메뉴 건너뛰기




Volumn 289, Issue 8, 2014, Pages 5051-5060

Dok-2 adaptor protein regulates the shear-dependent adhesive function of platelet integrinαIIbβ3 in mice

Author keywords

[No Author keywords available]

Indexed keywords

ADHESION; ADHESIVES; MAMMALS; PROTEINS;

EID: 84894471945     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.520148     Document Type: Article
Times cited : (14)

References (54)
  • 1
    • 0036851876 scopus 로고    scopus 로고
    • Platelets in atherothrombosis
    • Ruggeri, Z. M. (2002) Platelets in atherothrombosis. Nat. Med. 8, 1227-1234
    • (2002) Nat. Med. , vol.8 , pp. 1227-1234
    • Ruggeri, Z.M.1
  • 2
    • 0037271306 scopus 로고    scopus 로고
    • Scientific and therapeutic advances in antiplatelet therapy
    • Bhatt, D. L., and Topol, E. J. (2003) Scientific and therapeutic advances in antiplatelet therapy. Nat. Rev. Drug Discov. 2, 15-28
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 15-28
    • Bhatt, D.L.1    Topol, E.J.2
  • 3
    • 0242300217 scopus 로고    scopus 로고
    • Antiplatelet therapy. in search of the "magic bullet"
    • Jackson, S. P., and Schoenwaelder, S. M. (2003) Antiplatelet therapy. In search of the "magic bullet". Nat. Rev. Drug Discov. 2, 775-789
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 775-789
    • Jackson, S.P.1    Schoenwaelder, S.M.2
  • 5
    • 54049152026 scopus 로고    scopus 로고
    • The GPIIb/IIIa (integrin IIb3) odyssey. A technology-driven saga of a receptor with twists, turns, and even a bend
    • Coller, B. S., and Shattil, S. J. (2008) The GPIIb/IIIa (integrin IIb3) odyssey. A technology-driven saga of a receptor with twists, turns, and even a bend. Blood 112, 3011-3025
    • (2008) Blood , vol.112 , pp. 3011-3025
    • Coller, B.S.1    Shattil, S.J.2
  • 7
    • 4444264392 scopus 로고    scopus 로고
    • Integrins. Dynamic scaffolds for adhesion and signaling in platelets
    • Shattil, S. J., and Newman, P. J. (2004) Integrins. Dynamic scaffolds for adhesion and signaling in platelets. Blood 104, 1606-1615
    • (2004) Blood , vol.104 , pp. 1606-1615
    • Shattil, S.J.1    Newman, P.J.2
  • 9
    • 0034029126 scopus 로고    scopus 로고
    • Dok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signaling
    • Lemay, S., Davidson, D., Latour, S., and Veillette, A. (2000) Dok-3, a novel adapter molecule involved in the negative regulation of immunoreceptor signaling. Mol. Cell. Biol. 20, 2743-2754
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2743-2754
    • Lemay, S.1    Davidson, D.2    Latour, S.3    Veillette, A.4
  • 10
    • 0037816152 scopus 로고    scopus 로고
    • Two new substrates in insulin signaling, IRS5/DOK4 and IRS6/ DOK5
    • Cai, D., Dhe-Paganon, S., Melendez, P. A., Lee, J., and Shoelson, S. E. (2003) Two new substrates in insulin signaling, IRS5/DOK4 and IRS6/ DOK5. J. Biol. Chem. 278, 25323-25330
    • (2003) J. Biol. Chem. , vol.278 , pp. 25323-25330
    • Cai, D.1    Dhe-Paganon, S.2    Melendez, P.A.3    Lee, J.4    Shoelson, S.E.5
  • 11
    • 0031459864 scopus 로고    scopus 로고
    • P62(dok). A constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells
    • Carpino, N., Wisniewski, D., Strife, A., Marshak, D., Kobayashi, R., Stillman, B., and Clarkson, B. (1997) p62(dok). A constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells. Cell 88, 197-204
    • (1997) Cell , vol.88 , pp. 197-204
    • Carpino, N.1    Wisniewski, D.2    Strife, A.3    Marshak, D.4    Kobayashi, R.5    Stillman, B.6    Clarkson, B.7
  • 12
    • 0035939661 scopus 로고    scopus 로고
