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Volumn 67, Issue 5, 2010, Pages 286-296

Characterization of L-plastin Interaction with beta integrin and its regulation by micro-calpain

Author keywords

Calpain; Integrin; Interaction; Plastin fimbrin

Indexed keywords

ACTIN BINDING PROTEIN; BETA1 INTEGRIN; BETA2 INTEGRIN; CALCIUM; CALPAIN 1; L PLASTIN; MEMBRANE PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 77953563048     PISSN: 19493584     EISSN: 19493592     Source Type: Journal    
DOI: 10.1002/cm.20442     Document Type: Article
Times cited : (22)

References (64)
  • 1
    • 0028964234 scopus 로고
    • Cytoskeletal rearrangements and the functional role of T-plastin during entry of Shigella Flexneri into Hela cells
    • Adam T, Arpin M, Prevost MC, Gounon P, Sansonetti PJ. 1995. Cytoskeletal rearrangements and the functional role of T-plastin during entry of Shigella Flexneri into Hela cells. J Cell Biol 129:367-381.
    • (1995) J Cell Biol , vol.129 , pp. 367-381
    • Adam, T.1    Arpin, M.2    Prevost, M.C.3    Gounon, P.4    Sansonetti, P.J.5
  • 2
    • 0028587210 scopus 로고
    • Functional differences between l- and t-plastin isoforms
    • Arpin M, Friederich E, Algrain M, Vernel F, Louvard D. 1994. Functional differences between l- and t-plastin isoforms. J Cell Biol 127(6, Part 2): 1995-2008.
    • (1994) J Cell Biol , vol.127 , Issue.6 PART 2 , pp. 1995-2008
    • Arpin, M.1    Friederich, E.2    Algrain, M.3    Vernel, F.4    Louvard, D.5
  • 3
    • 0027970388 scopus 로고
    • Characterization of neural cell adhesion sites: Point contacts are the sites of interaction between integrins and the cytoskeleton in PC12 cells
    • Arregui CO, Carbonetto S, McKerracher L. 1994. Characterization of neural cell adhesion sites: Point contacts are the sites of interaction between integrins and the cytoskeleton in PC12 cells. J Neurosci 14(11, Part 2):6967-6977
    • (1994) J Neurosci , vol.14 , Issue.11 PART 2 , pp. 6967-6977
    • Arregui, C.O.1    Carbonetto, S.2    McKerracher, L.3
  • 6
    • 0019313223 scopus 로고
    • Fimbrin, a new microfilament-associated protein present in microvilli and other cell surface structures
    • Bretscher A, Weber K. 1980. Fimbrin, a new microfilament-associated protein present in microvilli and other cell surface structures. J Cell Biol 86(1): 335-340.
    • (1980) J Cell Biol , vol.86 , Issue.1 , pp. 335-340
    • Bretscher, A.1    Weber, K.2
  • 7
    • 0020460868 scopus 로고
    • Nonerythrocyte spectrins: Actinmembrane attachment proteins occurring in many cell types
    • Burridge K, Kelly T, Mangeat P. 1982. Nonerythrocyte spectrins: Actinmembrane attachment proteins occurring in many cell types. J Cell Biol 95(2, Part 1):478-486.
    • (1982) J Cell Biol , vol.95 , Issue.2 PART 1 , pp. 478-486
    • Burridge, K.1    Kelly, T.2    Mangeat, P.3
  • 8
    • 33745482350 scopus 로고    scopus 로고
    • Inhibition of calpain stabilises podosomes and impairs dendritic cell motility
    • Calle Y, Carragher NO, Thrasher AJ, Jones GE. 2006. Inhibition of calpain stabilises podosomes and impairs dendritic cell motility. J Cell Sci 119(Pt 11):2375-2385.
    • (2006) J Cell Sci , vol.119 , Issue.PART 11 , pp. 2375-2385
    • Calle, Y.1    Carragher, N.O.2    Thrasher, A.J.3    Jones, G.E.4
  • 10
    • 0033598182 scopus 로고    scopus 로고
    • Integrating the actin and vimentin cytoskeletons. Adhesion-dependent formation of fimbrin-vimentin complexes in macrophages
    • Correia I, Chu D, Chou YH, Goldman RD, Matsudaira P. 1999. Integrating the actin and vimentin cytoskeletons. Adhesion-dependent formation of fimbrin-vimentin complexes in macrophages. J Cell Biol 146(4):831-842.
