메뉴 건너뛰기




Volumn 107, Issue 8, 2006, Pages 3145-3152

Arf6 plays an early role in platelet activation by collagen and convulxin

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 3; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 6; COLLAGEN; CONVULXIN; GUANOSINE TRIPHOSPHATASE; PEPTIDE; PROTEIN CDC42; RAC1 PROTEIN; RAL PROTEIN; RAP1 PROTEIN; RHO GUANOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG;

EID: 33645736307     PISSN: 00064971     EISSN: 00064971     Source Type: Journal    
DOI: 10.1182/blood-2005-09-3563     Document Type: Article
Times cited : (43)

References (66)
  • 1
    • 0038494921 scopus 로고    scopus 로고
    • Platelet-collagen interaction: Is GPVI the central receptor?
    • Nieswandt B, Watson SP. Platelet-collagen interaction: is GPVI the central receptor? Blood. 2003;102:449-461.
    • (2003) Blood , vol.102 , pp. 449-461
    • Nieswandt, B.1    Watson, S.P.2
  • 2
    • 0141484537 scopus 로고    scopus 로고
    • Thrombin and platelet activation
    • Brass LF. Thrombin and platelet activation. Chest. 2003;124:18S-25S.
    • (2003) Chest , vol.124
    • Brass, L.F.1
  • 3
    • 4444313230 scopus 로고    scopus 로고
    • Platelet receptors for adenine nucleotides and thromboxane A2
    • Murugappan S, Shankar H, Kunapuli SP. Platelet receptors for adenine nucleotides and thromboxane A2. Semin Thromb Hemost. 2004;30:411-418.
    • (2004) Semin Thromb Hemost , vol.30 , pp. 411-418
    • Murugappan, S.1    Shankar, H.2    Kunapuli, S.P.3
  • 4
    • 0035895076 scopus 로고    scopus 로고
    • Rac, a small guanosine triphosphate-binding protein, and p21-activated kinase are activated during platelet spreading on collagen-coated surfaces: Roles of integrin α2β1
    • Suzuki-Inoue K, Yatomi Y, Asazuma N, et al. Rac, a small guanosine triphosphate-binding protein, and p21-activated kinase are activated during platelet spreading on collagen-coated surfaces: roles of integrin α2β1. Blood. 2001;98:3708-3716.
    • (2001) Blood , vol.98 , pp. 3708-3716
    • Suzuki-Inoue, K.1    Yatomi, Y.2    Asazuma, N.3
  • 5
    • 0037114750 scopus 로고    scopus 로고
    • Cdc42/Rac1-dependent activation of the p21-activated kinase (PAK) regulates human platelet lamellipodia spreading: Implication of the cortical-actin binding protein cortactin
    • Vidal C, Geny B, Melle J, Jandrot-Perrus M, Fontenay-Roupie M. Cdc42/Rac1-dependent activation of the p21-activated kinase (PAK) regulates human platelet lamellipodia spreading: implication of the cortical-actin binding protein cortactin. Blood. 2002;100:4462-4469.
    • (2002) Blood , vol.100 , pp. 4462-4469
    • Vidal, C.1    Geny, B.2    Melle, J.3    Jandrot-Perrus, M.4    Fontenay-Roupie, M.5
  • 6
    • 4744370340 scopus 로고    scopus 로고
    • Rho and Rho-kinase mediate thrombin-induced phosphatidylinositol 4-phosphate 5-kinase trafficking in platelets
    • Yang SA, Carpenter CL, Abrams CS. Rho and Rho-kinase mediate thrombin-induced phosphatidylinositol 4-phosphate 5-kinase trafficking in platelets. J Biol Chem. 2004;279:42331-42336.
    • (2004) J Biol Chem , vol.279 , pp. 42331-42336
    • Yang, S.A.1    Carpenter, C.L.2    Abrams, C.S.3
  • 7
    • 0037067748 scopus 로고    scopus 로고
    • Relationships between Rap1b, affinity modulation of integrin αIIbβ3, and the actin cytoskeleton
    • Bertoni A, Tadokoro S, Eto K, et al. Relationships between Rap1b, affinity modulation of integrin αIIbβ3, and the actin cytoskeleton. J Biol Chem. 2002;277:25715-25721.
