메뉴 건너뛰기




Volumn 8, Issue 2, 2013, Pages

The Tandem PH Domain-Containing Protein 2 (TAPP2) Regulates Chemokine-Induced Cytoskeletal Reorganization and Malignant B Cell Migration

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CHEMOKINE; F ACTIN; MYOSIN II; PHOSPHATIDYLINOSITOL 3 KINASE; RAC PROTEIN; RHO FACTOR; STROMAL CELL DERIVED FACTOR 1; TANDEM PH DOMAIN CONTAINING PROTEIN 2; UNCLASSIFIED DRUG; UTROPHIN;

EID: 84874513447     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0057809     Document Type: Article
Times cited : (16)

References (44)
  • 1
    • 34247481994 scopus 로고    scopus 로고
    • The CXCR4 chemokine receptor in acute and chronic leukaemia: a marrow homing receptor and potential therapeutic target
    • Burger JA, Burkle A, (2007) The CXCR4 chemokine receptor in acute and chronic leukaemia: a marrow homing receptor and potential therapeutic target. Br J Haematol 137: 288-296.
    • (2007) Br J Haematol , vol.137 , pp. 288-296
    • Burger, J.A.1    Burkle, A.2
  • 2
    • 70350734809 scopus 로고    scopus 로고
    • The microenvironment in mature B-cell malignancies: a target for new treatment strategies
    • Burger JA, Ghia P, Rosenwald A, Caligaris-Cappio F, (2009) The microenvironment in mature B-cell malignancies: a target for new treatment strategies. Blood 114: 3367-3375.
    • (2009) Blood , vol.114 , pp. 3367-3375
    • Burger, J.A.1    Ghia, P.2    Rosenwald, A.3    Caligaris-Cappio, F.4
  • 3
    • 58149332686 scopus 로고    scopus 로고
    • Translating an Antagonist of Chemokine Receptor CXCR4: from bench to bedside
    • Wong D, Korz W, (2008) Translating an Antagonist of Chemokine Receptor CXCR4: from bench to bedside. Clin Cancer Res 14: 7975-7980.
    • (2008) Clin Cancer Res , vol.14 , pp. 7975-7980
    • Wong, D.1    Korz, W.2
  • 4
    • 77953090345 scopus 로고    scopus 로고
    • CXCL12 (SDF-1)/CXCR4 pathway in cancer
    • Teicher BA, Fricker SP, (2010) CXCL12 (SDF-1)/CXCR4 pathway in cancer. Clin Cancer Res 16: 2927-2931.
    • (2010) Clin Cancer Res , vol.16 , pp. 2927-2931
    • Teicher, B.A.1    Fricker, S.P.2
  • 5
    • 70349735988 scopus 로고    scopus 로고
    • Therapeutic targeting of microenvironmental interactions in leukemia: mechanisms and approaches
    • Konopleva M, Tabe Y, Zeng Z, Andreeff M, (2009) Therapeutic targeting of microenvironmental interactions in leukemia: mechanisms and approaches. Drug Resist Updat 12: 103-113.
    • (2009) Drug Resist Updat , vol.12 , pp. 103-113
    • Konopleva, M.1    Tabe, Y.2    Zeng, Z.3    Andreeff, M.4
  • 6
    • 67049137382 scopus 로고    scopus 로고
    • Isoform-selective phosphoinositide 3′-kinase inhibitors inhibit CXCR4 signaling and overcome stromal cell-mediated drug resistance in chronic lymphocytic leukemia: a novel therapeutic approach
    • Niedermeier M, Hennessy BT, Knight ZA, Henneberg M, Hu J, et al. (2009) Isoform-selective phosphoinositide 3′-kinase inhibitors inhibit CXCR4 signaling and overcome stromal cell-mediated drug resistance in chronic lymphocytic leukemia: a novel therapeutic approach. Blood 113: 5549-5557.
