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Volumn 7, Issue 8, 2012, Pages

Filamin A-hinge region 1-EGFP: A novel tool for tracking the cellular functions of filamin A in real-time

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN; CHEMOKINE RECEPTOR CCR2; CHEMOKINE RECEPTOR CCR2B; FILAMIN A; UNCLASSIFIED DRUG;

EID: 84864740249     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0040864     Document Type: Article
Times cited : (7)

References (44)
  • 2
    • 0025184841 scopus 로고
    • Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring
    • Gorlin JB, Yamin R, Egan S, Stewart M, Stossel TP, et al. (1990) Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring. J Cell Biol 111: 1089-1105.
    • (1990) J Cell Biol , vol.111 , pp. 1089-1105
    • Gorlin, J.B.1    Yamin, R.2    Egan, S.3    Stewart, M.4    Stossel, T.P.5
  • 3
    • 0035938225 scopus 로고    scopus 로고
    • Structural and functional aspects of filamins
    • van der Flier A, Sonnenberg A, (2001) Structural and functional aspects of filamins. Biochim Biophys Acta 1538: 99-117.
    • (2001) Biochim Biophys Acta , vol.1538 , pp. 99-117
    • van der Flier, A.1    Sonnenberg, A.2
  • 4
    • 32544453848 scopus 로고    scopus 로고
    • Calcineurin dephosphorylates the C-terminal region of filamin in an important regulatory site: a possible mechanism for filamin mobilization and cell signaling
    • Garcia E, Stracher A, Jay D, (2006) Calcineurin dephosphorylates the C-terminal region of filamin in an important regulatory site: a possible mechanism for filamin mobilization and cell signaling. Arch Biochem Biophys 446: 140-150.
    • (2006) Arch Biochem Biophys , vol.446 , pp. 140-150
    • Garcia, E.1    Stracher, A.2    Jay, D.3
  • 5
    • 0025734201 scopus 로고
    • Evidence that a 27-residue sequence is the actin-binding site of ABP-120
    • Bresnick AR, Janmey PA, Condeelis J, (1991) Evidence that a 27-residue sequence is the actin-binding site of ABP-120. J Biol Chem 266: 12989-12993.
    • (1991) J Biol Chem , vol.266 , pp. 12989-12993
    • Bresnick, A.R.1    Janmey, P.A.2    Condeelis, J.3
  • 6
    • 0028837008 scopus 로고
    • Calcium/calmodulin-dependent regulation of the NH2-terminal F-actin binding domain of utrophin
    • Winder SJ, Kendrick-Jones J, (1995) Calcium/calmodulin-dependent regulation of the NH2-terminal F-actin binding domain of utrophin. FEBS Lett 357: 125-128.
    • (1995) FEBS Lett , vol.357 , pp. 125-128
    • Winder, S.J.1    Kendrick-Jones, J.2
  • 10
  • 11
    • 0032483459 scopus 로고    scopus 로고
    • Filamin binds to the cytoplasmic domain of the beta1-integrin. Identification of amino acids responsible for this interaction
    • Loo DT, Kanner SB, Aruffo A, (1998) Filamin binds to the cytoplasmic domain of the beta1-integrin. Identification of amino acids responsible for this interaction. J Biol Chem 273: 23304-23312.
    • (1998) J Biol Chem , vol.273 , pp. 23304-23312
    • Loo, D.T.1    Kanner, S.B.2    Aruffo, A.3
  • 12
    • 0028958438 scopus 로고
    • Direct interaction of filamin (ABP-280) with the beta 2-integrin subunit CD18
    • Sharma CP, Ezzell RM, Arnaout MA, (1995) Direct interaction of filamin (ABP-280) with the beta 2-integrin subunit CD18. J Immunol 154: 3461-3470.
    • (1995) J Immunol , vol.154 , pp. 3461-3470
    • Sharma, C.P.1    Ezzell, R.M.2    Arnaout, M.A.3
  • 13
    • 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
  • 14
    • 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
  • 16
    • 0033768873 scopus 로고    scopus 로고
    • Androgen receptor nuclear translocation is facilitated by the f-actin cross-linking protein filamin
    • Ozanne DM, Brady ME, Cook S, Gaughan L, Neal DE, et al. (2000) Androgen receptor nuclear translocation is facilitated by the f-actin cross-linking protein filamin. Mol Endocrinol 14: 1618-1626.