    • Novel p62dok family members, dok-4 and dok-5, are substrates of the c-Ret receptor tyrosine kinase and mediate neuronal differentiation
    • Grimm, J., Sachs, M., Britsch, S., Di Cesare, S., Schwarz-Romond, T., Alitalo, K., and Birchmeier, W. (2001) Novel p62dok family members, dok-4 and dok-5, are substrates of the c-Ret receptor tyrosine kinase and mediate neuronal differentiation. J. Cell Biol. 154, 345-354
    • (2001) J. Cell Biol. , vol.154 , pp. 345-354
    • Grimm, J.1    Sachs, M.2    Britsch, S.3    Di Cesare, S.4    Schwarz-Romond, T.5    Alitalo, K.6    Birchmeier, W.7
  • 16
    • 33846419172 scopus 로고    scopus 로고
    • Differential regulation of adapter proteins Dok2 and Dok1 in platelets, leading to an association of Dok2 with integrin IIb3
    • Hughan, S. C., and Watson, S. P. (2007) Differential regulation of adapter proteins Dok2 and Dok1 in platelets, leading to an association of Dok2 with integrin IIb3. J. Thromb. Haemost. 5, 387-394
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 387-394
    • Hughan, S.C.1    Watson, S.P.2
  • 17
    • 70350015034 scopus 로고    scopus 로고
    • Proteomic analysis of integrin IIb3 outside-in signaling reveals Src-kinase-independent phosphorylation of Dok-1 and Dok-3 leading to SHIP-1 interactions
    • Senis, Y. A., Antrobus, R., Severin, S., Parguiña, A. F., Rosa, I., Zitzmann, N., Watson, S. P., and García, A. (2009) Proteomic analysis of integrin IIb3 outside-in signaling reveals Src-kinase-independent phosphorylation of Dok-1 and Dok-3 leading to SHIP-1 interactions. J. Thromb. Haemost. 7, 1718-1726
    • (2009) J. Thromb. Haemost. , vol.7 , pp. 1718-1726
    • Senis, Y.A.1    Antrobus, R.2    Severin, S.3    Parguiña, A.F.4    Rosa, I.5    Zitzmann, N.6    Watson, S.P.7    García, A.8
  • 18
    • 2442458850 scopus 로고    scopus 로고
    • Pleckstrin homology and phosphotyrosine-binding domain-dependent membrane association and tyrosine phosphorylation of Dok-4, an inhibitory adapter molecule expressed in epithelial cells
    • Bedirian, A., Baldwin, C., Abe, J., Takano, T., and Lemay, S. (2004) Pleckstrin homology and phosphotyrosine-binding domain-dependent membrane association and tyrosine phosphorylation of Dok-4, an inhibitory adapter molecule expressed in epithelial cells. J. Biol. Chem. 279, 19335-19349
    • (2004) J. Biol. Chem. , vol.279 , pp. 19335-19349
    • Bedirian, A.1    Baldwin, C.2    Abe, J.3    Takano, T.4    Lemay, S.5
  • 22
    • 0033979324 scopus 로고    scopus 로고
    • Role of the rasGAP-associated docking protein p62(dok) in negative regulation of B cell receptor-mediated signaling
    • Yamanashi, Y., Tamura, T., Kanamori, T., Yamane, H., Nariuchi, H., Yamamoto, T., and Baltimore, D. (2000) Role of the rasGAP-associated docking protein p62(dok) in negative regulation of B cell receptor-mediated signaling. Genes Dev. 14, 11-16
    • (2000) Genes Dev. , vol.14 , pp. 11-16
    • Yamanashi, Y.1    Tamura, T.2    Kanamori, T.3    Yamane, H.4    Nariuchi, H.5    Yamamoto, T.6    Baltimore, D.7
  • 25
    • 33645221824 scopus 로고    scopus 로고
    • Dok-1 independently attenuates Ras/mitogen-activated protein kinase and Src/c-myc pathways to inhibit platelet-derived growth factor-induced mitogenesis
    • Zhao, M., Janas, J. A., Niki, M., Pandolfi, P. P., and Van Aelst, L. (2006) Dok-1 independently attenuates Ras/mitogen-activated protein kinase and Src/c-myc pathways to inhibit platelet-derived growth factor-induced mitogenesis. Mol. Cell. Biol. 26, 2479-2489
