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Volumn 5, Issue 8, 2010, Pages

Filamin a binds to CCR2B and regulates its internalization

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; BETA ARRESTIN 2; CHEMOKINE RECEPTOR CCR2; CHEMOKINE RECEPTOR CCR2B; FILAMIN A; MONOCYTE CHEMOTACTIC PROTEIN 1; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; ACTIN; BETA ARRESTIN; CONTRACTILE PROTEIN; FILAMINS; RETINA S ANTIGEN;

EID: 77957865152     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0012212     Document Type: Article
Times cited : (22)

References (38)
  • 1
    • 50049123401 scopus 로고    scopus 로고
    • Chemokines and leukocyte traffic
    • Sallusto F, Baggiolini M (2008) Chemokines and leukocyte traffic. Nat Immunol 9: 949-952.
    • (2008) Nat Immunol , vol.9 , pp. 949-952
    • Sallusto, F.1    Baggiolini, M.2
  • 2
    • 38949205852 scopus 로고    scopus 로고
    • Chemokines and cancer: Migration, intracellular signalling and intercellular communication in the microenvironment
    • O'Hayre M, Salanga CL, Handel TM, Allen SJ (2008) Chemokines and cancer: migration, intracellular signalling and intercellular communication in the microenvironment. Biochem J 409: 635-649.
    • (2008) Biochem J , vol.409 , pp. 635-649
    • O'Hayre, M.1    Salanga, C.L.2    Handel, T.M.3    Allen, S.J.4
  • 3
    • 50049102160 scopus 로고    scopus 로고
    • How chemokines invite leukocytes to dance
    • Thelen M, Stein JV (2008) How chemokines invite leukocytes to dance. Nat Immunol 9: 953-959.
    • (2008) Nat Immunol , vol.9 , pp. 953-959
    • Thelen, M.1    Stein, J.V.2
  • 4
    • 33845412884 scopus 로고    scopus 로고
    • GRKs and arrestins: Regulators of migration and inflammation
    • Vroon A, Heijnen CJ, Kavelaars A (2006) GRKs and arrestins: regulators of migration and inflammation. J Leukoc Biol 80: 1214-1221.
    • (2006) J Leukoc Biol , vol.80 , pp. 1214-1221
    • Vroon, A.1    Heijnen, C.J.2    Kavelaars, A.3
  • 5
    • 0030589242 scopus 로고    scopus 로고
    • Phosphorylation by a G protein-coupled kinase inhibits signaling and promotes internalization of the monocyte chemoattractant protein-1 receptor. Critical role of carboxyl-tail serines/threonines in receptor function
    • Franci C, Gosling J, Tsou CL, Coughlin SR, Charo IF (1996) Phosphorylation by a G protein-coupled kinase inhibits signaling and promotes internalization of the monocyte chemoattractant protein-1 receptor. Critical role of carboxyl-tail serines/threonines in receptor function. J Immunol 157: 5606-5612.
    • (1996) J Immunol , vol.157 , pp. 5606-5612
    • Franci, C.1    Gosling, J.2    Tsou, C.L.3    Coughlin, S.R.4    Charo, I.F.5
  • 6
    • 0031747997 scopus 로고    scopus 로고
    • The role of receptor kinases and arrestins in G protein-coupled receptor regulation
    • Krupnick JG, Benovic JL (1998) The role of receptor kinases and arrestins in G protein-coupled receptor regulation. Annu Rev Pharmacol Toxicol 38: 289-319.
    • (1998) Annu Rev Pharmacol Toxicol , vol.38 , pp. 289-319
    • Krupnick, J.G.1    Benovic, J.L.2
  • 7
    • 0032539904 scopus 로고    scopus 로고
    • Monocyte chemoattractant protein-1-induced CCR2B receptor desensitization mediated by the G protein-coupled receptor kinase 2
    • Aragay AM, Mellado M, Frade JM, Martin AM, Jimenez-Sainz MC, et al. (1998) Monocyte chemoattractant protein-1-induced CCR2B receptor desensitization mediated by the G protein-coupled receptor kinase 2. Proc Natl Acad Sci U S A 95: 2985-2990.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 2985-2990
    • Aragay, A.M.1    Mellado, M.2    Frade, J.M.3    Martin, A.M.4    Jimenez-Sainz, M.C.5
  • 8
    • 2342519446 scopus 로고    scopus 로고
    • Reduced GRK2 level in T cells potentiates chemotaxis and signaling in response to CCL4
    • Vroon A, Heijnen CJ, Lombardi MS, Cobelens PM, Mayor F, Jr., et al. (2004) Reduced GRK2 level in T cells potentiates chemotaxis and signaling in response to CCL4. J Leukoc Biol 75: 901-909.