    • (2002) J Biol Chem , vol.277 , pp. 25715-25721
    • Bertoni, A.1    Tadokoro, S.2    Eto, K.3
  • 9
    • 0033199617 scopus 로고    scopus 로고
    • Rab6 is phosphorylated in thrombin-activated platelets by a protein kinase C-dependent mechanism: Effects on GTP/GDP binding and cellular distribution
    • Fitzgerald ML, Reed GL. Rab6 is phosphorylated in thrombin-activated platelets by a protein kinase C-dependent mechanism: effects on GTP/GDP binding and cellular distribution. Biochem J. 1999;342:353-360.
    • (1999) Biochem J , vol.342 , pp. 353-360
    • Fitzgerald, M.L.1    Reed, G.L.2
  • 11
    • 1642275392 scopus 로고    scopus 로고
    • Munc13-4 is a GTP-Rab27-binding protein regulating dense core granule secretion in platelets
    • Shirakawa R, Higashi T, Tabuchi A, et al. Munc13-4 is a GTP-Rab27-binding protein regulating dense core granule secretion in platelets. J Biol Chem. 2004;279:10730-10737.
    • (2004) J Biol Chem , vol.279 , pp. 10730-10737
    • Shirakawa, R.1    Higashi, T.2    Tabuchi, A.3
  • 12
    • 0031944085 scopus 로고    scopus 로고
    • Activation of the small GTPase Ral in platelets
    • Wolthuis RM, Franke B, van Triest M, et al. Activation of the small GTPase Ral in platelets. Mol Cell Biol. 1998;18:2486-2491.
    • (1998) Mol Cell Biol , vol.18 , pp. 2486-2491
    • Wolthuis, R.M.1    Franke, B.2    Van Triest, M.3
  • 13
    • 0030570831 scopus 로고    scopus 로고
    • Association of Ral GTP-binding protein with human platelet dense granules
    • Mark BL, Jilkina O, Bhullar RP. Association of Ral GTP-binding protein with human platelet dense granules. Biochem Biophys Res Commun. 1996;225:40-46.
    • (1996) Biochem Biophys Res Commun , vol.225 , pp. 40-46
    • Mark, B.L.1    Jilkina, O.2    Bhullar, R.P.3
  • 14
    • 0037047280 scopus 로고    scopus 로고
    • Calmodulin binds RalA and RalB and is required for the thrombin-induced activation of Ral in human platelets
    • Clough RR, Sidhu RS, Bhullar RP. Calmodulin binds RalA and RalB and is required for the thrombin-induced activation of Ral in human platelets. J Biol Chem. 2002;277:28972-28980.
    • (2002) J Biol Chem , vol.277 , pp. 28972-28980
    • Clough, R.R.1    Sidhu, R.S.2    Bhullar, R.P.3
  • 15
    • 0034700364 scopus 로고    scopus 로고
    • Molecular aspects of the cellular activities of ADP-ribosylation factors
    • Randazzo PA, Nie Z, Miura K, Hsu VW. Molecular aspects of the cellular activities of ADP-ribosylation factors. Sci STKE. 2000;2000:RE1.
    • (2000) Sci STKE , vol.2000
    • Randazzo, P.A.1    Nie, Z.2    Miura, K.3    Hsu, V.W.4
  • 16
    • 0142211351 scopus 로고    scopus 로고
    • Multiple roles for Arf6: Sorting, structuring, and signaling at the plasma membrane
    • Donaldson JG. Multiple roles for Arf6: sorting, structuring, and signaling at the plasma membrane. J Biol Chem. 2003;278:41573-41576.
    • (2003) J Biol Chem , vol.278 , pp. 41573-41576
    • Donaldson, J.G.1
  • 17
    • 0026708135 scopus 로고
    • The amino terminus of ADP-ribosylation factor (ARF) is a critical determinant of ARF activities and is a potent and specific inhibitor of protein transport
    • Kahn RA, Randazzo P, Serafini T, et al. The amino terminus of ADP-ribosylation factor (ARF) is a critical determinant of ARF activities and is a potent and specific inhibitor of protein transport. J Biol Chem. 1992;267:13039-13046.