    • (1999) J Cell Biol , vol.146 , Issue.4 , pp. 831-842
    • Correia, I.1    Chu, D.2    Chou, Y.H.3    Goldman, R.D.4    Matsudaira, P.5
  • 11
    • 0036889845 scopus 로고    scopus 로고
    • Transient expression of the t-isoform of plastins/fimbrin in the stereocilia of developing auditory hair cells
    • Daudet N, Lebart MC. 2002. Transient expression of the t-isoform of plastins/ fimbrin in the stereocilia of developing auditory hair cells. Cell Motil Cytoskeleton 53(4):326-336.
    • (2002) Cell Motil Cytoskeleton , vol.53 , Issue.4 , pp. 326-336
    • Daudet, N.1    Lebart, M.C.2
  • 13
    • 22144496125 scopus 로고    scopus 로고
    • Plastins: Versatile modulators of actin organization in (patho)physiological cellular processes
    • Delanote V, Vandekerckhove J, Gettemans J. 2005b. Plastins: Versatile modulators of actin organization in (patho)physiological cellular processes. Acta Pharmacol Sin 26(7):769-779.
    • (2005) Acta Pharmacol Sin , vol.26 , Issue.7 , pp. 769-779
    • Delanote, V.1    Vandekerckhove, J.2    Gettemans, J.3
  • 14
    • 75149169810 scopus 로고    scopus 로고
    • An alpaca single-domain antibody blocks filopodia formation by obstructing L-plastin-mediated F-actin bundling
    • Delanote V, Vanloo B, Catillon M, Friederich E, Vandekerckhove J, Gettemans J. 2010. An alpaca single-domain antibody blocks filopodia formation by obstructing L-plastin-mediated F-actin bundling. FASEB J 24(1):105-118.
    • (2010) FASEB J , vol.24 , Issue.1 , pp. 105-118
    • Delanote, V.1    Vanloo, B.2    Catillon, M.3    Friederich, E.4    Vandekerckhove, J.5    Gettemans, J.6
  • 15
    • 0037078326 scopus 로고    scopus 로고
    • 2+ changes and calpain activation are required for β integrin-accelerated phagocytosis by human neutrophils
    • 2+ changes and calpain activation are required for β integrin-accelerated phagocytosis by human neutrophils. J Cell Biol 159(1):181-189.
    • (2002) J Cell Biol , vol.159 , Issue.1 , pp. 181-189
    • Dewitt, S.1    Hallett, M.B.2
  • 16
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti JM, Campbell KP. 1993. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol 122(4):809-823.
    • (1993) J Cell Biol , vol.122 , Issue.4 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 17
    • 0037512351 scopus 로고    scopus 로고
    • Macrophage podosomes assemble at the leading lamella by growth and fragmentation
    • Evans JG, Correia I, Krasavina O, Watson N, Matsudaira P. 2003. Macrophage podosomes assemble at the leading lamella by growth and fragmentation. J Cell Biol 161(4):697-705.
    • (2003) J Cell Biol , vol.161 , Issue.4 , pp. 697-705
    • Evans, J.G.1    Correia, I.2    Krasavina, O.3    Watson, N.4    Matsudaira, P.5
  • 18
    • 29244445476 scopus 로고    scopus 로고
    • Calpain 1-c filamin interaction in muscle cells: A possible in situ regulation by PKC-a
    • Fabrice R, Carole JN, Anne M, Dieter F, Yves B. 2006. Calpain 1-c filamin interaction in muscle cells: A possible in situ regulation by PKC-a. Int J Biochem Cell Biol 38(3):404-413.
    • (2006) Int J Biochem Cell Biol , vol.38 , Issue.3 , pp. 404-413
    • Fabrice, R.1    Carole, J.N.2    Anne, M.3    Dieter, F.4    Yves, B.5
  • 19
    • 26244434596 scopus 로고    scopus 로고
    • Regulating cell migration: Calpains make the cut
    • Franco SJ, Huttenlocher A. 2005. Regulating cell migration: Calpains make the cut. J Cell Sci 118(Pt 17):3829-3838.