    • (2004) J Leukoc Biol , vol.75 , pp. 901-909
    • Vroon, A.1    Heijnen, C.J.2    Lombardi, M.S.3    Cobelens, P.M.4    Mayor Jr., F.5
  • 9
    • 0041854289 scopus 로고    scopus 로고
    • Signaling pathways for monocyte chemoattractant protein 1-mediated extracellular signal-regulated kinase activation
    • Jimenez-Sainz MC, Fast B, Mayor F, Jr., Aragay AM (2003) Signaling pathways for monocyte chemoattractant protein 1-mediated extracellular signal-regulated kinase activation. Mol Pharmacol 64: 773-782.
    • (2003) Mol Pharmacol , vol.64 , pp. 773-782
    • Jimenez-Sainz, M.C.1    Fast, B.2    Mayor Jr., F.3    Aragay, A.M.4
  • 10
    • 23944454929 scopus 로고    scopus 로고
    • Pivotal function for cytoplasmic protein FROUNT in CCR2-mediated monocyte chemotaxis
    • Terashima Y, Onai N, Murai M, Enomoto M, Poonpiriya V, et al. (2005) Pivotal function for cytoplasmic protein FROUNT in CCR2-mediated monocyte chemotaxis. Nat Immunol 6: 827-835.
    • (2005) Nat Immunol , vol.6 , pp. 827-835
    • Terashima, Y.1    Onai, N.2    Murai, M.3    Enomoto, M.4    Poonpiriya, V.5
  • 12
    • 0035942279 scopus 로고    scopus 로고
    • Dopamine D2 and D3 receptors are linked to the actin cytoskeleton via interaction with filamin A
    • Lin R, Karpa K, Kabbani N, Goldman-Rakic P, Levenson R (2001) Dopamine D2 and D3 receptors are linked to the actin cytoskeleton via interaction with filamin A. Proc Natl Acad Sci U S A 98: 5258-5263.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 5258-5263
    • Lin, R.1    Karpa, K.2    Kabbani, N.3    Goldman-Rakic, P.4    Levenson, R.5
  • 13
    • 0034548877 scopus 로고    scopus 로고
    • Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin
    • Petrecca K, Miller DM, Shrier A (2000) Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin. J Neurosci 20: 8736-8744.
    • (2000) J Neurosci , vol.20 , pp. 8736-8744
    • Petrecca, K.1    Miller, D.M.2    Shrier, A.3
  • 16
    • 0035969247 scopus 로고    scopus 로고
    • Filamin A, the Arp2/3 complex, and the morphology and function of cortical actin filaments in human melanoma cells
    • Flanagan LA, Chou J, Falet H, Neujahr R, Hartwig JH, et al. (2001) Filamin A, the Arp2/3 complex, and the morphology and function of cortical actin filaments in human melanoma cells. J Cell Biol 155: 511-517.
    • (2001) J Cell Biol , vol.155 , pp. 511-517
    • Flanagan, L.A.1    Chou, J.2    Falet, H.3    Neujahr, R.4    Hartwig, J.H.5
  • 17
    • 0036496624 scopus 로고    scopus 로고
    • Association of dopamine D(3) receptors with actin-binding protein 280 (ABP-280)
    • Li M, Li C, Weingarten P, Bunzow JR, Grandy DK, et al. (2002) Association of dopamine D(3) receptors with actin-binding protein 280 (ABP-280). Biochem Pharmacol 63: 859-863.
    • (2002) Biochem Pharmacol , vol.63 , pp. 859-863
    • Li, M.1    Li, C.2    Weingarten, P.3    Bunzow, J.R.4    Grandy, D.K.5
  • 18
    • 0036966954 scopus 로고    scopus 로고
    • Dominant negative mutants of filamin A block cell surface expression of the D2 dopamine receptor
    • Lin R, Canfield V, Levenson R (2002) Dominant negative mutants of filamin A block cell surface expression of the D2 dopamine receptor. Pharmacology 66: 173-181.
    • (2002) Pharmacology , vol.66 , pp. 173-181
    • Lin, R.1    Canfield, V.2    Levenson, R.3
  • 19
    • 0035860795 scopus 로고    scopus 로고
    • Interaction of the calcium-sensing receptor and filamin, a potential scaffolding protein
    • Awata H, Huang C, Handlogten ME, Miller RT (2001) Interaction of the calcium-sensing receptor and filamin, a potential scaffolding protein. J Biol Chem 276: 34871-34879.