    • (2000) Mol Endocrinol , vol.14 , pp. 1618-1626
    • Ozanne, D.M.1    Brady, M.E.2    Cook, S.3    Gaughan, L.4    Neal, D.E.5
  • 19
    • 33750533178 scopus 로고    scopus 로고
    • CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse
    • Tavano R, Contento RL, Baranda SJ, Soligo M, Tuosto L, et al. (2006) CD28 interaction with filamin-A controls lipid raft accumulation at the T-cell immunological synapse. Nat Cell Biol 8: 1270-1276.
    • (2006) Nat Cell Biol , vol.8 , pp. 1270-1276
    • Tavano, R.1    Contento, R.L.2    Baranda, S.J.3    Soligo, M.4    Tuosto, L.5
  • 20
    • 0021996756 scopus 로고
    • Identification of two proteins (actin-binding protein and P235) that are hydrolyzed by endogenous Ca2+-dependent protease during platelet aggregation
    • Fox JE, Goll DE, Reynolds CC, Phillips DR, (1985) Identification of two proteins (actin-binding protein and P235) that are hydrolyzed by endogenous Ca2+-dependent protease during platelet aggregation. J Biol Chem 260: 1060-1066.
    • (1985) J Biol Chem , vol.260 , pp. 1060-1066
    • Fox, J.E.1    Goll, D.E.2    Reynolds, C.C.3    Phillips, D.R.4
  • 21
    • 0036168356 scopus 로고    scopus 로고
    • Cutting to the chase: calpain proteases in cell motility
    • Glading A, Lauffenburger DA, Wells A, (2002) Cutting to the chase: calpain proteases in cell motility. Trends Cell Biol 12: 46-54.
    • (2002) Trends Cell Biol , vol.12 , pp. 46-54
    • Glading, A.1    Lauffenburger, D.A.2    Wells, A.3
  • 22
    • 0025915427 scopus 로고
    • Cell migration and actin organization in cultured human primary, recurrent cutaneous and metastatic melanoma. Time-lapse and image analysis
    • Byers HR, Etoh T, Doherty JR, Sober AJ, Mihm MC Jr, (1991) Cell migration and actin organization in cultured human primary, recurrent cutaneous and metastatic melanoma. Time-lapse and image analysis. Am J Pathol 139: 423-435.
    • (1991) Am J Pathol , vol.139 , pp. 423-435
    • Byers, H.R.1    Etoh, T.2    Doherty, J.R.3    Sober, A.J.4    Mihm Jr., M.C.5
  • 23
    • 0026543374 scopus 로고
    • Actin-binding protein requirement for cortical stability and efficient locomotion
    • Cunningham CC, Gorlin JB, Kwiatkowski DJ, Hartwig JH, Janmey PA, et al. (1992) Actin-binding protein requirement for cortical stability and efficient locomotion. Science 255: 325-327.
    • (1992) Science , vol.255 , pp. 325-327
    • Cunningham, C.C.1    Gorlin, J.B.2    Kwiatkowski, D.J.3    Hartwig, J.H.4    Janmey, P.A.5
  • 24
    • 68049126309 scopus 로고    scopus 로고
    • Filamin A is essential for active cell stiffening but not passive stiffening under external force
    • Kasza KE, Nakamura F, Hu S, Kollmannsberger P, Bonakdar N, et al. (2009) Filamin A is essential for active cell stiffening but not passive stiffening under external force. Biophys J 96: 4326-4335.
    • (2009) Biophys J , vol.96 , pp. 4326-4335
    • Kasza, K.E.1    Nakamura, F.2    Hu, S.3    Kollmannsberger, P.4    Bonakdar, N.5
  • 25
    • 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
  • 26
    • 33947314576 scopus 로고    scopus 로고
    • Regulation of receptor trafficking by GRKs and arrestins
    • Moore CA, Milano SK, Benovic JL, (2007) Regulation of receptor trafficking by GRKs and arrestins. Annu Rev Physiol 69: 451-482.
