin filaments in lamellipodia. Nat Cell Biol 12:429-435
    • (2010) Nat Cell Biol , vol.12 , pp. 429-435
    • Urban, E.1    Jacob, S.2    Nemethova, M.3    Resch, G.P.4    Small, J.V.5
  • 45
    • 84871519238 scopus 로고    scopus 로고
    • New insights into the regulation and cellular functions of the ARP2/3 complex
    • Rotty JD, Wu C, Bear JE (2013) New insights into the regulation and cellular functions of the ARP2/3 complex. Nat Rev Mol Cell Biol 14:7-12
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 7-12
    • Rotty, J.D.1    Wu, C.2    Bear, J.E.3
  • 46
    • 24644441368 scopus 로고    scopus 로고
    • The comings and goings of actin: Coupling protrusion and retraction in cell motility
    • DOI 10.1016/j.ceb.2005.08.004, PII S0955067405001079
    • Small JV, Resch GP (2005) The comings and goings of actin: coupling protrusion and retraction in cell motility. Curr Opin Cell Biol 17:517-523 (Pubitemid 41267166)
    • (2005) Current Opinion in Cell Biology , vol.17 , Issue.5 SPEC. ISS. , pp. 517-523
    • Small, J.V.1    Resch, G.P.2
  • 47
    • 0035735907 scopus 로고    scopus 로고
    • On the mechanism of cleavage furrow ingression in Dictyostelium
    • Weber I (2001) On the mechanism of cleavage furrow ingression in Dictyostelium. Cell Struct Funct 26:577-584
    • (2001) Cell Struct Funct , vol.26 , pp. 577-584
    • Weber, I.1
  • 48
    • 0033081026 scopus 로고    scopus 로고
    • Cytokinesis mediated through the recruitment of cortexillins into the cleavage furrow
    • DOI 10.1093/emboj/18.3.586
    • Weber I, Gerisch G, Heizer C, Murphy J, Badelt K, Stock A, Schwartz JM, Faix J (1999) Cytokinesis mediated through the recruitment of cortexillins into the cleavage furrow. EMBO J 18:586-594 (Pubitemid 29057243)
    • (1999) EMBO Journal , vol.18 , Issue.3 , pp. 586-594
    • Weber, I.1    Gerisch, G.2    Heizer, C.3    Murphy, J.4    Badelt, K.5    Stock, A.6    Schwartz, J.-M.7    Faix, J.8
  • 50
    • 38849209071 scopus 로고    scopus 로고
    • Abi Mutants in Dictyostelium Reveal Specific Roles for the SCAR/WAVE Complex in Cytokinesis
    • DOI 10.1016/j.cub.2008.01.026, PII S0960982208000730
    • Pollitt AY, Insall RH (2008) Abi mutants in Dictyostelium reveal specific roles for the SCAR/WAVE complex in cytokinesis. Curr Biol 18:203-210 (Pubitemid 351192320)
    • (2008) Current Biology , vol.18 , Issue.3 , pp. 203-210
    • Pollitt, A.Y.1    Insall, R.H.2
  • 51
    • 79960706295 scopus 로고    scopus 로고
    • The 'invisible hand': Regulation of RHO GTPases by RHOGDIs
    • Garcia-Mata R, Boulter E, Burridge K (2011) The 'invisible hand': regulation of RHO GTPases by RHOGDIs. Nat Rev Mol Cell Biol 12:493-504
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 493-504
    • Garcia-Mata, R.1    Boulter, E.2    Burridge, K.3
  • 53
    • 10344260216 scopus 로고    scopus 로고
    • Phosphorylation of IQGAP1 modulates its binding to Cdc42, revealing a new type of Rho-GTPase regulator
    • DOI 10.1074/jbc.M408113200
    • Grohmanova K, Schlaepfer D, Hess D, Gutierrez P, Beck M, Kroschewski R (2004) Phosphorylation of IQGAP1 modulates its binding to Cdc42, revealing a new type of rho-GTPase regulator. J Biol Chem 279:48495-48504 (Pubitemid 39625723)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.47 , pp. 48495-48504
    • Grohmanova, K.1    Schlaepfer, D.2    Hess, D.3    Gutierrez, P.4    Beck, M.5    Kroschewski, R.6
  • 54
    • 84876463300 scopus 로고    scopus 로고
    • A dual role model for active Rac1 in cell migration
    • Faix J, Weber I (2013) A dual role model for active Rac1 in cell migration. Small GTPases 4:110-115
    • (2013) Small GTPases , vol.4 , pp. 110-115