    • (2001) J Biol Chem , vol.276 , pp. 34871-34879
    • Awata, H.1    Huang, C.2    Handlogten, M.E.3    Miller, R.T.4
  • 20
    • 0035860748 scopus 로고    scopus 로고
    • Filamin-A binds to the carboxyl-terminal tail of the calcium-sensing receptor, an interaction that participates in CaR-mediated activation of mitogen-activated protein kinase
    • Hjalm G, MacLeod RJ, Kifor O, Chattopadhyay N, Brown EM (2001) Filamin-A binds to the carboxyl-terminal tail of the calcium-sensing receptor, an interaction that participates in CaR-mediated activation of mitogen-activated protein kinase. J Biol Chem 276: 34880-34887.
    • (2001) J Biol Chem , vol.276 , pp. 34880-34887
    • Hjalm, G.1    Macleod, R.J.2    Kifor, O.3    Chattopadhyay, N.4    Brown, E.M.5
  • 21
    • 0037070641 scopus 로고    scopus 로고
    • The actin-binding protein Filamin-A interacts with the metabotropic glutamate receptor type 7
    • Enz R (2002) The actin-binding protein Filamin-A interacts with the metabotropic glutamate receptor type 7. FEBS Lett 514: 184-188.
    • (2002) FEBS Lett , vol.514 , pp. 184-188
    • Enz, R.1
  • 22
    • 0038532256 scopus 로고    scopus 로고
    • Binding of filamin to the C-terminal tail of the calcitonin receptor controls recycling
    • Seck T, Baron R, Horne WC (2003) Binding of filamin to the C-terminal tail of the calcitonin receptor controls recycling. J Biol Chem 278: 10408-10416.
    • (2003) J Biol Chem , vol.278 , pp. 10408-10416
    • Seck, T.1    Baron, R.2    Horne, W.C.3
  • 23
    • 0142210175 scopus 로고    scopus 로고
    • Interaction between the mu opioid receptor and filamin A is involved in receptor regulation and trafficking
    • Onoprishvili I, Andria ML, Kramer HK, Ancevska-Taneva N, Hiller JM, et al. (2003) Interaction between the mu opioid receptor and filamin A is involved in receptor regulation and trafficking. Mol Pharmacol 64: 1092-1100.
    • (2003) Mol Pharmacol , vol.64 , pp. 1092-1100
    • Onoprishvili, I.1    Andria, M.L.2    Kramer, H.K.3    Ancevska-Taneva, N.4    Hiller, J.M.5
  • 24
    • 71749121849 scopus 로고    scopus 로고
    • Identification and characterization of multiple similar ligand-binding repeats in filamin: Implication on filamin-mediated receptor clustering and cross-talk
    • Ithychanda SS, Hsu D, Li H, Yan L, Liu D, et al. (2009) Identification and characterization of multiple similar ligand-binding repeats in filamin: implication on filamin-mediated receptor clustering and cross-talk. J Biol Chem 284: 35113-35121.
    • (2009) J Biol Chem , vol.284 , pp. 35113-35121
    • Ithychanda, S.S.1    Hsu, D.2    Li, H.3    Yan, L.4    Liu, D.5
  • 25
    • 26844517614 scopus 로고    scopus 로고
    • A modular design for the clathrinand actin-mediated endocytosis machinery
    • Kaksonen M, Toret CP, Drubin DG (2005) A modular design for the clathrinand actin-mediated endocytosis machinery. Cell 123: 305-320.
    • (2005) Cell , vol.123 , pp. 305-320
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 26
    • 0036714223 scopus 로고    scopus 로고
    • Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits
    • Merrifield CJ, Feldman ME, Wan L, Almers W (2002) Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits. Nat Cell Biol 4: 691-698.
    • (2002) Nat Cell Biol , vol.4 , pp. 691-698
    • Merrifield, C.J.1    Feldman, M.E.2    Wan, L.3    Almers, W.4
  • 27
    • 16844377622 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase regulates dopamine D3 receptor signaling by modulating the stability of a receptor-filamin-beta-arrestin complex. A case of autoreceptor regulation
    • Kim KM, Gainetdinov RR, Laporte SA, Caron MG, Barak LS (2005) G protein-coupled receptor kinase regulates dopamine D3 receptor signaling by modulating the stability of a receptor-filamin-beta-arrestin complex. A case of autoreceptor regulation. J Biol Chem 280: 12774-12780.
    • (2005) J Biol Chem , vol.280 , pp. 12774-12780
    • Kim, K.M.1    Gainetdinov, R.R.2    Laporte, S.A.3    Caron, M.G.4    Barak, L.S.5
  • 28
    • 33646263875 scopus 로고    scopus 로고
    • Cooperative regulation of extracellular signal-regulated kinase activation and cell shape change by filamin A and beta-arrestins
    • Scott MG, Pierotti V, Storez H, Lindberg E, Thuret A, et al. (2006) Cooperative regulation of extracellular signal-regulated kinase activation and cell shape change by filamin A and beta-arrestins. Mol Cell Biol 26: 3432-3445.
