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Volumn 11, Issue 7, 2010, Pages 639-650

Structural portrait of filamin interaction mechanisms

Author keywords

Actin; Actin binding proteins; Cystoskeleton; Filamin; Z disk

Indexed keywords

ACTIN; FILAMIN;

EID: 79251481827     PISSN: 13892037     EISSN: None     Source Type: Journal    
DOI: 10.2174/138920310794109111     Document Type: Article
Times cited : (15)

References (74)
  • 1
  • 2
    • 0032883413 scopus 로고    scopus 로고
    • Structural mechanism of muscle contraction
    • Geeves, M.A.; Holmes, K.C. Structural mechanism of muscle contraction. Annu. Rev. Biochem., 1999,68, 687-728.
    • (1999) Annu. Rev. Biochem , vol.68 , pp. 687-728
    • Geeves, M.A.1    Holmes, K.C.2
  • 3
    • 0032832619 scopus 로고    scopus 로고
    • Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod
    • McCoy, A.J.; Fucini, P.; Noegel, A.A.; Stewart, M. Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod. Nat. Struct. Biol., 1999, 6, 836-841.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 836-841
    • McCoy, A.J.1    Fucini, P.2    Noegel, A.A.3    Stewart, M.4
  • 8
    • 58149202318 scopus 로고    scopus 로고
    • Terminal assembly of sarcomeric filaments by intermolecular betasheet formation
    • Pinotsis, N.; Abrusci, P.; Djinovic-Carugo, K.; Wilmanns, M. Terminal assembly of sarcomeric filaments by intermolecular betasheet formation. Trends Biochem. Sci., 2009, 34, 33-39.
    • (2009) Trends Biochem. Sci , vol.34 , pp. 33-39
    • Pinotsis, N.1    Abrusci, P.2    Djinovic-Carugo, K.3    Wilmanns, M.4
  • 14
    • 19444368524 scopus 로고    scopus 로고
    • Filamin A: Phenotypic diversity
    • Robertson, S.P. Filamin A: phenotypic diversity. Curr. Opin. Genet. Dev., 2005, 15, 301-307.
    • (2005) Curr. Opin. Genet. Dev , vol.15 , pp. 301-307
    • Robertson, S.P.1
  • 17
    • 0035969247 scopus 로고    scopus 로고
    • The Arp2/3 complex, and the morphology and function of cortical actin filaments in human melanoma cells
    • Flanagan, L.A.; Chou, J.; Falet, H.; Neujahr, R.; Hartwig, J.H.; Stossel, T.P. Filamin A, the Arp2/3 complex, and the morphology and function of cortical actin filaments in human melanoma cells. J. Cell. Biol., 2001, 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    Stossel, T.P.6    Filamin, A.7
  • 18
    • 0037077244 scopus 로고    scopus 로고
    • Cell death and mechanoprotection by filamin a in connective tissues after challenge by applied tensile forces
    • Kainulainen, T.; Pender, A.; D'Addario, M.; Feng, Y.; Lekic, P.; McCulloch, C.A., Cell death and mechanoprotection by filamin a in connective tissues after challenge by applied tensile forces. J. Biol. Chem., 2002, 277, 21998-22009.
    • (2002) J. Biol. Chem , vol.277 , pp. 21998-22009
    • Kainulainen, T.1    Pender, A.2    D'Addario, M.3    Feng, Y.4    Lekic, P.5    McCulloch, C.A.6
  • 20
    • 0037037545 scopus 로고    scopus 로고
    • Regulation of the subcellular localization of tumor necrosis factor receptor-associated factor (TRAF)2 by TRAF1 reveals mechanisms of TRAF2 signaling
    • Arron, J.R.; Pewzner-Jung, Y.; Walsh, M.C.; Kobayashi, T.; Choi, Y. Regulation of the subcellular localization of tumor necrosis factor receptor-associated factor (TRAF)2 by TRAF1 reveals mechanisms of TRAF2 signaling. J. Exp. Med., 2002, 196, 923-934.