    • Faix, J.1    Weber, I.2
  • 56
    • 34547699211 scopus 로고    scopus 로고
    • Mathematical model for spatial segregation of the Rho-family GTPases based on inhibitory crosstalk
    • DOI 10.1007/s11538-007-9200-6
    • Jilkine A, Marée AFM, Edelstein-Keshet L (2007) Mathematical model for spatial segregation of the Rho-family GTPases based on inhibitory crosstalk. Bull Math Biol 69:1943-1978 (Pubitemid 47222246)
    • (2007) Bulletin of Mathematical Biology , vol.69 , Issue.6 , pp. 1943-1978
    • Jilkine, A.1    Maree, A.F.M.2    Edelstein-Keshet, L.3
  • 57
    • 33646764616 scopus 로고    scopus 로고
    • Spontaneous polarization in eukaryotic gradient sensing: A mathematical model based on mutual inhibition of frontness and backness pathways
    • Narang A (2006) Spontaneous polarization in eukaryotic gradient sensing: a mathematical model based on mutual inhibition of frontness and backness pathways. J Theor Biol 240:538-553
    • (2006) J Theor Biol , vol.240 , pp. 538-553
    • Narang, A.1
  • 58
    • 33845932606 scopus 로고    scopus 로고
    • Role of RacC for the regulation of WASP and phosphatidylinositol 3-kinase during chemotaxis of Dictyostelium
    • DOI 10.1074/jbc.M605997200
    • Han JW, Leeper L, Rivero F, Chung CY (2006) Role of RacC for the regulation of WASP and phosphatidylinositol 3-kinase during chemotaxis of Dictyostelium. J Biol Chem 281:35224-35234 (Pubitemid 46036560)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.46 , pp. 35224-35234
    • Han, J.W.1    Leeper, L.2    Rivero, F.3    Chung, C.Y.4
  • 59
    • 0029945192 scopus 로고    scopus 로고
    • A novel member of the rho family of small GTP-binding proteins is specifically required for cytokinesis
    • DOI 10.1083/jcb.133.6.1321
    • Larochelle DA, Vithalani KK, De Lozanne A (1996) A novel member of the rho family of small GTP-binding proteins is specifically required for cytokinesis. J Cell Biol 133:1321-1329 (Pubitemid 26192332)
    • (1996) Journal of Cell Biology , vol.133 , Issue.6 , pp. 1321-1329
    • Larochelle, D.A.1    Vithalani, K.K.2    De Lozanne, A.3
  • 61
    • 0034009562 scopus 로고    scopus 로고
    • The Dictyostelium RasS protein is required for macropinocytosis, phagocytosis and the control of cell movement
    • Chubb JR, Wilkins A, Thomas GM, Insall RH (2000) The Dictyostelium RasS protein is required for macropinocytosis, phagocytosis and the control of cell movement. J Cell Sci 113:709-719 (Pubitemid 30133048)
    • (2000) Journal of Cell Science , vol.113 , Issue.4 , pp. 709-719
    • Chubb, J.R.1    Wilkins, A.2    Thomas, G.M.3    Insall, R.H.4
  • 63
    • 0027772188 scopus 로고
    • The locomotion, shape and pseudopodial dynamics of unstimulated Dictyostelium cells are not random
    • Killich T, Plath PJ, Wei X, Bultmann H, Rensing L, Vicker MG (1993) The locomotion, shape and pseudopodial dynamics of unstimulated Dictyostelium cells are not random. J Cell Sci 106:1005-1013 (Pubitemid 24018389)
    • (1993) Journal of Cell Science , vol.106 , Issue.4 , pp. 1005-1013
    • Killich, T.1    Plath, P.J.2    Wei, X.3    Bultmann, H.4    Rensing, L.5    Vicker, M.G.6
  • 64
    • 0030892179 scopus 로고    scopus 로고
    • Inversely correlated cycles in speed and turning in an ameba: An oscillatory model of cell locomotion
    • Shenderov AD, Sheetz MP (1997) Inversely correlated cycles in speed and turning in an ameba: an oscillatory model of cell locomotion. Biophys J 72:2382-2389 (Pubitemid 27184467)
    • (1997) Biophysical Journal , vol.72 , Issue.5 , pp. 2382-2389
    • Shenderov, A.D.1    Sheetz, M.P.2
  • 65
    • 33748259785 scopus 로고    scopus 로고
    • Is there a pilot in a pseudopod?