    • (1992) J Biol Chem , vol.267 , pp. 13039-13046
    • Kahn, R.A.1    Randazzo, P.2    Serafini, T.3
  • 18
    • 0031037998 scopus 로고    scopus 로고
    • Regulated exocytosis in chromaffin cells: A potential role for a secretory granule-associated ARF6 protein
    • Galas MC, Helms JB, Vitale N, Thierse D, Aunis D, Bader MF. Regulated exocytosis in chromaffin cells: a potential role for a secretory granule-associated ARF6 protein. J Biol Chem. 1997;272:2788-2793.
    • (1997) J Biol Chem , vol.272 , pp. 2788-2793
    • Galas, M.C.1    Helms, J.B.2    Vitale, N.3    Thierse, D.4    Aunis, D.5    Bader, M.F.6
  • 19
    • 0031889838 scopus 로고    scopus 로고
    • Regulated exocytosis in chromaffin cells: Translocation of ARF6 stimulates a plasma membrane-associated phospholipase D
    • Caumont AS, Galas MC, Vitale N, Aunis D, Bader MF. Regulated exocytosis in chromaffin cells: translocation of ARF6 stimulates a plasma membrane-associated phospholipase D. J Biol Chem. 1998;273:1373-1379.
    • (1998) J Biol Chem , vol.273 , pp. 1373-1379
    • Caumont, A.S.1    Galas, M.C.2    Vitale, N.3    Aunis, D.4    Bader, M.F.5
  • 20
    • 0346729933 scopus 로고    scopus 로고
    • ARNO and ARF6 regulate axonal elongation and branching through downstream activation of phosphatidylinositol 4-phosphate 5-kinase alpha
    • Hernandez-Deviez DJ, Roth MG, Casanova JE, Wilson JM. ARNO and ARF6 regulate axonal elongation and branching through downstream activation of phosphatidylinositol 4-phosphate 5-kinase alpha. Mol Biol Cell. 2004;15:111-120.
    • (2004) Mol Biol Cell , vol.15 , pp. 111-120
    • Hernandez-Deviez, D.J.1    Roth, M.G.2    Casanova, J.E.3    Wilson, J.M.4
  • 21
    • 0035837426 scopus 로고    scopus 로고
    • The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways
    • Tarricone C, Xiao B, Justin N, et al. The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. Nature. 2001;411:215-219.
    • (2001) Nature , vol.411 , pp. 215-219
    • Tarricone, C.1    Xiao, B.2    Justin, N.3
  • 22
    • 0034812543 scopus 로고    scopus 로고
    • Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1
    • Shin OH, Exton JH. Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1. Biochem Biophys Res Commun. 2001;285:1267-1273.
    • (2001) Biochem Biophys Res Commun , vol.285 , pp. 1267-1273
    • Shin, O.H.1    Exton, J.H.2
  • 23
    • 0346725004 scopus 로고    scopus 로고
    • Arf GAPs: Multifunctional proteins that regulate membrane traffic and actin remodelling
    • Randazzo PA, Hirsch DS. Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling. Cell Signal. 2004;16:401-413.
    • (2004) Cell Signal , vol.16 , pp. 401-413
    • Randazzo, P.A.1    Hirsch, D.S.2
  • 24
    • 0034306280 scopus 로고    scopus 로고
    • Cytohesins and centaurins: Mediators of PI 3-kinase-regulated Arf signaling
    • Jackson TR, Kearns BG, Theibert AB. Cytohesins and centaurins: mediators of PI 3-kinase-regulated Arf signaling. Trends Biochem Sci. 2000;25:489-495.
    • (2000) Trends Biochem Sci , vol.25 , pp. 489-495
    • Jackson, T.R.1    Kearns, B.G.2    Theibert, A.B.3
  • 25
    • 4644262225 scopus 로고    scopus 로고
    • Platelet glycoprotein VI: Its structure and function
    • Moroi M, Jung SM. Platelet glycoprotein VI: its structure and function. Thromb Res. 2004;114:221-233.
    • (2004) Thromb Res , vol.114 , pp. 221-233
    • Moroi, M.1    Jung, S.M.2
  • 26
    • 0037441754 scopus 로고    scopus 로고
    • Identification of P2Y12-dependent and -independent mechanisms of glycoprotein VI-mediated Rap1 activation in platelets
    • Larson MK, Chen H, Kahn ML, et al. Identification of P2Y12-dependent and -independent mechanisms of glycoprotein VI-mediated Rap1 activation in platelets. Blood. 2003;101:1409-1415.