    • (2007) Annu Rev Physiol , vol.69 , pp. 451-482
    • Moore, C.A.1    Milano, S.K.2    Benovic, J.L.3
  • 27
    • 62849095585 scopus 로고    scopus 로고
    • Molecular basis of filamin A-FilGAP interaction and its impairment in congenital disorders associated with filamin A mutations
    • Nakamura F, Heikkinen O, Pentikainen OT, Osborn TM, Kasza KE, et al. (2009) Molecular basis of filamin A-FilGAP interaction and its impairment in congenital disorders associated with filamin A mutations. PLoS One 4: e4928.
    • (2009) PLoS One , vol.4
    • Nakamura, F.1    Heikkinen, O.2    Pentikainen, O.T.3    Osborn, T.M.4    Kasza, K.E.5
  • 28
    • 32344453990 scopus 로고    scopus 로고
    • Prestressed F-actin networks cross-linked by hinged filamins replicate mechanical properties of cells
    • Gardel ML, Nakamura F, Hartwig JH, Crocker JC, Stossel TP, et al. (2006) Prestressed F-actin networks cross-linked by hinged filamins replicate mechanical properties of cells. Proc Natl Acad Sci U S A 103: 1762-1767.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 1762-1767
    • Gardel, M.L.1    Nakamura, F.2    Hartwig, J.H.3    Crocker, J.C.4    Stossel, T.P.5
  • 30
    • 13444256235 scopus 로고    scopus 로고
    • FOXC1 transcriptional regulatory activity is impaired by PBX1 in a filamin A-mediated manner
    • Berry FB, O'Neill MA, Coca-Prados M, Walter MA, (2005) FOXC1 transcriptional regulatory activity is impaired by PBX1 in a filamin A-mediated manner. Mol Cell Biol 25: 1415-1424.
    • (2005) Mol Cell Biol , vol.25 , pp. 1415-1424
    • Berry, F.B.1    O'Neill, M.A.2    Coca-Prados, M.3    Walter, M.A.4
  • 31
    • 33847419281 scopus 로고    scopus 로고
    • Filamin links cell shape and cytoskeletal structure to Rho regulation by controlling accumulation of p190RhoGAP in lipid rafts
    • Mammoto A, Huang S, Ingber DE, (2007) Filamin links cell shape and cytoskeletal structure to Rho regulation by controlling accumulation of p190RhoGAP in lipid rafts. J Cell Sci 120: 456-467.
    • (2007) J Cell Sci , vol.120 , pp. 456-467
    • Mammoto, A.1    Huang, S.2    Ingber, D.E.3
  • 32
    • 0029020632 scopus 로고
    • Actin polymerization and intracellular solvent flow in cell surface blebbing
    • Cunningham CC, (1995) Actin polymerization and intracellular solvent flow in cell surface blebbing. J Cell Biol 129: 1589-1599.
    • (1995) J Cell Biol , vol.129 , pp. 1589-1599
    • Cunningham, C.C.1
  • 34
    • 33745767358 scopus 로고    scopus 로고
    • Harnessing actin dynamics for clathrin-mediated endocytosis
    • Kaksonen M, Toret CP, Drubin DG, (2006) Harnessing actin dynamics for clathrin-mediated endocytosis. Nat Rev Mol Cell Biol 7: 404-414.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 404-414
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 35
    • 0037039414 scopus 로고    scopus 로고
    • The large GTPase dynamin regulates actin comet formation and movement in living cells
    • Orth JD, Krueger EW, Cao H, McNiven MA, (2002) The large GTPase dynamin regulates actin comet formation and movement in living cells. Proc Natl Acad Sci U S A 99: 167-172.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 167-172
    • Orth, J.D.1    Krueger, E.W.2    Cao, H.3    McNiven, M.A.4
  • 36
    • 33846628565 scopus 로고    scopus 로고
    • RhoB and the mammalian Diaphanous-related formin mDia2 in endosome trafficking
    • Wallar BJ, Deward AD, Resau JH, Alberts AS, (2007) RhoB and the mammalian Diaphanous-related formin mDia2 in endosome trafficking. Exp Cell Res 313: 560-571.