    • Weber I (2006) Is there a pilot in a pseudopod? Eur J Cell Biol 85:915-924
    • (2006) Eur J Cell Biol , vol.85 , pp. 915-924
    • Weber, I.1
  • 66
    • 78650478516 scopus 로고    scopus 로고
    • A conceptual molecular network for chemotactic behaviors characterized by feedback of molecules cycling between the membrane and the cytosol
    • Otsuji M, Terashima Y, Ishihara S, Kuroda S, Matsushima K (2010) A conceptual molecular network for chemotactic behaviors characterized by feedback of molecules cycling between the membrane and the cytosol. Sci Signal 3:ra89
    • (2010) Sci Signal , vol.3
    • Otsuji, M.1    Terashima, Y.2    Ishihara, S.3    Kuroda, S.4    Matsushima, K.5
  • 67
    • 0037376655 scopus 로고    scopus 로고
    • Sniffers, buzzers, toggles and blinkers: Dynamics of regulatory and signaling pathways in the cell
    • DOI 10.1016/S0955-0674(03)00017-6
    • Tyson JJ, Chen KC, Novak B (2003) Sniffers, buzzers, toggles and blinkers: dynamics of regulatory and signaling pathways in the cell. Curr Opin Cell Biol 15:221-231 (Pubitemid 36332198)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.2 , pp. 221-231
    • Tyson, J.J.1    Chen, K.C.2    Novak, B.3
  • 69
  • 71
    • 0033588976 scopus 로고    scopus 로고
    • Op18/stathmin mediates multiple region-specific tubulin and microtubule- regulating activities
    • DOI 10.1083/jcb.146.6.1289
    • Larsson N, Segerman B, Howell B, Fridell K, Cassimeris L, Gullberg M (1999) Op18/stathmin mediates multiple regionspecific tubulin and microtubule-regulating activities. J Cell Biol 146:1289-1302 (Pubitemid 29477696)
    • (1999) Journal of Cell Biology , vol.146 , Issue.6 , pp. 1289-1302
    • Larsson, N.1    Segerman, B.2    Howell, B.3    Fridell, K.4    Cassimeris, L.5    Gullberg, M.6
  • 73
    • 0028221324 scopus 로고
    • Calcium and magnesium binding to rat parvalbumin
    • DOI 10.1111/j.1432-1033.1994.tb18836.x
    • Eberhard M, Erne P (1994) Calcium and magnesium binding to rat parvalbumin. Eur J Biochem 222:21-26 (Pubitemid 24161320)
    • (1994) European Journal of Biochemistry , vol.222 , Issue.1 , pp. 21-26
    • Eberhard, M.1    Erne, P.2
  • 76
    • 26944450513 scopus 로고    scopus 로고
    • An electrostatic steering mechanism of Cdc42 recognition by Wiskott-Aldrich syndrome proteins
    • DOI 10.1016/j.molcel.2005.08.036, PII S1097276505016023
    • Hemsath L, Dvorsky R, Fiegen D, Carlier M-F, Ahmadian MR (2005) An electrostatic steering mechanism of Cdc42 recognition by Wiskott-Aldrich syndrome proteins. Mol Cell 20:313-324 (Pubitemid 41484175)
    • (2005) Molecular Cell , vol.20 , Issue.2 , pp. 313-324
    • Hemsath, L.1    Dvorsky, R.2    Fiegen, D.3    Carlier, M.-F.4    Ahmadian, M.R.5
  • 77
    • 67649392701 scopus 로고    scopus 로고
    • Determination of in vivo dissociation constant, KD, of Cdc42-effector complexes in live mammalian cells using single wavelength fluorescence cross-correlation spectroscopy
    • Sudhaharan T, Liu P, Foo YH, Bu W, Lim KB, Wohland T, Ahmed S (2009) Determination of in vivo dissociation constant, KD, of Cdc42-effector complexes in live mammalian cells using single wavelength fluorescence cross-correlation spectroscopy. J Biol Chem 284:13602-13609
    • (2009) J Biol Chem , vol.284 , pp. 13602-13609