    • (2002) J. Exp. Med , vol.196 , pp. 923-934
    • Arron, J.R.1    Pewzner-Jung, Y.2    Walsh, M.C.3    Kobayashi, T.4    Choi, Y.5
  • 21
    • 0035860795 scopus 로고    scopus 로고
    • Interaction of the calcium-sensing receptor and filamin, a potential scaffolding protein
    • Awata, H.; Huang, C.; Handlogten, M.E.; Miller, R.T. Interaction of the calcium-sensing receptor and filamin, a potential scaffolding protein. J. Biol. Chem. 2001, 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
  • 24
    • 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. Dopamine D2 and D3 receptors are linked to the actin cytoskeleton via interaction with filamin A. Proc. Natl. Acad. Sci. USA, 2001, 98, 5258-5263.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5258-5263
    • Lin, R.1    Karpa, K.2    Kabbani, N.3    Goldman-Rakic, P.4    Levenson, R.5
  • 25
    • 0037070641 scopus 로고    scopus 로고
    • The actin-binding protein Filamin-A interacts with the metabotropic glutamate receptor type 7
    • Enz, R. The actin-binding protein Filamin-A interacts with the metabotropic glutamate receptor type 7. FEBS Lett., 2002, 514, 184-188.
    • (2002) FEBS Lett , vol.514 , pp. 184-188
    • Enz, R.1
  • 26
    • 0038532256 scopus 로고    scopus 로고
    • Binding of filamin to the C-terminal tail of the calcitonin receptor controls recycling
    • Seck, T.; Baron, R.; Horne, W. C., Binding of filamin to the C-terminal tail of the calcitonin receptor controls recycling. J Biol Chem 2003,278, 10408-16.
    • (2003) J Biol Chem , vol.278 , pp. 10408-16
    • Seck, T.1    Baron, R.2    Horne, W.C.3
  • 27
    • 0142211278 scopus 로고    scopus 로고
    • Direct interaction between the actin-binding protein filamin-A and the inwardly rectifying potassium channel, Kir2.1
    • Sampson, L.J.; Leyland, M.L.; Dart, C. Direct interaction between the actin-binding protein filamin-A and the inwardly rectifying potassium channel, Kir2.1. J. Biol. Chem., 2003, 278, 41988-41997.
    • (2003) J. Biol. Chem , vol.278 , pp. 41988-41997
    • Sampson, L.J.1    Leyland, M.L.2    Dart, C.3
  • 28
    • 3042587718 scopus 로고    scopus 로고
    • Interaction of filamin A with the integrin beta 7 cytoplasmic domain: Role of alternative splicing and phosphorylation
    • Travis, M.A.; van der Flier, A.; Kammerer, R.A.; Mould, A.P.; Sonnenberg, A.; Humphries, M.J. Interaction of filamin A with the integrin beta 7 cytoplasmic domain: role of alternative splicing and phosphorylation. FEBS Lett., 2004, 569, 185-190.
    • (2004) FEBS Lett , vol.569 , pp. 185-190
    • Travis, M.A.1    van der Flier, A.2    Kammerer, R.A.3    Mould, A.P.4    Sonnenberg, A.5    Humphries, M.J.6
  • 29
    • 0038607443 scopus 로고    scopus 로고
    • The F-actin cross-linking and focal adhesion protein filamin A is a ligand and in vivo substrate for protein kinase C alpha
    • Tigges, U.; Koch, B.; Wissing, J.; Jockusch, B.M.; Ziegler, W.H. The F-actin cross-linking and focal adhesion protein filamin A is a ligand and in vivo substrate for protein kinase C alpha. J. Biol. Chem., 2003, 278, 23561-23569.
    • (2003) J. Biol. Chem , vol.278 , pp. 23561-23569
    • Tigges, U.1    Koch, B.2    Wissing, J.3    Jockusch, B.M.4    Ziegler, W.H.5
  • 30
    • 0034715945 scopus 로고    scopus 로고
    • Caveolae: Uniform structures with multiple functions in signaling, cell growth, and cancer
    • Stahlhut, M.; Sandvig, K.; van Deurs, B. Caveolae: uniform structures with multiple functions in signaling, cell growth, and cancer. Exp. Cell. Res., 2000, 261, 111-118.