    • (2009) Blood , vol.113 , pp. 5549-5557
    • Niedermeier, M.1    Hennessy, B.T.2    Knight, Z.A.3    Henneberg, M.4    Hu, J.5
  • 7
    • 0038784379 scopus 로고    scopus 로고
    • CD40 induces human multiple myeloma cell migration via phosphatidylinositol 3-kinase/AKT/NF-kappa B signaling
    • Tai YT, Podar K, Mitsiades N, Lin B, Mitsiades C, et al. (2003) CD40 induces human multiple myeloma cell migration via phosphatidylinositol 3-kinase/AKT/NF-kappa B signaling. Blood 101: 2762-2769.
    • (2003) Blood , vol.101 , pp. 2762-2769
    • Tai, Y.T.1    Podar, K.2    Mitsiades, N.3    Lin, B.4    Mitsiades, C.5
  • 8
    • 69549096143 scopus 로고    scopus 로고
    • Cell biology of the movement of breast cancer cells: intracellular signalling and the actin cytoskeleton
    • Jiang P, Enomoto A, Takahashi M, (2009) Cell biology of the movement of breast cancer cells: intracellular signalling and the actin cytoskeleton. Cancer Lett 284: 122-130.
    • (2009) Cancer Lett , vol.284 , pp. 122-130
    • Jiang, P.1    Enomoto, A.2    Takahashi, M.3
  • 9
    • 84874196138 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase signaling pathway in normal and malignant B cells: activation mechanisms, regulation and impact on cellular functions
    • Pauls SD, Lafarge ST, Landego I, Zhang T, Marshall AJ, (2012) The phosphoinositide 3-kinase signaling pathway in normal and malignant B cells: activation mechanisms, regulation and impact on cellular functions. Front Immunol 3: 224.
    • (2012) Front Immunol , vol.3 , pp. 224
    • Pauls, S.D.1    Lafarge, S.T.2    Landego, I.3    Zhang, T.4    Marshall, A.J.5
  • 10
    • 58149395054 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinases in cell migration
    • Cain RJ, Ridley AJ, (2009) Phosphoinositide 3-kinases in cell migration. Biol Cell 101: 13-29.
    • (2009) Biol Cell , vol.101 , pp. 13-29
    • Cain, R.J.1    Ridley, A.J.2
  • 11
    • 0842346270 scopus 로고    scopus 로고
    • Do phosphoinositide 3-kinases direct lymphocyte navigation?
    • Ward SG, (2004) Do phosphoinositide 3-kinases direct lymphocyte navigation? Trends Immunol 25: 67-74.
    • (2004) Trends Immunol , vol.25 , pp. 67-74
    • Ward, S.G.1
  • 12
    • 77952911072 scopus 로고    scopus 로고
    • Eukaryotic chemotaxis: a network of signaling pathways controls motility, directional sensing, and polarity
    • Swaney KF, Huang CH, Devreotes PN, (2010) Eukaryotic chemotaxis: a network of signaling pathways controls motility, directional sensing, and polarity. Annu Rev Biophys 39: 265-289.
    • (2010) Annu Rev Biophys , vol.39 , pp. 265-289
    • Swaney, K.F.1    Huang, C.H.2    Devreotes, P.N.3
  • 13
    • 70350405643 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase-regulated adapters in lymphocyte activation
    • Zhang TT, Li H, Cheung SM, Costantini JL, Hou S, et al. (2009) Phosphoinositide 3-kinase-regulated adapters in lymphocyte activation. Immunol Rev 232: 255-272.
    • (2009) Immunol Rev , vol.232 , pp. 255-272
    • Zhang, T.T.1    Li, H.2    Cheung, S.M.3    Costantini, J.L.4    Hou, S.5
  • 14
    • 84867214110 scopus 로고    scopus 로고
    • Interaction of TAPP adapter proteins with phosphatidylinositol (3,4)-bisphosphate regulates B-cell activation and autoantibody production
    • Landego I, Jayachandran N, Wullschleger S, Zhang TT, Gibson IW, et al. (2012) Interaction of TAPP adapter proteins with phosphatidylinositol (3,4)-bisphosphate regulates B-cell activation and autoantibody production. Eur J Immunol.