    • (2006) Mol Cell Biol , vol.26 , pp. 3432-3445
    • Scott, M.G.1    Pierotti, V.2    Storez, H.3    Lindberg, E.4    Thuret, A.5
  • 29
    • 15744379719 scopus 로고    scopus 로고
    • High affinity interaction with filamin A protects against calcium-sensing receptor degradation
    • Zhang M, Breitwieser GE (2005) High affinity interaction with filamin A protects against calcium-sensing receptor degradation. J Biol Chem 280: 11140-11146.
    • (2005) J Biol Chem , vol.280 , pp. 11140-11146
    • Zhang, M.1    Breitwieser, G.E.2
  • 30
    • 0031408331 scopus 로고    scopus 로고
    • Cytoskeletal protein ABP-280 directs the intracellular trafficking of furin and modulates proprotein processing in the endocytic pathway
    • Liu G, Thomas L, Warren RA, Enns CA, Cunningham CC, et al. (1997) Cytoskeletal protein ABP-280 directs the intracellular trafficking of furin and modulates proprotein processing in the endocytic pathway. J Cell Biol 139: 1719-1733.
    • (1997) J Cell Biol , vol.139 , pp. 1719-1733
    • Liu, G.1    Thomas, L.2    Warren, R.A.3    Enns, C.A.4    Cunningham, C.C.5
  • 31
    • 34548339698 scopus 로고    scopus 로고
    • Roles of protein kinase C and actin-binding protein 280 in the regulation of intracellular trafficking of dopamine D3 receptor
    • Cho EY, Cho DI, Park JH, Kurose H, Caron MG, et al. (2007) Roles of protein kinase C and actin-binding protein 280 in the regulation of intracellular trafficking of dopamine D3 receptor. Mol Endocrinol 21: 2242-2254.
    • (2007) Mol Endocrinol , vol.21 , pp. 2242-2254
    • Cho, E.Y.1    Cho, D.I.2    Park, J.H.3    Kurose, H.4    Caron, M.G.5
  • 33
    • 70350142558 scopus 로고    scopus 로고
    • The role of vesicle trafficking in epithelial cell motility
    • Fletcher SJ, Rappoport JZ (2009) The role of vesicle trafficking in epithelial cell motility. Biochem Soc Trans 37: 1072-1076.
    • (2009) Biochem Soc Trans , vol.37 , pp. 1072-1076
    • Fletcher, S.J.1    Rappoport, J.Z.2
  • 34
    • 0032494121 scopus 로고    scopus 로고
    • The cytoplasmic tail of rhodopsin acts as a novel apical sorting signal in polarized MDCK cells
    • Chuang JZ, Sung CH (1998) The cytoplasmic tail of rhodopsin acts as a novel apical sorting signal in polarized MDCK cells. J Cell Biol 142: 1245-1256.
    • (1998) J Cell Biol , vol.142 , pp. 1245-1256
    • Chuang, J.Z.1    Sung, C.H.2
  • 36
    • 33845792555 scopus 로고    scopus 로고
    • CellProfiler: Image analysis software for identifying and quantifying cell phenotypes
    • Carpenter AE, Jones TR, Lamprecht MR, Clarke C, Kang IH, et al. (2006) CellProfiler: image analysis software for identifying and quantifying cell phenotypes. Genome Biol 7: R100.
    • (2006) Genome Biol , vol.7
    • Carpenter, A.E.1    Jones, T.R.2    Lamprecht, M.R.3    Clarke, C.4    Kang, I.H.5
  • 37
    • 58149141565 scopus 로고    scopus 로고
    • High-affinity binding of southern African HIV type 1 subtype C envelope protein, gp120, to the CCR5 coreceptor
    • Fromme BJ, Coetsee M, Van Der Watt P, Chan MC, Sperling KM, et al. (2008) High-affinity binding of southern African HIV type 1 subtype C envelope protein, gp120, to the CCR5 coreceptor. AIDS Res Hum Retroviruses 24: 1527-1536.
    • (2008) AIDS Res Hum Retroviruses , vol.24 , pp. 1527-1536
    • Fromme, B.J.1    Coetsee, M.2    van der Watt, P.3    Chan, M.C.4    Sperling, K.M.5
  • 38
    • 33644895118 scopus 로고    scopus 로고
    • Silencing of filamin A gene expression inhibits Ca2+ -sensing receptor signaling
    • Huang C, Wu Z, Hujer KM, Miller RT (2006) Silencing of filamin A gene expression inhibits Ca2+ -sensing receptor signaling. FEBS Lett 580: 1795-1800.
    • (2006) FEBS Lett , vol.580 , pp. 1795-1800
    • Huang, C.1    Wu, Z.2    Hujer, K.M.3    Miller, R.T.4


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