    • (2007) Exp Cell Res , vol.313 , pp. 560-571
    • Wallar, B.J.1    Deward, A.D.2    Resau, J.H.3    Alberts, A.S.4
  • 37
    • 0033662155 scopus 로고    scopus 로고
    • The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin
    • Bellanger JM, Astier C, Sardet C, Ohta Y, Stossel TP, et al. (2000) The Rac1- and RhoG-specific GEF domain of Trio targets filamin to remodel cytoskeletal actin. Nat Cell Biol 2: 888-892.
    • (2000) Nat Cell Biol , vol.2 , pp. 888-892
    • Bellanger, J.M.1    Astier, C.2    Sardet, C.3    Ohta, Y.4    Stossel, T.P.5
  • 38
    • 0036773284 scopus 로고    scopus 로고
    • Calcium-sensing receptor activation of rho involves filamin and rho-guanine nucleotide exchange factor
    • Pi M, Spurney RF, Tu Q, Hinson T, Quarles LD, (2002) Calcium-sensing receptor activation of rho involves filamin and rho-guanine nucleotide exchange factor. Endocrinology 143: 3830-3838.
    • (2002) Endocrinology , vol.143 , pp. 3830-3838
    • Pi, M.1    Spurney, R.F.2    Tu, Q.3    Hinson, T.4    Quarles, L.D.5
  • 39
    • 0036711657 scopus 로고    scopus 로고
    • Filamin is essential in actin cytoskeletal assembly mediated by p21-activated kinase 1
    • Vadlamudi RK, Li F, Adam L, Nguyen D, Ohta Y, et al. (2002) Filamin is essential in actin cytoskeletal assembly mediated by p21-activated kinase 1. Nat Cell Biol 4: 681-690.
    • (2002) Nat Cell Biol , vol.4 , pp. 681-690
    • Vadlamudi, R.K.1    Li, F.2    Adam, L.3    Nguyen, D.4    Ohta, Y.5
  • 40
    • 0037459068 scopus 로고    scopus 로고
    • The carboxy-terminal pleckstrin homology domain of ROCK interacts with filamin-A
    • Ueda K, Ohta Y, Hosoya H, (2003) The carboxy-terminal pleckstrin homology domain of ROCK interacts with filamin-A. Biochem Biophys Res Commun 301: 886-890.
    • (2003) Biochem Biophys Res Commun , vol.301 , pp. 886-890
    • Ueda, K.1    Ohta, Y.2    Hosoya, H.3
  • 41
    • 33746658154 scopus 로고    scopus 로고
    • FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control actin remodelling
    • Ohta Y, Hartwig JH, Stossel TP, (2006) FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control actin remodelling. Nat Cell Biol 8: 803-814.
    • (2006) Nat Cell Biol , vol.8 , pp. 803-814
    • Ohta, Y.1    Hartwig, J.H.2    Stossel, T.P.3
  • 42
    • 58749087548 scopus 로고    scopus 로고
    • Disruption of neural progenitors along the ventricular and subventricular zones in periventricular heterotopia
    • Ferland RJ, Batiz LF, Neal J, Lian G, Bundock E, et al. (2009) Disruption of neural progenitors along the ventricular and subventricular zones in periventricular heterotopia. Hum Mol Genet 18: 497-516.
    • (2009) Hum Mol Genet , vol.18 , pp. 497-516
    • Ferland, R.J.1    Batiz, L.F.2    Neal, J.3    Lian, G.4    Bundock, E.5
  • 43
    • 0030820352 scopus 로고    scopus 로고
    • Myosin II is associated with Golgi membranes: identification of p200 as nonmuscle myosin II on Golgi-derived vesicles
    • Ikonen E, de Almeid JB, Fath KR, Burgess DR, Ashman K, et al. (1997) Myosin II is associated with Golgi membranes: identification of p200 as nonmuscle myosin II on Golgi-derived vesicles. J Cell Sci 110 (Pt 18): 2155-2164.
    • (1997) J Cell Sci , vol.110 , Issue.Pt 18 , pp. 2155-2164
    • Ikonen, E.1    de Almeid, J.B.2    Fath, K.R.3    Burgess, D.R.4    Ashman, K.5
  • 44
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.