    • (2012) Eur J Immunol.
    • Landego, I.1    Jayachandran, N.2    Wullschleger, S.3    Zhang, T.T.4    Gibson, I.W.5
  • 15
    • 0034306455 scopus 로고    scopus 로고
    • Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities
    • Dowler S, Currie RA, Campbell DG, Deak M, Kular G, et al. (2000) Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem J 351: 19-31.
    • (2000) Biochem J , vol.351 , pp. 19-31
    • Dowler, S.1    Currie, R.A.2    Campbell, D.G.3    Deak, M.4    Kular, G.5
  • 16
    • 0036310638 scopus 로고    scopus 로고
    • TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase signaling in B cells: sustained plasma membrane recruitment triggered by the B-cell antigen receptor
    • Marshall AJ, Krahn AK, Ma K, Duronio V, Hou S, (2002) TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase signaling in B cells: sustained plasma membrane recruitment triggered by the B-cell antigen receptor. Mol Cell Biol 22: 5479-5491.
    • (2002) Mol Cell Biol , vol.22 , pp. 5479-5491
    • Marshall, A.J.1    Krahn, A.K.2    Ma, K.3    Duronio, V.4    Hou, S.5
  • 17
    • 73949099919 scopus 로고    scopus 로고
    • TAPP2 links phosphoinositide 3-kinase signaling to B cell adhesion through interaction with the cytoskeletal protein utrophin: expression of a novel cell adhesion-promoting complex in B cell leukemia
    • Costantini JL, Cheung SM, Hou S, Li H, Kung SK, et al. (2009) TAPP2 links phosphoinositide 3-kinase signaling to B cell adhesion through interaction with the cytoskeletal protein utrophin: expression of a novel cell adhesion-promoting complex in B cell leukemia. Blood.
    • (2009) Blood
    • Costantini, J.L.1    Cheung, S.M.2    Hou, S.3    Li, H.4    Kung, S.K.5
  • 18
    • 33746589459 scopus 로고    scopus 로고
    • Clinical significance of ZAP-70 protein expression in B-cell chronic lymphocytic leukemia
    • Del Principe MI, Del Poeta G, Buccisano F, Maurillo L, Venditti A, et al. (2006) Clinical significance of ZAP-70 protein expression in B-cell chronic lymphocytic leukemia. Blood 108: 853-861.
    • (2006) Blood , vol.108 , pp. 853-861
    • Del Principe, M.I.1    Del Poeta, G.2    Buccisano, F.3    Maurillo, L.4    Venditti, A.5
  • 19
    • 33646433940 scopus 로고    scopus 로고
    • ZAP-70 expression is associated with enhanced ability to respond to migratory and survival signals in B-cell chronic lymphocytic leukemia (B-CLL)
    • Richardson SJ, Matthews C, Catherwood MA, Alexander HD, Carey BS, et al. (2006) ZAP-70 expression is associated with enhanced ability to respond to migratory and survival signals in B-cell chronic lymphocytic leukemia (B-CLL). Blood 107: 3584-3592.
    • (2006) Blood , vol.107 , pp. 3584-3592
    • Richardson, S.J.1    Matthews, C.2    Catherwood, M.A.3    Alexander, H.D.4    Carey, B.S.5
  • 20
    • 14844343641 scopus 로고    scopus 로고
    • Dystroglycan is involved in laminin-1-stimulated motility of Muller glial cells: combined velocity and directionality analysis
    • Mehes E, Czirok A, Hegedus B, Szabo B, Vicsek T, et al. (2005) Dystroglycan is involved in laminin-1-stimulated motility of Muller glial cells: combined velocity and directionality analysis. Glia 49: 492-500.
