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Volumn 24, Issue 2, 2014, Pages 156-164

INF2-mediated severing through actin filament encirclement and disruption

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN;

EID: 84892780734     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2013.12.018     Document Type: Article
Times cited : (48)

References (47)
  • 1
    • 34848927902 scopus 로고    scopus 로고
    • The many faces of actin: Matching assembly factors with cellular structures
    • E.S. Chhabra, and H.N. Higgs The many faces of actin: matching assembly factors with cellular structures Nat. Cell Biol. 9 2007 1110 1121
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1110-1121
    • Chhabra, E.S.1    Higgs, H.N.2
  • 2
    • 0742305302 scopus 로고    scopus 로고
    • A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin
    • J.B. Moseley, I. Sagot, A.L. Manning, Y. Xu, M.J. Eck, D. Pellman, and B.L. Goode A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin Mol. Biol. Cell 15 2004 896 907
    • (2004) Mol. Biol. Cell , vol.15 , pp. 896-907
    • Moseley, J.B.1    Sagot, I.2    Manning, A.L.3    Xu, Y.4    Eck, M.J.5    Pellman, D.6    Goode, B.L.7
  • 3
    • 60749122102 scopus 로고    scopus 로고
    • Actin nucleation and elongation factors: Mechanisms and interplay
    • M.A. Chesarone, and B.L. Goode Actin nucleation and elongation factors: mechanisms and interplay Curr. Opin. Cell Biol. 21 2009 28 37
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 28-37
    • Chesarone, M.A.1    Goode, B.L.2
  • 4
    • 67749135871 scopus 로고    scopus 로고
    • Review of the mechanism of processive actin filament elongation by formins
    • A.S. Paul, and T.D. Pollard Review of the mechanism of processive actin filament elongation by formins Cell Motil. Cytoskeleton 66 2009 606 617
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 606-617
    • Paul, A.S.1    Pollard, T.D.2
  • 5
    • 11144281883 scopus 로고    scopus 로고
    • Phylogenetic analysis of the formin homology 2 domain
    • H.N. Higgs, and K.J. Peterson Phylogenetic analysis of the formin homology 2 domain Mol. Biol. Cell 16 2005 1 13
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1-13
    • Higgs, H.N.1    Peterson, K.J.2
  • 6
    • 84856279315 scopus 로고    scopus 로고
    • The C terminus of formin FMNL3 accelerates actin polymerization and contains a WH2 domain-like sequence that binds both monomers and filament barbed ends
    • E.G. Heimsath Jr., and H.N. Higgs The C terminus of formin FMNL3 accelerates actin polymerization and contains a WH2 domain-like sequence that binds both monomers and filament barbed ends J. Biol. Chem. 287 2012 3087 3098
    • (2012) J. Biol. Chem. , vol.287 , pp. 3087-3098
    • Heimsath, Jr.E.G.1    Higgs, H.N.2
  • 8
    • 33748745132 scopus 로고    scopus 로고
    • INF2 Is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization
    • E.S. Chhabra, and H.N. Higgs INF2 Is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization J. Biol. Chem. 281 2006 26754 26767
    • (2006) J. Biol. Chem. , vol.281 , pp. 26754-26767
    • Chhabra, E.S.1    Higgs, H.N.2
  • 9
    • 84055217451 scopus 로고    scopus 로고
    • Splice variant-specific cellular function of the formin INF2 in maintenance of Golgi architecture
    • V. Ramabhadran, F. Korobova, G.J. Rahme, and H.N. Higgs Splice variant-specific cellular function of the formin INF2 in maintenance of Golgi architecture Mol. Biol. Cell 22 2011 4822 4833
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4822-4833
    • Ramabhadran, V.1    Korobova, F.2    Rahme, G.J.3    Higgs, H.N.4
  • 10