    • (2003) Blood , vol.101 , pp. 1409-1415
    • Larson, M.K.1    Chen, H.2    Kahn, M.L.3
  • 27
    • 13244262795 scopus 로고    scopus 로고
    • Activation of the small GTPase Rap2B in agonist-stimulated human platelets
    • Greco F, Sinigaglia F, Balduini C, Torti M. Activation of the small GTPase Rap2B in agonist-stimulated human platelets. J Thromb Haemost. 2004;2:2223-2230.
    • (2004) J Thromb Haemost , vol.2 , pp. 2223-2230
    • Greco, F.1    Sinigaglia, F.2    Balduini, C.3    Torti, M.4
  • 28
    • 0035798144 scopus 로고    scopus 로고
    • Characterisation of Rac activation in thrombin- and collagen-stimulated human blood platelets
    • Soulet C, Gendreau S, Missy K, Benard V, Plantavid M, Payrastre B. Characterisation of Rac activation in thrombin- and collagen-stimulated human blood platelets. FEBS Lett. 2001;507:253-258.
    • (2001) FEBS Lett , vol.507 , pp. 253-258
    • Soulet, C.1    Gendreau, S.2    Missy, K.3    Benard, V.4    Plantavid, M.5    Payrastre, B.6
  • 29
    • 0036208705 scopus 로고    scopus 로고
    • Towards complete analysis of the platelet proteome
    • O'Neill EE, Brock CJ, von Kriegsheim AF, et al. Towards complete analysis of the platelet proteome. Proteomics. 2002;2:288-305.
    • (2002) Proteomics , vol.2 , pp. 288-305
    • O'Neill, E.E.1    Brock, C.J.2    Von Kriegsheim, A.F.3
  • 30
    • 0037458731 scopus 로고    scopus 로고
    • CrkL directs ASAP1 to peripheral focal adhesions
    • Oda A, Wada I, Miura K, et al. CrkL directs ASAP1 to peripheral focal adhesions. J Biol Chem. 2003;278:6456-6460.
    • (2003) J Biol Chem , vol.278 , pp. 6456-6460
    • Oda, A.1    Wada, I.2    Miura, K.3
  • 31
    • 0031690587 scopus 로고    scopus 로고
    • Localization of endogenous ARF6 to sites of cortical actin rearrangement and involvement of ARF6 in cell spreading
    • Song J, Khachikian Z, Radhakrishna H, Donaldson JG. Localization of endogenous ARF6 to sites of cortical actin rearrangement and involvement of ARF6 in cell spreading. J Cell Sci. 1998;111:2257-2267.
    • (1998) J Cell Sci , vol.111 , pp. 2257-2267
    • Song, J.1    Khachikian, Z.2    Radhakrishna, H.3    Donaldson, J.G.4
  • 32
    • 0033573955 scopus 로고    scopus 로고
    • Intracellular localization of SNAP-23 to endosomal compartments
    • Chen D, Whiteheart SW. Intracellular localization of SNAP-23 to endosomal compartments. Biochem Biophys Res Commun. 1999;255:340-346.
    • (1999) Biochem Biophys Res Commun , vol.255 , pp. 340-346
    • Chen, D.1    Whiteheart, S.W.2
  • 33
    • 0037020150 scopus 로고    scopus 로고
    • SNAP-23 is a target for calpain cleavage in activated platelets
    • Rutledge TW, Whiteheart SW. SNAP-23 is a target for calpain cleavage in activated platelets. J Biol Chem. 2002;277:37009-37015.
    • (2002) J Biol Chem , vol.277 , pp. 37009-37015
    • Rutledge, T.W.1    Whiteheart, S.W.2
  • 34
    • 0034599528 scopus 로고    scopus 로고
    • GGAs: A family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex
    • Dell'Angelica EC, Puertollano R, Mullins C, et al. GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex. J Cell Biol. 2000;149:81-94.