    • (2005) Glia , vol.49 , pp. 492-500
    • Mehes, E.1    Czirok, A.2    Hegedus, B.3    Szabo, B.4    Vicsek, T.5
  • 21
    • 76249109093 scopus 로고    scopus 로고
    • Differential regulation of protrusion and polarity by PI3K during neutrophil motility in live zebrafish
    • Yoo SK, Deng Q, Cavnar PJ, Wu YI, Hahn KM, et al. (2010) Differential regulation of protrusion and polarity by PI3K during neutrophil motility in live zebrafish. Dev Cell 18: 226-236.
    • (2010) Dev Cell , vol.18 , pp. 226-236
    • Yoo, S.K.1    Deng, Q.2    Cavnar, P.J.3    Wu, Y.I.4    Hahn, K.M.5
  • 22
    • 33745308103 scopus 로고    scopus 로고
    • PI3K and RAC signalling in leukocyte and cancer cell migration
    • Barber MA, Welch HC, (2006) PI3K and RAC signalling in leukocyte and cancer cell migration. Bull Cancer 93: E44-52.
    • (2006) Bull Cancer , vol.93
    • Barber, M.A.1    Welch, H.C.2
  • 23
    • 0025143240 scopus 로고
    • Functional characterization of two stromal cell lines that support B lymphopoiesis
    • Henderson AJ, Johnson A, Dorshkind K, (1990) Functional characterization of two stromal cell lines that support B lymphopoiesis. J Immunol 145: 423-428.
    • (1990) J Immunol , vol.145 , pp. 423-428
    • Henderson, A.J.1    Johnson, A.2    Dorshkind, K.3
  • 24
    • 73949091167 scopus 로고    scopus 로고
    • The pleckstrin homology domain adaptor protein Bam32/DAPP1 is required for germinal center progression
    • Zhang TT, Al-Alwan M, Marshall AJ, (2010) The pleckstrin homology domain adaptor protein Bam32/DAPP1 is required for germinal center progression. J Immunol 184: 164-172.
    • (2010) J Immunol , vol.184 , pp. 164-172
    • Zhang, T.T.1    Al-Alwan, M.2    Marshall, A.J.3
  • 25
    • 0033485625 scopus 로고    scopus 로고
    • Chronic lymphocytic leukemia B cells express functional CXCR4 chemokine receptors that mediate spontaneous migration beneath bone marrow stromal cells
    • Burger JA, Burger M, Kipps TJ, (1999) Chronic lymphocytic leukemia B cells express functional CXCR4 chemokine receptors that mediate spontaneous migration beneath bone marrow stromal cells. Blood 94: 3658-3667.
    • (1999) Blood , vol.94 , pp. 3658-3667
    • Burger, J.A.1    Burger, M.2    Kipps, T.J.3
  • 26
    • 33750476278 scopus 로고    scopus 로고
    • T cell chemotaxis in a simple microfluidic device
    • Lin F, Butcher EC, (2006) T cell chemotaxis in a simple microfluidic device. Lab Chip 6: 1462-1469.
    • (2006) Lab Chip , vol.6 , pp. 1462-1469
    • Lin, F.1    Butcher, E.C.2
  • 27
    • 33947288392 scopus 로고    scopus 로고
    • Regulation of phosphoinositide 3-kinase signaling by oxidants: hydrogen peroxide selectively enhances immunoreceptor-induced recruitment of phosphatidylinositol (3,4) bisphosphate-binding PH domain proteins
    • Cheung SM, Kornelson JC, Al-Alwan M, Marshall AJ, (2007) Regulation of phosphoinositide 3-kinase signaling by oxidants: hydrogen peroxide selectively enhances immunoreceptor-induced recruitment of phosphatidylinositol (3,4) bisphosphate-binding PH domain proteins. Cell Signal 19: 902-912.