    • (2000) Exp. Cell. Res , vol.261 , pp. 111-118
    • Stahlhut, M.1    Sandvig, K.2    van Deurs, B.3
  • 31
    • 0036711657 scopus 로고    scopus 로고
    • Filamin is essential in actin cytoskeletal assembly mediated by p21-activated kinase 1
    • Vadlamudi, R.K.; Li, F.; Adam, L.; Nguyen, D.; Ohta, Y.; Stossel, T.P.; Kumar, R. Filamin is essential in actin cytoskeletal assembly mediated by p21-activated kinase 1. Nat. Cell. Biol., 2002, 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    Stossel, T.P.6    Kumar, R.7
  • 32
    • 14944370105 scopus 로고    scopus 로고
    • Migfilin and its binding partners: From cell biology to human diseases
    • Wu, C. Migfilin and its binding partners: from cell biology to human diseases. J. Cell. Sci., 2005, 118, 659-664.
    • (2005) J. Cell. Sci , vol.118 , pp. 659-664
    • Wu, C.1
  • 33
    • 0037418837 scopus 로고    scopus 로고
    • Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation
    • Tu, Y.; Wu, S.; Shi, X.; Chen, K.; Wu, C. Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell, 2003, 113, 37-47.
    • (2003) Cell , vol.113 , pp. 37-47
    • Tu, Y.1    Wu, S.2    Shi, X.3    Chen, K.4    Wu, C.5
  • 37
    • 0032578772 scopus 로고    scopus 로고
    • Molecular cloning of human ABPL, an actin-binding protein homologue
    • Xie, Z.; Xu, W.; Davie, E.W.; Chung, D.W. Molecular cloning of human ABPL, an actin-binding protein homologue. Biochem. Biophys. Res. Commun., 1998, 251, 914-919.
    • (1998) Biochem. Biophys. Res. Commun , vol.251 , pp. 914-919
    • Xie, Z.1    Xu, W.2    Davie, E.W.3    Chung, D.W.4
  • 40
    • 33744941082 scopus 로고    scopus 로고
    • Unusual splicing events result in distinct Xin isoforms that associate differentially with filamin c and Mena/VASP
    • van der Ven, P.F.; Ehler, E.; Vakeel, P.; Eulitz, S.; Schenk, J.A.; Milting, H.; Micheel, B.; Furst, D.O. Unusual splicing events result in distinct Xin isoforms that associate differentially with filamin c and Mena/VASP. Exp. Cell. Res., 2006, 312, 2154-2167.
    • (2006) Exp. Cell. Res , vol.312 , pp. 2154-2167
    • van der Ven, P.F.1    Ehler, E.2    Vakeel, P.3    Eulitz, S.4    Schenk, J.A.5    Milting, H.6    Micheel, B.7    Furst, D.O.8
  • 41
    • 9444268202 scopus 로고    scopus 로고
    • Filamin C interacts with the muscular dystrophy KY protein and is abnormally distributed in mouse KY deficient muscle fibres
    • Beatham, J.; Romero, R.; Townsend, S.K.; Hacker, T.; van der Ven, P.F.; Blanco, G. Filamin C interacts with the muscular dystrophy KY protein and is abnormally distributed in mouse KY deficient muscle fibres. Hum. Mol. Genet., 2004, 13, 2863-2874.
    • (2004) Hum. Mol. Genet , vol.13 , pp. 2863-2874
    • Beatham, J.1    Romero, R.2    Townsend, S.K.3    Hacker, T.4    van der Ven, P.F.5    Blanco, G.6
  • 42
    • 33747753150 scopus 로고    scopus 로고
    • Loss of FilaminC (FLNc) results in severe defects in myogenesis and myotube structure
    • Dalkilic, I.; Schienda, J.; Thompson, T.G.; Kunkel, L.M. Loss of FilaminC (FLNc) results in severe defects in myogenesis and myotube structure. Mol. Cell. Biol., 2006, 26, 6522-6534.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 6522-6534
    • Dalkilic, I.1    Schienda, J.2    Thompson, T.G.3    Kunkel, L.M.4
  • 43
    • 51349145767 scopus 로고    scopus 로고
    • Molecular pathology of myofibrillar myopathies
    • Ferrer, I.; Olive, M. Molecular pathology of myofibrillar myopathies. Expert. Rev. Mol. Med., 2008, 10, e25.