    • Sudhaharan, T.1    Liu, P.2    Foo, Y.H.3    Bu, W.4    Lim, K.B.5    Wohland, T.6    Ahmed, S.7
  • 78
    • 0034673107 scopus 로고    scopus 로고
    • Residues in Cdc42 that specify binding to individual CRIB effector proteins
    • DOI 10.1021/bi991567z
    • Owen D, Mott HR, Laue ED, Lowe PN (2000) Residues in Cdc42 that specify binding to individual crib effector proteins. Biochemistry 39:1243-1250 (Pubitemid 30090690)
    • (2000) Biochemistry , vol.39 , Issue.6 , pp. 1243-1250
    • Owen, D.1    Mott, H.R.2    Laue, E.D.3    Lowe, P.N.4
  • 80
    • 0032568579 scopus 로고    scopus 로고
    • Delineation of the Cdc42/Rac-binding domain of p21-activated kinase
    • DOI 10.1021/bi980140+
    • Thompson G, Owen D, Chalk PA, Lowe PN (1998) Delineation of the Cdc42/Rac-binding domain of p21-activated kinase. Biochemistry 37:7885-7891 (Pubitemid 28248649)
    • (1998) Biochemistry , vol.37 , Issue.21 , pp. 7885-7891
    • Thompson, G.1    Owen, D.2    Chalk, P.A.3    Lowe, P.N.4
  • 81
    • 0347627541 scopus 로고    scopus 로고
    • Comparative functional analysis of the Rac GTPases
    • DOI 10.1016/S0014-5793(03)01351-6
    • Haeusler LC, Blumenstein L, Stege P, Dvorsky R, Ahmadian MR (2003) Comparative functional analysis of the Rac GTPases. FEBS Lett 555:556-560 (Pubitemid 37532610)
    • (2003) FEBS Letters , vol.555 , Issue.3 , pp. 556-560
    • Haeusler, L.C.1    Blumenstein, L.2    Stege, P.3    Dvorsky, R.4    Ahmadian, M.R.5
  • 83
    • 0030746214 scopus 로고    scopus 로고
    • Rac binding to p67(phox). Structural basis for interactions of the Rac1 effector region and insert region with components of the respiratory burst oxidase
    • DOI 10.1074/jbc.272.30.18834
    • Nisimoto Y, Freeman JL, Motalebi SA, Hirshberg M, Lambeth JD (1997) Rac binding to p67(phox). Structural basis for interactions of the Rac1 effector region and insert region with components of the respiratory burst oxidase. J Biol Chem 272:18834-18841 (Pubitemid 27318232)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.30 , pp. 18834-18841
    • Nisimoto, Y.1    Freeman, J.L.R.2    Motalebi, S.A.3    Hirshberg, M.4    Lambeth, J.D.5
  • 84
    • 84904345599 scopus 로고    scopus 로고
    • Biochemical analysis of the interactions of IQGAP1 C-terminal domain with CDC42
    • Elliott SF, Allen G, Timson DJ (2012) Biochemical analysis of the interactions of IQGAP1 C-terminal domain with CDC42. World J Biol Chem 3:53-60
    • (2012) World J Biol Chem , vol.3 , pp. 53-60
    • Elliott, S.F.1    Allen, G.2    Timson, D.J.3
  • 86
    • 68949136866 scopus 로고    scopus 로고
    • Determination of dissociation constants in living zebrafish embryos with single wavelength fluorescence crosscorrelation spectroscopy
    • Shi X, Foo YH, Sudhaharan T, Chong S-W, Korzh V, Ahmed S, Wohland T (2009) Determination of dissociation constants in living zebrafish embryos with single wavelength fluorescence crosscorrelation spectroscopy. Biophys J 97:678-686
    • (2009) Biophys J , vol.97 , pp. 678-686
    • Shi, X.1    Foo, Y.H.2    Sudhaharan, T.3    Chong, S.-W.4    Korzh, V.5    Ahmed, S.6    Wohland, T.7
  • 88
    • 0029864175 scopus 로고    scopus 로고
    • Equilibrium and kinetic measurements reveal rapidly reversible binding of Ras to Raf
    • DOI 10.1074/jbc.271.12.6713