    • 78650666890 scopus 로고    scopus 로고
    • Formin INF2 regulates MAL-mediated transport of Lck to the plasma membrane of human T lymphocytes
    • L. Andrés-Delgado, O.M. Antón, R. Madrid, J.A. Byrne, and M.A. Alonso Formin INF2 regulates MAL-mediated transport of Lck to the plasma membrane of human T lymphocytes Blood 116 2010 5919 5929
    • (2010) Blood , vol.116 , pp. 5919-5929
    • Andrés-Delgado, L.1    Antón, O.M.2    Madrid, R.3    Byrne, J.A.4    Alonso, M.A.5
  • 12
    • 67650566835 scopus 로고    scopus 로고
    • INF2 is an endoplasmic reticulum-associated formin protein
    • E.S. Chhabra, V. Ramabhadran, S.A. Gerber, and H.N. Higgs INF2 is an endoplasmic reticulum-associated formin protein J. Cell Sci. 122 2009 1430 1440
    • (2009) J. Cell Sci. , vol.122 , pp. 1430-1440
    • Chhabra, E.S.1    Ramabhadran, V.2    Gerber, S.A.3    Higgs, H.N.4
  • 13
    • 84872769447 scopus 로고    scopus 로고
    • An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2
    • F. Korobova, V. Ramabhadran, and H.N. Higgs An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2 Science 339 2013 464 467
    • (2013) Science , vol.339 , pp. 464-467
    • Korobova, F.1    Ramabhadran, V.2    Higgs, H.N.3
  • 16
    • 0026340941 scopus 로고
    • Characterization of actin filament severing by actophorin from Acanthamoeba castellanii
    • S.K. Maciver, H.G. Zot, and T.D. Pollard Characterization of actin filament severing by actophorin from Acanthamoeba castellanii J. Cell Biol. 115 1991 1611 1620
    • (1991) J. Cell Biol. , vol.115 , pp. 1611-1620
    • Maciver, S.K.1    Zot, H.G.2    Pollard, T.D.3
  • 17
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor with G- and F-actin
    • S.M. Hayden, P.S. Miller, A. Brauweiler, and J.R. Bamburg Analysis of the interactions of actin depolymerizing factor with G- and F-actin Biochemistry 32 1993 9994 10004
    • (1993) Biochemistry , vol.32 , pp. 9994-10004
    • Hayden, S.M.1    Miller, P.S.2    Brauweiler, A.3    Bamburg, J.R.4
  • 18
    • 77950022821 scopus 로고    scopus 로고
    • How cofilin severs an actin filament
    • E.M. De La Cruz How cofilin severs an actin filament Biophys. Rev. 1 2009 51 59
    • (2009) Biophys. Rev. , vol.1 , pp. 51-59
    • De La Cruz, E.M.1
  • 19
    • 0037080339 scopus 로고    scopus 로고
    • Hydrolysis of ATP by polymerized actin depends on the bound divalent cation but not profilin
    • L. Blanchoin, and T.D. Pollard Hydrolysis of ATP by polymerized actin depends on the bound divalent cation but not profilin Biochemistry 41 2002 597 602
    • (2002) Biochemistry , vol.41 , pp. 597-602
    • Blanchoin, L.1    Pollard, T.D.2
  • 20
    • 0033060250 scopus 로고    scopus 로고
    • Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments
    • L. Blanchoin, and T.D. Pollard Mechanism of interaction of Acanthamoeba actophorin (ADF/Cofilin) with actin filaments J. Biol. Chem. 274 1999 15538 15546
    • (1999) J. Biol. Chem. , vol.274 , pp. 15538-15546
    • Blanchoin, L.1    Pollard, T.D.2
  • 22
    • 0023727152 scopus 로고
    • The hydrolysis of ATP that accompanies actin polymerization is essentially irreversible
    • M.F. Carlier, D. Pantaloni, J.A. Evans, P.K. Lambooy, E.D. Korn, and M.R. Webb The hydrolysis of ATP that accompanies actin polymerization is essentially irreversible FEBS Lett. 235 1988 211 214
    • (1988) FEBS Lett. , vol.235 , pp. 211-214
    • Carlier, M.F.1    Pantaloni, D.2    Evans, J.A.3    Lambooy, P.K.4    Korn, E.D.5    Webb, M.R.6
  • 23
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • A. McGough, B. Pope, W. Chiu, and A. Weeds Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function J. Cell Biol. 138 1997 771 781