    • (2005) J Cell Sci , vol.118 , Issue.PART 17 , pp. 3829-3838
    • Franco, S.J.1    Huttenlocher, A.2
  • 21
    • 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 β4.
    • Garcia-Alvarez B, Bobkov A, Sonnenberg A, de Pereda JM. 2003. Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin β4. Structure (Camb) 11(6):615-625.
    • (2003) Structure (Camb) , vol.11 , Issue.6 , pp. 615-625
    • Garcia-Alvarez, B.1    Bobkov, A.2    Sonnenberg, A.3    De Pereda, J.M.4
  • 22
  • 23
    • 17244373549 scopus 로고    scopus 로고
    • Actin-filament cross-linking protein T-plastin increases Arp2/3-mediated actin-based movement
    • Giganti A, Plastino J, Janji B, Van Troys M, Lentz D, Ampe C, Sykes C, Friederich E. 2005. Actin-filament cross-linking protein T-plastin increases Arp2/3-mediated actin-based movement. J Cell Sci 118(Pt 6):1255-1265.
    • (2005) J Cell Sci , vol.118 , Issue.PART 6 , pp. 1255-1265
    • Giganti, A.1    Plastino, J.2    Janji, B.3    Van Troys, M.4    Lentz, D.5    Ampe, C.6    Sykes, C.7    Friederich, E.8
  • 24
    • 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(1):46-54.
    • (2002) Trends Cell Biol , vol.12 , Issue.1 , pp. 46-54
    • Glading, A.1    Lauffenburger, D.A.2    Wells, A.3
  • 28
    • 0025014759 scopus 로고
    • Expression and function of chicken integrin b 1 subunit and its cytoplasmic domain mutants in mouse NIH 3T3 cells
    • Hayashi Y, Haimovich B, Reszka A, Boettiger D, Horwitz A. 1990. Expression and function of chicken integrin b 1 subunit and its cytoplasmic domain mutants in mouse NIH 3T3 cells. J Cell Biol 110(1):175-184.
    • (1990) J Cell Biol , vol.110 , Issue.1 , pp. 175-184
    • Hayashi, Y.1    Haimovich, B.2    Reszka, A.3    Boettiger, D.4    Horwitz, A.5
  • 29
    • 33744536569 scopus 로고    scopus 로고
    • Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promotes its targeting to sites of actin assembly in cells
    • Janji B, Giganti A, De Corte V, Catillon M, Bruyneel E, Lentz D, Plastino J, Gettemans J, Friederich E. 2006. Phosphorylation on Ser5 increases the F-actin-binding activity of L-plastin and promotes its targeting to sites of actin assembly in cells. J Cell Sci 119(Pt 9):1947-1960.
    • (2006) J Cell Sci , vol.119 , Issue.PART 9 , pp. 1947-1960
    • Janji, B.1    Giganti, A.2    De Corte, V.3    Catillon, M.4    Bruyneel, E.5    Lentz, D.6    Plastino, J.7    Gettemans, J.8    Friederich, E.9
  • 30
    • 0032483008 scopus 로고    scopus 로고
    • A role for the actin-bundling protein L-plastin in the regulation of leukocyte integrin function
    • Jones SL, Wang J, Turck CW, Brown EJ. 1998. A role for the actin-bundling protein L-plastin in the regulation of leukocyte integrin function. Proc Natl Acad Sci USA 95(16):9331-9336.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.16 , pp. 9331-9336
    • Jones, S.L.1    Wang, J.2    Turck, C.W.3    Brown, E.J.4
  • 31
    • 13844253573 scopus 로고    scopus 로고
    • Identification of the β1-integrin binding site on a-actinin by cryoelectron microscopy
    • Kelly DF, Taylor KA. 2005. Identification of the β1-integrin binding site on a-actinin by cryoelectron microscopy. J Struct Biol 149(3):290-302.
    • (2005) J Struct Biol , vol.149 , Issue.3 , pp. 290-302
    • Kelly, D.F.1    Taylor, K.A.2
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227(259):680-685.
    • (1970) Nature , vol.227 , Issue.259 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 33746155723 scopus 로고    scopus 로고
    • Calpain involvement in the remodeling of cytoskeletal anchorage complexes
    • Lebart MC, Benyamin Y. 2006. Calpain involvement in the remodeling of cytoskeletal anchorage complexes. FEBS J 273(15):3415-3426.