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2479-2489
    • Zhao, M.1    Janas, J.A.2    Niki, M.3    Pandolfi, P.P.4    Van Aelst, L.5
  • 26
    • 33846240313 scopus 로고    scopus 로고
    • Identification of a 2-stage platelet aggregation process mediating shear-dependent thrombus formation
    • Maxwell, M. J., Westein, E., Nesbitt, W. S., Giuliano, S., Dopheide, S. M., and Jackson, S. P. (2007) Identification of a 2-stage platelet aggregation process mediating shear-dependent thrombus formation. Blood 109, 566-576
    • (2007) Blood , vol.109 , pp. 566-576
    • Maxwell, M.J.1    Westein, E.2    Nesbitt, W.S.3    Giuliano, S.4    Dopheide, S.M.5    Jackson, S.P.6
  • 28
    • 30144444264 scopus 로고    scopus 로고
    • Adaptation of the Folts and electrolytic methods of arterial thrombosis for the study of anti-thrombotic molecules in small animals
    • Sturgeon, S. A., Jones, C., Angus, J. A., and Wright, C. E. (2006) Adaptation of the Folts and electrolytic methods of arterial thrombosis for the study of anti-thrombotic molecules in small animals. J. Pharmacol. Toxicol. Methods 53, 20-29
    • (2006) J. Pharmacol. Toxicol. Methods , vol.53 , pp. 20-29
    • Sturgeon, S.A.1    Jones, C.2    Angus, J.A.3    Wright, C.E.4
  • 29
    • 0028784215 scopus 로고
    • Multiple defects in the immune system of Lyn-deficient mice, culminating in autoimmune disease
    • Hibbs, M. L., Tarlinton, D. M., Armes, J., Grail, D., Hodgson, G., Maglitto, R., Stacker, S. A., and Dunn, A. R. (1995) Multiple defects in the immune system of Lyn-deficient mice, culminating in autoimmune disease. Cell 83, 301-311
    • (1995) Cell , vol.83 , pp. 301-311
    • Hibbs, M.L.1    Tarlinton, D.M.2    Armes, J.3    Grail, D.4    Hodgson, G.5    Maglitto, R.6    Stacker, S.A.7    Dunn, A.R.8
  • 30
    • 3543010757 scopus 로고    scopus 로고
    • SHIP1 and Lyn kinase negatively regulate integrin IIb 3 signaling in platelets
    • Maxwell, M. J., Yuan, Y., Anderson, K. E., Hibbs, M. L., Salem, H. H., and Jackson, S. P. (2004) SHIP1 and Lyn kinase negatively regulate integrin IIb 3 signaling in platelets. J. Biol. Chem. 279, 32196-32204
    • (2004) J. Biol. Chem. , vol.279 , pp. 32196-32204
    • Maxwell, M.J.1    Yuan, Y.2    Anderson, K.E.3    Hibbs, M.L.4    Salem, H.H.5    Jackson, S.P.6
  • 31
    • 0041816451 scopus 로고    scopus 로고
    • Integrin IIb 3-dependent calcium signals regulate platelet-fibrinogen interactions under flow. Involvement of phospholipase C2
    • Goncalves, I., Hughan, S. C., Schoenwaelder, S. M., Yap, C. L., Yuan, Y., and Jackson, S. P. (2003) Integrin IIb 3-dependent calcium signals regulate platelet-fibrinogen interactions under flow. Involvement of phospholipase C 2. J. Biol. Chem. 278, 34812-34822
    • (2003) J. Biol. Chem. , vol.278 , pp. 34812-34822
    • Goncalves, I.1    Hughan, S.C.2    Schoenwaelder, S.M.3    Yap, C.L.4    Yuan, Y.5    Jackson, S.P.6
  • 32
    • 0036090365 scopus 로고    scopus 로고
    • Shear-dependent tether formation during platelet translocation on von Willebrand factor
    • Dopheide, S. M., Maxwell, M. J., and Jackson, S. P. (2002) Shear-dependent tether formation during platelet translocation on von Willebrand factor. Blood 99, 159-167
    • (2002) Blood , vol.99 , pp. 159-167
    • Dopheide, S.M.1    Maxwell, M.J.2    Jackson, S.P.3
  • 33
    • 0034742636 scopus 로고    scopus 로고
    • 3 tyrosine phosphorylation in IIb3 (platelet membrane GP IIb-IIIa) outside-in integrin signaling