    • (2000) J Cell Biol , vol.149 , pp. 81-94
    • Dell'Angelica, E.C.1    Puertollano, R.2    Mullins, C.3
  • 35
    • 0037101770 scopus 로고    scopus 로고
    • GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors
    • Takatsu H, Yoshino K, Toda K, Nakayama K. GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors. Biochem J. 2002;365:369-378.
    • (2002) Biochem J , vol.365 , pp. 369-378
    • Takatsu, H.1    Yoshino, K.2    Toda, K.3    Nakayama, K.4
  • 37
    • 0033777071 scopus 로고    scopus 로고
    • Determination of GTP loading on Rho
    • Ren XD, Schwartz MA. Determination of GTP loading on Rho. Methods Enzymol. 2000;325:264-272.
    • (2000) Methods Enzymol , vol.325 , pp. 264-272
    • Ren, X.D.1    Schwartz, M.A.2
  • 38
    • 0031014969 scopus 로고    scopus 로고
    • 2+-mediated activation of Rap1 in human platelets
    • 2+-mediated activation of Rap1 in human platelets. EMBO J. 1997;16:252-259.
    • (1997) EMBO J , vol.16 , pp. 252-259
    • Franke, B.1    Akkerman, J.W.2    Bos, J.L.3
  • 40
    • 0029832697 scopus 로고    scopus 로고
    • Intracellular distribution of Arf proteins in mammalian cells: Arf6 is uniquely localized to the plasma membrane
    • Cavenagh MM, Whitney JA, Carroll K, et al. Intracellular distribution of Arf proteins in mammalian cells: Arf6 is uniquely localized to the plasma membrane. J Biol Chem. 1996;271:21767-21774.
    • (1996) J Biol Chem , vol.271 , pp. 21767-21774
    • Cavenagh, M.M.1    Whitney, J.A.2    Carroll, K.3
  • 41
    • 14044252159 scopus 로고    scopus 로고
    • G protein-coupled receptor endocytosis in ADP-ribosylation factor 6-depleted cells
    • Houndolo T, Boulay PL, Claing A. G protein-coupled receptor endocytosis in ADP-ribosylation factor 6-depleted cells. J Biol Chem. 2005;280:5598-5604.
    • (2005) J Biol Chem , vol.280 , pp. 5598-5604
    • Houndolo, T.1    Boulay, P.L.2    Claing, A.3
  • 43
    • 0033937941 scopus 로고    scopus 로고
    • Regulators and effectors of the ARF GTPases
    • Donaldson JG, Jackson CL. Regulators and effectors of the ARF GTPases. Curr Opin Cell Biol. 2000;12:475-482.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 475-482
    • Donaldson, J.G.1    Jackson, C.L.2
  • 45
    • 0033950864 scopus 로고    scopus 로고
    • Turning on ARF: The Sec7 family of guanine-nucleotide-exchange factors
    • Jackson CL, Casanova JE. Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors. Trends Cell Biol. 2000;10:60-67.
    • (2000) Trends Cell Biol , vol.10 , pp. 60-67
    • Jackson, C.L.1    Casanova, J.E.2
  • 46
    • 0023784561 scopus 로고
    • Interaction of fibrinogen with its platelet receptor: Differential effects of α and γ chain fibrinogen peptides on the glycoprotein IIb-IIIa complex
    • Bennett JS, Shattil SJ, Power JW, Gartner TK. Interaction of fibrinogen with its platelet receptor: differential effects of α and γ chain fibrinogen peptides on the glycoprotein IIb-IIIa complex. J Biol Chem. 1988;263:12948-12953.
    • (1988) J Biol Chem , vol.263 , pp. 12948-12953
    • Bennett, J.S.1    Shattil, S.J.2    Power, J.W.3    Gartner, T.K.4
  • 47
    • 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
  • 48
  • 49
    • 0035817625 scopus 로고    scopus 로고
    • Activation of ARF6 by ARNO stimulates epithelial cell migration through downstream activation of both Rac1 and phospholipase D
    • Santy LC, Casanova JE. Activation of ARF6 by ARNO stimulates epithelial cell migration through downstream activation of both Rac1 and phospholipase D. J Cell Biol. 2001;154:599-610.