    • (2007) Cell Signal , vol.19 , pp. 902-912
    • Cheung, S.M.1    Kornelson, J.C.2    Al-Alwan, M.3    Marshall, A.J.4
  • 28
    • 4544261701 scopus 로고    scopus 로고
    • The adaptor protein Bam32 regulates Rac1 activation and actin remodeling through a phosphorylation-dependent mechanism
    • Allam A, Niiro H, Clark EA, Marshall AJ, (2004) The adaptor protein Bam32 regulates Rac1 activation and actin remodeling through a phosphorylation-dependent mechanism. J Biol Chem 279: 39775-39782.
    • (2004) J Biol Chem , vol.279 , pp. 39775-39782
    • Allam, A.1    Niiro, H.2    Clark, E.A.3    Marshall, A.J.4
  • 29
    • 35649027944 scopus 로고    scopus 로고
    • Versatile fluorescent probes for actin filaments based on the actin-binding domain of utrophin
    • Burkel BM, von Dassow G, Bement WM, (2007) Versatile fluorescent probes for actin filaments based on the actin-binding domain of utrophin. Cell Motil Cytoskeleton 64: 822-832.
    • (2007) Cell Motil Cytoskeleton , vol.64 , pp. 822-832
    • Burkel, B.M.1    von Dassow, G.2    Bement, W.M.3
  • 30
    • 11144234519 scopus 로고    scopus 로고
    • The phosphoinositol 3,4-bisphosphate-binding protein TAPP1 interacts with syntrophins and regulates actin cytoskeletal organization
    • Hogan A, Yakubchyk Y, Chabot J, Obagi C, Daher E, et al. (2004) The phosphoinositol 3,4-bisphosphate-binding protein TAPP1 interacts with syntrophins and regulates actin cytoskeletal organization. J Biol Chem 279: 53717-53724.
    • (2004) J Biol Chem , vol.279 , pp. 53717-53724
    • Hogan, A.1    Yakubchyk, Y.2    Chabot, J.3    Obagi, C.4    Daher, E.5
  • 31
    • 54249122300 scopus 로고    scopus 로고
    • The PCH family member proline-serine-threonine phosphatase-interacting protein 1 targets to the leukocyte uropod and regulates directed cell migration
    • Cooper KM, Bennin DA, Huttenlocher A, (2008) The PCH family member proline-serine-threonine phosphatase-interacting protein 1 targets to the leukocyte uropod and regulates directed cell migration. Mol Biol Cell 19: 3180-3191.
    • (2008) Mol Biol Cell , vol.19 , pp. 3180-3191
    • Cooper, K.M.1    Bennin, D.A.2    Huttenlocher, A.3
  • 32
    • 24644441368 scopus 로고    scopus 로고
    • The comings and goings of actin: coupling protrusion and retraction in cell motility
    • 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.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 517-523
    • Small, J.V.1    Resch, G.P.2
  • 33
    • 0027299745 scopus 로고
    • On the crawling of animal cells
    • Stossel TP, (1993) On the crawling of animal cells. Science 260: 1086-1094.
    • (1993) Science , vol.260 , pp. 1086-1094
    • Stossel, T.P.1
  • 34
    • 0034093830 scopus 로고    scopus 로고
    • Effects of the chemokine stromal cell-derived factor-1 on the migration and localization of precursor-B acute lymphoblastic leukemia cells within bone marrow stromal layers
    • Bradstock KF, Makrynikola V, Bianchi A, Shen W, Hewson J, et al. (2000) Effects of the chemokine stromal cell-derived factor-1 on the migration and localization of precursor-B acute lymphoblastic leukemia cells within bone marrow stromal layers. Leukemia 14: 882-888.
    • (2000) Leukemia , vol.14 , pp. 882-888
    • Bradstock, K.F.1    Makrynikola, V.2    Bianchi, A.3    Shen, W.4    Hewson, J.5
  • 35
    • 57349126275 scopus 로고    scopus 로고
    • Rapid turnover rate of phosphoinositides at the front of migrating MDCK cells
    • Nishioka T, Aoki K, Hikake K, Yoshizaki H, Kiyokawa E, et al. (2008) Rapid turnover rate of phosphoinositides at the front of migrating MDCK cells. Mol Biol Cell 19: 4213-4223.