    • (2008) Expert. Rev. Mol. Med , vol.e25 , pp. 10
    • Ferrer, I.1    Olive, M.2
  • 45
    • 53549117700 scopus 로고    scopus 로고
    • Myofibrillar myopathies
    • Selcen, D. Myofibrillar myopathies. Curr. Opin. Neurol., 2008, 21, 585-589.
    • (2008) Curr. Opin. Neurol , vol.21 , pp. 585-589
    • Selcen, D.1
  • 47
    • 73349141146 scopus 로고    scopus 로고
    • Structure of the human filamin A actin-binding domain
    • Ruskamo, S.; Ylanne, J. Structure of the human filamin A actin-binding domain. Acta Crystallogr. D Biol. Crystallogr., 2009, 65, 1217-1221.
    • (2009) Acta Crystallogr. D Biol. Crystallogr , vol.65 , pp. 1217-1221
    • Ruskamo, S.1    Ylanne, J.2
  • 49
    • 0037457811 scopus 로고    scopus 로고
    • The limits of promiscuity: Isoform-specific dimerization of filamins
    • Himmel, M.; Van Der Ven, P.F.; Stocklein, W.; Furst, D.O. The limits of promiscuity: isoform-specific dimerization of filamins. Biochemistry, 2003, 42, 430-439.
    • (2003) Biochemistry , vol.42 , pp. 430-439
    • Himmel, M.1    van der Ven, P.F.2    Stocklein, W.3    Furst, D.O.4
  • 50
    • 0017828655 scopus 로고
    • Filamin-actin interaction. Dissociation of binding from gelation by Ca(II)-activated proteolysis
    • Davies, P.J.; Wallach, D.; Willingham, M.C.; Pastan, I.; Yamaguchi, M.; Robson, R.M. Filamin-actin interaction. Dissociation of binding from gelation by Ca(II)-activated proteolysis. J. Biol. Chem., 1978, 253, 4036-4042.
    • (1978) J. Biol. Chem , vol.253 , pp. 4036-4042
    • Davies, P.J.1    Wallach, D.2    Willingham, M.C.3    Pastan, I.4    Yamaguchi, M.5    Robson, R.M.6
  • 53
    • 70450254336 scopus 로고    scopus 로고
    • Isoelectric points of multi-domain proteins
    • Carugo, O. Isoelectric points of multi-domain proteins. Bioinformation, 2007, 2, 101-104.
    • (2007) Bioinformation , vol.2 , pp. 101-104
    • Carugo, O.1
  • 55
    • 0026596306 scopus 로고
    • Analysis of the actin-binding domain of alpha-actinin by mutagenesis and demonstration that dystrophin contains a functionally homologous domain
    • Hemmings, L.; Kuhlman, P.A.; Critchley, D.R. Analysis of the actin-binding domain of alpha-actinin by mutagenesis and demonstration that dystrophin contains a functionally homologous domain. J. Cell. Biol., 1992, 116, 1369-1380.
    • (1992) J. Cell. Biol , vol.116 , pp. 1369-1380
    • Hemmings, L.1    Kuhlman, P.A.2    Critchley, D.R.3
  • 56
    • 0026655006 scopus 로고
    • The identification and characterisation of an actin-binding site in alpha-actinin by mutagenesis
    • Kuhlman, P.A.; Hemmings, L.; Critchley, D.R. The identification and characterisation of an actin-binding site in alpha-actinin by mutagenesis. FEBS Lett., 1992, 304, 201-206.
    • (1992) FEBS Lett , vol.304 , pp. 201-206
    • Kuhlman, P.A.1    Hemmings, L.2    Critchley, D.R.3
  • 57
    • 0025734201 scopus 로고
    • Evidence that a 27-residue sequence is the actin-binding site of ABP-120
    • Bresnick, A.R.; Janmey, P.A.; Condeelis, J. Evidence that a 27-residue sequence is the actin-binding site of ABP-120. J. Biol. Chem., 1991, 266, 12989-12993.