    • (2001) J Cell Biol , vol.154 , pp. 599-610
    • Santy, L.C.1    Casanova, J.E.2
  • 50
    • 0034095215 scopus 로고    scopus 로고
    • ADP-ribosylation factor 6 regulates actin cytoskeleton remodeling in coordination with Rac1 and RhoA
    • Boshans RL, Szanto S, van Aelst L, D'Souza-Schorey C. ADP-ribosylation factor 6 regulates actin cytoskeleton remodeling in coordination with Rac1 and RhoA. Mol Cell Biol. 2000;20:3685-3694.
    • (2000) Mol Cell Biol , vol.20 , pp. 3685-3694
    • Boshans, R.L.1    Szanto, S.2    Van Aelst, L.3    D'Souza-Schorey, C.4
  • 51
    • 0020698663 scopus 로고
    • Latrunculins: Novel marine toxins that disrupt microfilament organization in cultured cells
    • Spector I, Shochet NR, Kashman Y, Groweiss A. Latrunculins: novel marine toxins that disrupt microfilament organization in cultured cells. Science. 1983;219:493-495.
    • (1983) Science , vol.219 , pp. 493-495
    • Spector, I.1    Shochet, N.R.2    Kashman, Y.3    Groweiss, A.4
  • 52
    • 0035040153 scopus 로고    scopus 로고
    • Cell migration: GAPs between membrane traffic and the cytoskeleton
    • de Curtis I. Cell migration: GAPs between membrane traffic and the cytoskeleton. EMBO Rep. 2001;2:277-281.
    • (2001) EMBO Rep , vol.2 , pp. 277-281
    • De Curtis, I.1
  • 53
    • 0038784752 scopus 로고    scopus 로고
    • Regulation of exocytosis in adrenal chromaffin cells: Focus on ARF and Rho GTPases
    • Gasman S, Chasserot-Golaz S, Bader MF, Vitale N. Regulation of exocytosis in adrenal chromaffin cells: focus on ARF and Rho GTPases. Cell Signal. 2003;15:893-899.
    • (2003) Cell Signal , vol.15 , pp. 893-899
    • Gasman, S.1    Chasserot-Golaz, S.2    Bader, M.F.3    Vitale, N.4
  • 54
    • 0037076462 scopus 로고    scopus 로고
    • GTPase signaling: Bridging the GAP between ARF and Rho
    • Santy LC, Casanova JE. GTPase signaling: bridging the GAP between ARF and Rho. Curr Biol. 2002;12:R360-R362.
    • (2002) Curr Biol , vol.12
    • Santy, L.C.1    Casanova, J.E.2
  • 55
    • 0037040864 scopus 로고    scopus 로고
    • DEF-1/ASAP1 is a GTPase-activating protein (GAP) for ARF1 that enhances cell motility through a GAP-dependent mechanism
    • Furman C, Short SM, Subramanian RR, Zetter BR, Roberts TM. DEF-1/ASAP1 is a GTPase-activating protein (GAP) for ARF1 that enhances cell motility through a GAP-dependent mechanism. J Biol Chem. 2002;277:7962-7969.
    • (2002) J Biol Chem , vol.277 , pp. 7962-7969
    • Furman, C.1    Short, S.M.2    Subramanian, R.R.3    Zetter, B.R.4    Roberts, T.M.5
  • 56
    • 3042549223 scopus 로고    scopus 로고
    • ICln, a novel integrin αIIbβ3-associated protein, functionally regulates platelet activation
    • Larkin D, Murphy D, Reilly DF, et al. ICln, a novel integrin αIIbβ3-associated protein, functionally regulates platelet activation. J Biol Chem. 2004;279:27286-27293.
    • (2004) J Biol Chem , vol.279 , pp. 27286-27293
    • Larkin, D.1    Murphy, D.2    Reilly, D.F.3
  • 57
    • 0036797590 scopus 로고    scopus 로고
    • Pepducin-based intervention of thrombin-receptor signaling and systemic platelet activation
    • Covic L, Misra M, Badar J, Singh C, Kuliopulos A. Pepducin-based intervention of thrombin-receptor signaling and systemic platelet activation. Nat Med. 2002;8:1161-1165.