    • (1997) J. Cell Biol. , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 26
    • 0032516848 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction of actin-depolymerizing factor (ADF)/cofilin with G- and F-actins. Comparison of plant and human ADFs and effect of phosphorylation
    • F. Ressad, D. Didry, G.X. Xia, Y. Hong, N.H. Chua, D. Pantaloni, and M.F. Carlier Kinetic analysis of the interaction of actin-depolymerizing factor (ADF)/cofilin with G- and F-actins. Comparison of plant and human ADFs and effect of phosphorylation J. Biol. Chem. 273 1998 20894 20902
    • (1998) J. Biol. Chem. , vol.273 , pp. 20894-20902
    • Ressad, F.1    Didry, D.2    Xia, G.X.3    Hong, Y.4    Chua, N.H.5    Pantaloni, D.6    Carlier, M.F.7
  • 27
    • 30744462047 scopus 로고    scopus 로고
    • Cooperative effects of cofilin (ADF) on actin structure suggest allosteric mechanism of cofilin function
    • A.A. Bobkov, A. Muhlrad, D.A. Pavlov, K. Kokabi, A. Yilmaz, and E. Reisler Cooperative effects of cofilin (ADF) on actin structure suggest allosteric mechanism of cofilin function J. Mol. Biol. 356 2006 325 334
    • (2006) J. Mol. Biol. , vol.356 , pp. 325-334
    • Bobkov, A.A.1    Muhlrad, A.2    Pavlov, D.A.3    Kokabi, K.4    Yilmaz, A.5    Reisler, E.6
  • 29
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin
    • E. Andrianantoandro, and T.D. Pollard Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin Mol. Cell 24 2006 13 23
    • (2006) Mol. Cell , vol.24 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 30
    • 12544252575 scopus 로고    scopus 로고
    • Cofilin binding to muscle and non-muscle actin filaments: Isoform-dependent cooperative interactions
    • E.M. De La Cruz Cofilin binding to muscle and non-muscle actin filaments: isoform-dependent cooperative interactions J. Mol. Biol. 346 2005 557 564
    • (2005) J. Mol. Biol. , vol.346 , pp. 557-564
    • De La Cruz, E.M.1
  • 31
    • 84872043614 scopus 로고    scopus 로고
    • FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation
    • M.E. Thompson, E.G. Heimsath, T.J. Gauvin, H.N. Higgs, and F.J. Kull FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation Nat. Struct. Mol. Biol. 20 2013 111 118
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 111-118
    • Thompson, M.E.1    Heimsath, E.G.2    Gauvin, T.J.3    Higgs, H.N.4    Kull, F.J.5
  • 32
    • 13444280218 scopus 로고    scopus 로고
    • Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
    • T. Otomo, D.R. Tomchick, C. Otomo, S.C. Panchal, M. Machius, and M.K. Rosen Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain Nature 433 2005 488 494
    • (2005) Nature , vol.433 , pp. 488-494
    • Otomo, T.1    Tomchick, D.R.2    Otomo, C.3    Panchal, S.C.4    Machius, M.5    Rosen, M.K.6
  • 33
    • 0024297288 scopus 로고
    • Probing the mechanism of ATP hydrolysis on F-actin using vanadate and the structural analogs of phosphate BeF-3 and A1F-4
    • C. Combeau, and M.F. Carlier Probing the mechanism of ATP hydrolysis on F-actin using vanadate and the structural analogs of phosphate BeF-3 and A1F-4 J. Biol. Chem. 263 1988 17429 17436
    • (1988) J. Biol. Chem. , vol.263 , pp. 17429-17436
    • Combeau, C.1    Carlier, M.F.2
  • 34
    • 84876041581 scopus 로고    scopus 로고
    • Biophysics of actin filament severing by cofilin
    • W.A. Elam, H. Kang, and E.M. De la Cruz Biophysics of actin filament severing by cofilin FEBS Lett. 587 2013 1215 1219
    • (2013) FEBS Lett. , vol.587 , pp. 1215-1219
    • Elam, W.A.1    Kang, H.2    De La Cruz, E.M.3