    • (1991) J. Biol. Chem , vol.266 , pp. 12989-12993
    • Bresnick, A.R.1    Janmey, P.A.2    Condeelis, J.3
  • 58
    • 0025293017 scopus 로고
    • Identification of a short sequence essential for actin binding by Dictyostelium ABP-120
    • Bresnick, A.R.; Warren, V.; Condeelis, J. Identification of a short sequence essential for actin binding by Dictyostelium ABP-120. J. Biol. Chem., 1990, 265, 9236-9240.
    • (1990) J. Biol. Chem , vol.265 , pp. 9236-9240
    • Bresnick, A.R.1    Warren, V.2    Condeelis, J.3
  • 59
    • 0026595121 scopus 로고
    • Binding sites involved in the interaction of actin with the N-terminal region of dystrophin
    • Levine, B.A.; Moir, A.J.; Patchell, V.B.; Perry, S.V. Binding sites involved in the interaction of actin with the N-terminal region of dystrophin. FEBS Lett., 1992, 298, 44-48.
    • (1992) FEBS Lett , vol.298 , pp. 44-48
    • Levine, B.A.1    Moir, A.J.2    Patchell, V.B.3    Perry, S.V.4
  • 63
    • 0034657791 scopus 로고    scopus 로고
    • The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy
    • Norwood, F.L.; Sutherland-Smith, A.J.; Keep, N.H.; Kendrick-Jones, J. The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy. Structure, 2000, 8, 481-491.
    • (2000) Structure , vol.8 , pp. 481-491
    • Norwood, F.L.1    Sutherland-Smith, A.J.2    Keep, N.H.3    Kendrick-Jones, J.4
  • 64
    • 2442675099 scopus 로고    scopus 로고
    • Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin
    • Sevcik, J.; Urbanikova, L.; Kostan, J.; Janda, L.; Wiche, G. Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin. Eur. J. Biochem., 2004, 271, 1873-1884.
    • (2004) Eur. J. Biochem , vol.271 , pp. 1873-1884
    • Sevcik, J.1    Urbanikova, L.2    Kostan, J.3    Janda, L.4    Wiche, G.5
  • 65
    • 0141631492 scopus 로고    scopus 로고
    • Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4
    • Garcia-Alvarez, B.; Bobkov, A.; Sonnenberg, A.; de Pereda, J.M. Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4. Structure, 2003, 11, 615-625.
    • (2003) Structure , vol.11 , pp. 615-625
    • Garcia-Alvarez, B.1    Bobkov, A.2    Sonnenberg, A.3    de Pereda, J.M.4
  • 66
    • 38349177259 scopus 로고    scopus 로고
    • Crystal structure of the actin-binding domain of alpha-actinin-4 Lys255Glu mutant implicated in focal segmental glomerulosclerosis
    • Lee, S.H.; Weins, A.; Hayes, D.B.; Pollak, M.R.; Dominguez, R. Crystal structure of the actin-binding domain of alpha-actinin-4 Lys255Glu mutant implicated in focal segmental glomerulosclerosis. J. Mol. Biol., 2008, 376, 317-324.
    • (2008) J. Mol. Biol , vol.376 , pp. 317-324
    • Lee, S.H.1    Weins, A.2    Hayes, D.B.3    Pollak, M.R.4    Dominguez, R.5
  • 68
    • 33845543672 scopus 로고    scopus 로고
    • Otopalatodigital syndrome spectrum disorders: Otopalatodigital syndrome types 1 and 2, frontometaphyseal dysplasia and Melnick-Needles syndrome
    • Robertson, S.P. Otopalatodigital syndrome spectrum disorders: otopalatodigital syndrome types 1 and 2, frontometaphyseal dysplasia and Melnick-Needles syndrome. Eur. J. Hum. Genet., 2007, 15, 3-9.
    • (2007) Eur. J. Hum. Genet , vol.15 , pp. 3-9
    • Robertson, S.P.1
  • 69
    • 7944237936 scopus 로고    scopus 로고
    • The many faces of filamin: A versatile molecular scaffold for cell motility and signalling
    • Feng, Y.; Walsh, C.A. The many faces of filamin: a versatile molecular scaffold for cell motility and signalling. Nat. Cell. Biol., 2004, 6, 1034-1038.
    • (2004) Nat. Cell. Biol , vol.6 , pp. 1034-1038
    • Feng, Y.1    Walsh, C.A.2
  • 71


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