    • (2006) FEBS J , vol.273 , Issue.15 , pp. 3415-3426
    • Lebart, M.C.1    Benyamin, Y.2
  • 36
    • 0027416724 scopus 로고
    • Further characterization of the a-actinin-actin interface and comparison with filamin-binding sites on actin
    • Lebart MC, Mejean C, Roustan C, Benyamin Y. 1993. Further characterization of the a-actinin-actin interface and comparison with filamin-binding sites on actin. J Biol Chem 268(8):5642-5648.
    • (1993) J Biol Chem , vol.268 , Issue.8 , pp. 5642-5648
    • Lebart, M.C.1    Mejean, C.2    Roustan, C.3    Benyamin, Y.4
  • 37
    • 0028787396 scopus 로고
    • Actin interaction with purified dystrophin from electric organ of torpedo marmorata: Possible resemblance with filamin actin interface
    • Lebart MC, Casanova D, Benyamin Y. 1995. Actin interaction with purified dystrophin from electric organ of torpedo marmorata: Possible resemblance with filamin actin interface. J Muscle Res Cell Motil 16(5):543-552.
    • (1995) J Muscle Res Cell Motil , vol.16 , Issue.5 , pp. 543-552
    • Lebart, M.C.1    Casanova, D.2    Benyamin, Y.3
  • 38
    • 1542297717 scopus 로고    scopus 로고
    • Biochemical characterization of the L-plastin-actin interaction shows a resemblance with that of a-actinin and allows a distinction to be made between the two actin-binding domains of the molecule
    • Lebart MC, Hubert F, Boiteau C, Venteo S, Roustan C, Benyamin Y. 2004. Biochemical characterization of the L-plastin-actin interaction shows a resemblance with that of a-actinin and allows a distinction to be made between the two actin-binding domains of the molecule. Biochemistry 43(9):2428-2437.
    • (2004) Biochemistry , vol.43 , Issue.9 , pp. 2428-2437
    • Lebart, M.C.1    Hubert, F.2    Boiteau, C.3    Venteo, S.4    Roustan, C.5    Benyamin, Y.6
  • 39
    • 0025212744 scopus 로고
    • Correction of the N-terminal sequences of the human plastin isoforms by using anchored polymerase chain reaction: Identification of a potential calcium-binding domain
    • Lin CS, Aebersold RH, Leavitt J. 1990. Correction of the N-terminal sequences of the human plastin isoforms by using anchored polymerase chain reaction: Identification of a potential calcium-binding domain. Mol Cell Biol 10(4):1818-1821.
    • (1990) Mol Cell Biol , vol.10 , Issue.4 , pp. 1818-1821
    • Lin, C.S.1    Aebersold, R.H.2    Leavitt, J.3
  • 40
    • 0027511422 scopus 로고
    • Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells
    • Lin CS, Park T, Chen ZP, Leavitt J. 1993. Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells. J Biol Chem 268(4):2781-2792.
    • (1993) J Biol Chem , vol.268 , Issue.4 , pp. 2781-2792
    • Lin, C.S.1    Park, T.2    Chen, Z.P.3    Leavitt, J.4
  • 41
    • 0032442866 scopus 로고    scopus 로고
    • Analysis and mapping of plastin phosphorylation
    • Lin CS, Lau A, Lue TF. 1998. Analysis and mapping of plastin phosphorylation. DNA Cell Biol 17(12):1041-1046.
    • (1998) DNA Cell Biol , vol.17 , Issue.12 , pp. 1041-1046
    • Lin, C.S.1    Lau, A.2    Lue, T.F.3
  • 42
    • 0033965092 scopus 로고    scopus 로고
    • Upregulation of L-plastin gene by testosterone in breast and prostate cancer cells: Identification of three cooperative androgen receptor-binding sequences
    • Lin CS, Lau A, Yeh CC, Chang CH, Lue TF. 2000. Upregulation of L-plastin gene by testosterone in breast and prostate cancer cells: Identification of three cooperative androgen receptor-binding sequences. DNA Cell Biol 19(1):1-7.