    • (2002) Nat Med , vol.8 , pp. 1161-1165
    • Covic, L.1    Misra, M.2    Badar, J.3    Singh, C.4    Kuliopulos, A.5
  • 58
    • 0037040959 scopus 로고    scopus 로고
    • Selective in vivo inhibition of mitogen-activated protein kinase activation using cell-permeable peptides
    • Kelemen BR, Hsiao K, Goueli SA. Selective in vivo inhibition of mitogen-activated protein kinase activation using cell-permeable peptides. J Biol Chem. 2002;277:8741-8748.
    • (2002) J Biol Chem , vol.277 , pp. 8741-8748
    • Kelemen, B.R.1    Hsiao, K.2    Goueli, S.A.3
  • 59
    • 2342418629 scopus 로고    scopus 로고
    • Rho-family GTPases: It's not only Rac and Rho (and I like it)
    • Wennerberg K, Der CJ. Rho-family GTPases: it's not only Rac and Rho (and I like it). J Cell Sci. 2004;117:1301-1312.
    • (2004) J Cell Sci , vol.117 , pp. 1301-1312
    • Wennerberg, K.1    Der, C.J.2
  • 60
    • 0033601075 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation
    • Honda A, Nogami M, Yokozeki T, et al. Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation. Cell. 1999;99:521-532.
    • (1999) Cell , vol.99 , pp. 521-532
    • Honda, A.1    Nogami, M.2    Yokozeki, T.3
  • 61
    • 0029795963 scopus 로고    scopus 로고
    • Aluminum fluoride stimulates surface protrusions in cells overexpressing the ARF6 GTPase
    • Radhakrishna H, Klausner RD, Donaldson JG. Aluminum fluoride stimulates surface protrusions in cells overexpressing the ARF6 GTPase. J Cell Biol. 1996;134:935-947.
    • (1996) J Cell Biol , vol.134 , pp. 935-947
    • Radhakrishna, H.1    Klausner, R.D.2    Donaldson, J.G.3
  • 62
    • 0032900498 scopus 로고    scopus 로고
    • ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements
    • Radhakrishna H, Al-Awar O, Khachikian Z, Donaldson JG. ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements. J Cell Sci. 1999;112:855-866.
    • (1999) J Cell Sci , vol.112 , pp. 855-866
    • Radhakrishna, H.1    Al-Awar, O.2    Khachikian, Z.3    Donaldson, J.G.4
  • 63
    • 0030766987 scopus 로고    scopus 로고
    • A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytoskeletal rearrangements
    • D'Souza-Schorey C, Boshans RL, McDonough M, Stahl PD, Van Aelst L. A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytoskeletal rearrangements. EMBO J. 1997;16:5445-5454.
    • (1997) EMBO J , vol.16 , pp. 5445-5454
    • D'Souza-Schorey, C.1    Boshans, R.L.2    McDonough, M.3    Stahl, P.D.4    Van Aelst, L.5
  • 64
    • 0037201953 scopus 로고    scopus 로고
    • The regulation of phospholipase D by inositol phospholipids and small GTPases
    • Powner DJ, Wakelam MJ. The regulation of phospholipase D by inositol phospholipids and small GTPases. FEBS Lett. 2002;531:62-64.
    • (2002) FEBS Lett , vol.531 , pp. 62-64
    • Powner, D.J.1    Wakelam, M.J.2
  • 65
    • 0036227573 scopus 로고    scopus 로고
    • Antigen-stimulated activation of phospholipase D1b by Rac1, ARF6, and PKCα in RBL-2H3 cells
    • Powner DJ, Hodgkin MN, Wakelam MJ. Antigen-stimulated activation of phospholipase D1b by Rac1, ARF6, and PKCα in RBL-2H3 cells. Mol Biol Cell. 2002;13:1252-1262.
    • (2002) Mol Biol Cell , vol.13 , pp. 1252-1262
    • Powner, D.J.1    Hodgkin, M.N.2    Wakelam, M.J.3
  • 66
    • 0041475820 scopus 로고    scopus 로고
    • ARF6 regulates a plasma membrane pool of phosphatidylinositol(4,5) bisphosphate required for regulated exocytosis
    • Aikawa Y, Martin TF. ARF6 regulates a plasma membrane pool of phosphatidylinositol(4,5) bisphosphate required for regulated exocytosis. J Cell Biol. 2003;162:647-659.
    • (2003) J Cell Biol , vol.162 , pp. 647-659
    • Aikawa, Y.1    Martin, T.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.