  • 35
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture
    • Y.W. Xu, J.B. Moseley, I. Sagot, F. Poy, D. Pellman, B.L. Goode, and M.J. Eck Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture Cell 116 2004 711 723
    • (2004) Cell , vol.116 , pp. 711-723
    • Xu, Y.W.1    Moseley, J.B.2    Sagot, I.3    Poy, F.4    Pellman, D.5    Goode, B.L.6    Eck, M.J.7
  • 36
    • 33646867122 scopus 로고    scopus 로고
    • Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2
    • E.S. Harris, I. Rouiller, D. Hanein, and H.N. Higgs Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2 J. Biol. Chem. 281 2006 14383 14392
    • (2006) J. Biol. Chem. , vol.281 , pp. 14383-14392
    • Harris, E.S.1    Rouiller, I.2    Hanein, D.3    Higgs, H.N.4
  • 37
  • 39
    • 28044470753 scopus 로고    scopus 로고
    • Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly
    • D. Chereau, F. Kerff, P. Graceffa, Z. Grabarek, K. Langsetmo, and R. Dominguez Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly Proc. Natl. Acad. Sci. USA 102 2005 16644 16649
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16644-16649
    • Chereau, D.1    Kerff, F.2    Graceffa, P.3    Grabarek, Z.4    Langsetmo, K.5    Dominguez, R.6
  • 41
    • 0031879577 scopus 로고    scopus 로고
    • Determination of the gelsolin binding site on F-actin: Implications for severing and capping
    • A. McGough, W. Chiu, and M. Way Determination of the gelsolin binding site on F-actin: implications for severing and capping Biophys. J. 74 1998 764 772
    • (1998) Biophys. J. , vol.74 , pp. 764-772
    • McGough, A.1    Chiu, W.2    Way, M.3
  • 42
    • 0030564835 scopus 로고    scopus 로고
    • Cooperativity in F-actin: Binding of gelsolin at the barbed end affects structure and dynamics of the whole filament
    • E. Prochniewicz, Q.N. Zhang, P.A. Janmey, and D.D. Thomas Cooperativity in F-actin: binding of gelsolin at the barbed end affects structure and dynamics of the whole filament J. Mol. Biol. 260 1996 756 766
    • (1996) J. Mol. Biol. , vol.260 , pp. 756-766
    • Prochniewicz, E.1    Zhang, Q.N.2    Janmey, P.A.3    Thomas, D.D.4
  • 43
    • 0028920157 scopus 로고
    • Structural dynamics of F-actin: II. Cooperativity in structural transitions
    • A. Orlova, E. Prochniewicz, and E.H. Egelman Structural dynamics of F-actin: II. Cooperativity in structural transitions J. Mol. Biol. 245 1995 598 607
    • (1995) J. Mol. Biol. , vol.245 , pp. 598-607
    • Orlova, A.1    Prochniewicz, E.2    Egelman, E.H.3
  • 44
    • 0034614942 scopus 로고    scopus 로고
    • Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion
    • A.Y. Chan, M. Bailly, N. Zebda, J.E. Segall, and J.S. Condeelis Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion J. Cell Biol. 148 2000 531 542
    • (2000) J. Cell Biol. , vol.148 , pp. 531-542
    • Chan, A.Y.1    Bailly, M.2    Zebda, N.3    Segall, J.E.4    Condeelis, J.S.5
  • 46
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • S.J. Ludtke, P.R. Baldwin, and W. Chiu EMAN: semiautomated software for high-resolution single-particle reconstructions J. Struct. Biol. 128 1999 82 97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 47
    • 33845305513 scopus 로고    scopus 로고
    • The iterative helical real space reconstruction method: Surmounting the problems posed by real polymers
    • E.H. Egelman The iterative helical real space reconstruction method: surmounting the problems posed by real polymers J. Struct. Biol. 157 2007 83 94
    • (2007) J. Struct. Biol. , vol.157 , pp. 83-94
    • Egelman, E.H.1


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