    • Gorman C, Skinner RH, Skelly JV, Neidle S, Lowe PN (1996) Equilibrium and kinetic measurements reveal rapidly reversible binding of Ras to Raf. J Biol Chem 271:6713-6719 (Pubitemid 26104102)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.12 , pp. 6713-6719
    • Gorman, C.1    Skinner, R.H.2    Skelly, J.V.3    Neidle, S.4    Lowe, P.N.5
  • 89
    • 0032491205 scopus 로고    scopus 로고
    • Transient kinetic studies on the interaction of Ras and the Ras-binding domain of c-Raf-1 reveal rapid equilibration of the complex
    • DOI 10.1021/bi980764f
    • Sydor JR, Engelhard M, Wittinghofer A, Goody RS, Herrmann C (1998) Transient kinetic studies on the interaction of Ras and the Ras-binding domain of c-Raf-1 reveal rapid equilibration of the complex. Biochemistry 37:14292-14299 (Pubitemid 28471265)
    • (1998) Biochemistry , vol.37 , Issue.40 , pp. 14292-14299
    • Sydor, J.R.1    Engelhard, M.2    Wittinghofer, A.3    Goody, R.S.4    Herrmann, C.5
  • 90
    • 0033532074 scopus 로고    scopus 로고
    • Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily
    • Linnemann T, Geyer M, Jaitner BK, Block C, Kalbitzer HR, Wittinghofer A, Herrmann C (1999) Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily. J Biol Chem 274:13556-13562
    • (1999) J Biol Chem , vol.274 , pp. 13556-13562
    • Linnemann, T.1    Geyer, M.2    Jaitner, B.K.3    Block, C.4    Kalbitzer, H.R.5    Wittinghofer, A.6    Herrmann, C.7
  • 91
    • 0037040885 scopus 로고    scopus 로고
    • The activation of RalGDS can be achieved independently of its Ras binding domain: Implications of an activation mechanism in Ras effector specificity and signal distribution
    • DOI 10.1074/jbc.M110800200
    • Linnemann T, Kiel C, Herter P, Herrmann C (2002) The activation of RalGDS can be achieved independently of its Ras binding domain. implications of an activation mechanism in Ras effector specificity and signal distribution. J Biol Chem 277:7831-7837 (Pubitemid 34968231)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.10 , pp. 7831-7837
    • Linnemann, T.1    Kiel, C.2    Herter, P.3    Herrmann, C.4
  • 93
    • 0035184240 scopus 로고    scopus 로고
    • Solution structure of the Ras binding domain of the protein kinase Byr2 from Schizosaccharomyces pombe
    • DOI 10.1016/S0969-2126(01)00671-2, PII S0969212601006712
    • Gronwald W, Huber F, Grünewald P, Spörner M, Wohlgemuth S, Herrmann C, Kalbitzer HR (2001) Solution structure of the Ras binding domain of the protein kinase Byr2 from Schizosaccharomyces pombe. Structure 9:1029-1041 (Pubitemid 33092106)
    • (2001) Structure , vol.9 , Issue.11 , pp. 1029-1041
    • Gronwald, W.1    Huber, F.2    Grunewald, P.3    Sporner, M.4    Wohlgemuth, S.5    Herrmann, C.6    Kalbitzer, H.R.7
  • 94
    • 47949124438 scopus 로고    scopus 로고
    • Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II
    • Stieglitz B, Bee C, Schwarz D, Yildiz O, Moshnikova A, Khokhlatchev A, Herrmann C (2008) Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II. EMBO J 27:1995-2005
    • (2008) EMBO J , vol.27 , pp. 1995-2005
    • Stieglitz, B.1    Bee, C.2    Schwarz, D.3    Yildiz, O.4    Moshnikova, A.5    Khokhlatchev, A.6    Herrmann, C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.