    • (2008) Mol Biol Cell , vol.19 , pp. 4213-4223
    • Nishioka, T.1    Aoki, K.2    Hikake, K.3    Yoshizaki, H.4    Kiyokawa, E.5
  • 36
    • 0042354714 scopus 로고    scopus 로고
    • Divergent signals and cytoskeletal assemblies regulate self-organizing polarity in neutrophils
    • Xu J, Wang F, Van Keymeulen A, Herzmark P, Straight A, et al. (2003) Divergent signals and cytoskeletal assemblies regulate self-organizing polarity in neutrophils. Cell 114: 201-214.
    • (2003) Cell , vol.114 , pp. 201-214
    • Xu, J.1    Wang, F.2    Van Keymeulen, A.3    Herzmark, P.4    Straight, A.5
  • 37
    • 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
  • 39
    • 33747383933 scopus 로고    scopus 로고
    • Role of dystrophin and utrophin for assembly and function of the dystrophin glycoprotein complex in non-muscle tissue
    • Haenggi T, Fritschy JM, (2006) Role of dystrophin and utrophin for assembly and function of the dystrophin glycoprotein complex in non-muscle tissue. Cell Mol Life Sci 63: 1614-1631.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1614-1631
    • Haenggi, T.1    Fritschy, J.M.2
  • 40
    • 34247507672 scopus 로고    scopus 로고
    • Processing and assembly of the dystrophin glycoprotein complex
    • Allikian MJ, McNally EM, (2007) Processing and assembly of the dystrophin glycoprotein complex. Traffic 8: 177-183.
    • (2007) Traffic , vol.8 , pp. 177-183
    • Allikian, M.J.1    McNally, E.M.2
  • 41
    • 79955516270 scopus 로고    scopus 로고
    • Myosin IIA/IIB restrict adhesive and protrusive signaling to generate front-back polarity in migrating cells
    • Vicente-Manzanares M, Newell-Litwa K, Bachir AI, Whitmore LA, Horwitz AR, (2011) Myosin IIA/IIB restrict adhesive and protrusive signaling to generate front-back polarity in migrating cells. J Cell Biol 193: 381-396.
    • (2011) J Cell Biol , vol.193 , pp. 381-396
    • Vicente-Manzanares, M.1    Newell-Litwa, K.2    Bachir, A.I.3    Whitmore, L.A.4    Horwitz, A.R.5
  • 42
    • 0032475863 scopus 로고    scopus 로고
    • G protein signaling events are activated at the leading edge of chemotactic cells
    • Parent CA, Blacklock BJ, Froehlich WM, Murphy DB, Devreotes PN, (1998) G protein signaling events are activated at the leading edge of chemotactic cells. Cell 95: 81-91.
    • (1998) Cell , vol.95 , pp. 81-91
    • Parent, C.A.1    Blacklock, B.J.2    Froehlich, W.M.3    Murphy, D.B.4    Devreotes, P.N.5
  • 43
    • 13544249968 scopus 로고    scopus 로고
    • In vivo analysis of 3-phosphoinositide dynamics during Dictyostelium phagocytosis and chemotaxis
    • Dormann D, Weijer G, Dowler S, Weijer CJ, (2004) In vivo analysis of 3-phosphoinositide dynamics during Dictyostelium phagocytosis and chemotaxis. J Cell Sci 117: 6497-6509.
    • (2004) J Cell Sci , vol.117 , pp. 6497-6509
    • Dormann, D.1    Weijer, G.2    Dowler, S.3    Weijer, C.J.4
  • 44
    • 79955366131 scopus 로고    scopus 로고
    • PI3K and chemotaxis: a priming issue?
    • Afonso PV, Parent CA, (2011) PI3K and chemotaxis: a priming issue? Sci Signal 4: pe22.
    • (2011) Sci Signal , vol.4
    • Afonso, P.V.1    Parent, C.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.