    • Phillips, D. R., Nannizzi-Alaimo, L., and Prasad, K. S. (2001) 3 tyrosine phosphorylation in IIb3 (platelet membrane GP IIb-IIIa) outside-in integrin signaling. Thromb. Haemost. 86, 246-258
    • (2001) Thromb. Haemost. , vol.86 , pp. 246-258
    • Phillips, D.R.1    Nannizzi-Alaimo, L.2    Prasad, K.S.3
  • 34
    • 13344295095 scopus 로고    scopus 로고
    • Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor
    • Savage, B., Saldívar, E., and Ruggeri, Z. M. (1996) Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor. Cell 84, 289-297
    • (1996) Cell , vol.84 , pp. 289-297
    • Savage, B.1    Saldívar, E.2    Ruggeri, Z.M.3
  • 35
    • 33750530393 scopus 로고    scopus 로고
    • Tcell receptor for antigen induces linker for activation of T cell-dependent activation of a negative signaling complex involving Dok-2, SHIP-1, and Grb-2
    • Dong, S., Corre, B., Foulon, E., Dufour, E., Veillette, A., Acuto, O., and Michel, F. (2006)Tcell receptor for antigen induces linker for activation of T cell-dependent activation of a negative signaling complex involving Dok-2, SHIP-1, and Grb-2. J. Exp. Med. 203, 2509-2518
    • (2006) J. Exp. Med. , vol.203 , pp. 2509-2518
    • Dong, S.1    Corre, B.2    Foulon, E.3    Dufour, E.4    Veillette, A.5    Acuto, O.6    Michel, F.7
  • 36
    • 0033529502 scopus 로고    scopus 로고
    • Independent SH2-binding sites mediate interaction of Dok-related protein with RasGTPase-activating protein and Nck
    • Lock, P., Casagranda, F., and Dunn, A. R. (1999) Independent SH2-binding sites mediate interaction of Dok-related protein with RasGTPase-activating protein and Nck. J. Biol. Chem. 274, 22775-22784
    • (1999) J. Biol. Chem. , vol.274 , pp. 22775-22784
    • Lock, P.1    Casagranda, F.2    Dunn, A.R.3
  • 37
    • 70350406465 scopus 로고    scopus 로고
    • The roles of Dok family adapters in immunoreceptor signaling
    • Mashima, R., Hishida, Y., Tezuka, T., and Yamanashi, Y. (2009) The roles of Dok family adapters in immunoreceptor signaling. Immunol. Rev. 232, 273-285
    • (2009) Immunol. Rev. , vol.232 , pp. 273-285
    • Mashima, R.1    Hishida, Y.2    Tezuka, T.3    Yamanashi, Y.4
  • 38
    • 84858865586 scopus 로고    scopus 로고
    • The inositol 5-phosphatase SHIP-1 and adaptors Dok-1 and 2 play central roles in CD4-mediated inhibitory signaling
    • Waterman, P. M., Marschner, S., Brandl, E., and Cambier, J. C. (2012) The inositol 5-phosphatase SHIP-1 and adaptors Dok-1 and 2 play central roles in CD4-mediated inhibitory signaling. Immunol. Lett. 143, 122-130
    • (2012) Immunol. Lett. , vol.143 , pp. 122-130
    • Waterman, P.M.1    Marschner, S.2    Brandl, E.3    Cambier, J.C.4
  • 44
    • 34347407347 scopus 로고    scopus 로고
    • Dok-3 plays a nonredundant role in negative regulation of B-cell activation
    • Ng, C. H., Xu, S., and Lam, K. P. (2007) Dok-3 plays a nonredundant role in negative regulation of B-cell activation. Blood 110, 259-266
    • (2007) Blood , vol.110 , pp. 259-266
    • Ng, C.H.1    Xu, S.2    Lam, K.P.3
  • 45
    • 33847240085 scopus 로고    scopus 로고
    • Subcellular localization of Grb2 by the adaptor protein Dok-3 restricts the intensity of Ca2+ signaling in B cells
    • Stork, B., Neumann, K., Goldbeck, I., Alers, S., Kähne, T., Naumann, M., Engelke, M., and Wienands, J. (2007) Subcellular localization of Grb2 by the adaptor protein Dok-3 restricts the intensity of Ca2+ signaling in B cells. EMBO J. 26, 1140-1149
    • (2007) EMBO J. , vol.26 , pp. 1140-1149
    • Stork, B.1    Neumann, K.2    Goldbeck, I.3    Alers, S.4    Kähne, T.5    Naumann, M.6    Engelke, M.7    Wienands, J.8
  • 46
    • 0037255263 scopus 로고    scopus 로고
    • Dok protein family members are involved in signaling mediated by the type 1 Fc receptor
    • Abramson, J., Rozenblum, G., and Pecht, I. (2003) Dok protein family members are involved in signaling mediated by the type 1 Fc receptor. Eur. J. Immunol. 33, 85-91
    • (2003) Eur. J. Immunol. , vol.33 , pp. 85-91
    • Abramson, J.1    Rozenblum, G.2    Pecht, I.3
  • 47
    • 0035367576 scopus 로고    scopus 로고
    • Proximal protein tyrosine kinases in immunoreceptor signaling
    • Latour, S., and Veillette, A. (2001) Proximal protein tyrosine kinases in immunoreceptor signaling. Curr. Opin. Immunol. 13, 299-306
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 299-306
    • Latour, S.1    Veillette, A.2
  • 48
    • 0034672357 scopus 로고    scopus 로고
    • Fyn and Lyn phosphorylate the Fc receptor chain downstream of glycoprotein VI in murine platelets, and Lyn regulates a novel feedback pathway
    • Quek, L. S., Pasquet, J. M., Hers, I., Cornall, R., Knight, G., Barnes, M., Hibbs, M. L., Dunn, A. R., Lowell, C. A., and Watson, S. P. (2000) Fyn and Lyn phosphorylate the Fc receptor chain downstream of glycoprotein VI in murine platelets, and Lyn regulates a novel feedback pathway. Blood 96, 4246-4253
    • (2000) Blood , vol.96 , pp. 4246-4253
    • Quek, L.S.1    Pasquet, J.M.2    Hers, I.3    Cornall, R.4    Knight, G.5    Barnes, M.6    Hibbs, M.L.7    Dunn, A.R.8    Lowell, C.A.9    Watson, S.P.10
  • 50
    • 0037108442 scopus 로고    scopus 로고
    • Sequential cytoplasmic calcium signals in a 2-stage platelet activation process induced by the glycoprotein i mechanoreceptor
    • Mazzucato, M., Pradella, P., Cozzi, M. R., De Marco, L., and Ruggeri, Z. M. (2002) Sequential cytoplasmic calcium signals in a 2-stage platelet activation process induced by the glycoprotein I mechanoreceptor. Blood 100, 2793-2800
    • (2002) Blood , vol.100 , pp. 2793-2800
    • Mazzucato, M.1    Pradella, P.2    Cozzi, M.R.3    De Marco, L.4    Ruggeri, Z.M.5
  • 51
    • 4744362161 scopus 로고    scopus 로고
    • Disabled-2 is a negative regulator of integrin (IIb)(3)-mediated fibrinogen adhesion and cell signaling
    • Huang, C. L., Cheng, J. C., Liao, C. H., Stern, A., Hsieh, J. T., Wang, C. H., Hsu, H. L., and Tseng, C. P. (2004) Disabled-2 is a negative regulator of integrin (IIb)(3)-mediated fibrinogen adhesion and cell signaling. J. Biol. Chem. 279, 42279-42289
    • (2004) J. Biol. Chem. , vol.279 , pp. 42279-42289
    • Huang, C.L.1    Cheng, J.C.2    Liao, C.H.3    Stern, A.4    Hsieh, J.T.5    Wang, C.H.6    Hsu, H.L.7    Tseng, C.P.8
  • 53
    • 77950453194 scopus 로고    scopus 로고
    • Role forADAPin shear flow-induced platelet mechanotransduction
    • Kasirer-Friede, A., Ruggeri, Z. M., and Shattil, S. J. (2010) Role forADAPin shear flow-induced platelet mechanotransduction. Blood 115, 2274-2282
    • (2010) Blood , vol.115 , pp. 2274-2282
    • Kasirer-Friede, A.1    Ruggeri, Z.M.2    Shattil, S.J.3
  • 54
    • 0041328292 scopus 로고    scopus 로고
    • Platelets as predictors of vascular risk. Is there a practical index of platelet activity?
    • Tsiara, S., Elisaf, M., Jagroop, I. A., and Mikhailidis, D. P. (2003) Platelets as predictors of vascular risk. Is there a practical index of platelet activity? Clin. Appl. Thromb. Hemost. 9, 177-190
    • (2003) Clin. Appl. Thromb. Hemost. , vol.9 , pp. 177-190
    • Tsiara, S.1    Elisaf, M.2    Jagroop, I.A.3    Mikhailidis, D.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.