    • (2000) DNA Cell Biol , vol.19 , Issue.1 , pp. 1-7
    • Lin, C.S.1    Lau, A.2    Yeh, C.C.3    Chang, C.H.4    Lue, T.F.5
  • 43
    • 0033731119 scopus 로고    scopus 로고
    • Integrin cytoplasmic domainbinding proteins
    • Liu S, Calderwood DA, Ginsberg MH. 2000. Integrin cytoplasmic domainbinding proteins. J Cell Sci 113 (Part 20):3563-3571.
    • (2000) J Cell Sci , vol.113 , Issue.PART 20 , pp. 3563-3571
    • Liu, S.1    Calderwood, D.A.2    Ginsberg, M.H.3
  • 44
    • 0032483459 scopus 로고    scopus 로고
    • Filamin binds to the cytoplasmic domain of the β1-integrin. Identification of amino acids responsible for this interaction
    • Loo DT, Kanner SB, Aruffo A. 1998. Filamin binds to the cytoplasmic domain of the β1-integrin. Identification of amino acids responsible for this interaction. J Biol Chem 273(36):23304-23312.
    • (1998) J Biol Chem , vol.273 , Issue.36 , pp. 23304-23312
    • Loo, D.T.1    Kanner, S.B.2    Aruffo, A.3
  • 45
    • 0023123876 scopus 로고
    • Rous sarcoma virus-transformed fibroblasts and cells of monocytic origin display a peculiar dot-like organization of cytoskeletal proteins involved in microfilament-membrane interactions
    • Marchisio PC, Cirillo D, Teti A, Zambonin-Zallone A, Tarone G. 1987. Rous sarcoma virus-transformed fibroblasts and cells of monocytic origin display a peculiar dot-like organization of cytoskeletal proteins involved in microfilament-membrane interactions. Exp Cell Res 169(1):202-214.
    • (1987) Exp Cell Res , vol.169 , Issue.1 , pp. 202-214
    • Marchisio, P.C.1    Cirillo, D.2    Teti, A.3    Zambonin-Zallone, A.4    Tarone, G.5
  • 46
    • 0027324435 scopus 로고
    • Fimbrin localized to an insoluble cytoskeletal fraction is constitutively phosphorylated on its headpiece domain in adherent macrophages
    • Messier JM, Shaw LM, Chafel M, Matsudaira P, Mercurio AM. 1993. Fimbrin localized to an insoluble cytoskeletal fraction is constitutively phosphorylated on its headpiece domain in adherent macrophages. Cell Motil Cytoskeleton 25(3):223-233.
    • (1993) Cell Motil Cytoskeleton , vol.25 , Issue.3 , pp. 223-233
    • Messier, J.M.1    Shaw, L.M.2    Chafel, M.3    Matsudaira, P.4    Mercurio, A.M.5
  • 47
    • 0025350798 scopus 로고
    • Immunological comparison between albumins of three species of mice (genus Mus)
    • Montgelard C, Benyamin Y, Roustan C. 1990. Immunological comparison between albumins of three species of mice (genus Mus). Experientia 46(3): 303-307.
    • (1990) Experientia , vol.46 , Issue.3 , pp. 303-307
    • Montgelard, C.1    Benyamin, Y.2    Roustan, C.3
  • 48
    • 0347087509 scopus 로고    scopus 로고
    • Regulation of β1C and β1A integrin expression in prostate carcinoma cells
    • Moro L, Perlino E, Marra E, Languino LR, Greco M. 2004. Regulation of β1C and β1A integrin expression in prostate carcinoma cells. J Biol Chem 279(3):1692-1702.
    • (2004) J Biol Chem , vol.279 , Issue.3 , pp. 1692-1702
    • Moro, L.1    Perlino, E.2    Marra, E.3    Languino, L.R.4    Greco, M.5
  • 49
    • 0033565261 scopus 로고    scopus 로고
    • PKCa regulates β1 integrin-dependent cell motility through association and control of integrin traffic
    • Ng T, Shima D, Squire A, Bastiaens PI, Gschmeissner S, Humphries MJ, Parker PJ. 1999. PKCa regulates β1 integrin-dependent cell motility through association and control of integrin traffic. EMBO J 18(14): 3909-3923.
    • (1999) EMBO J , vol.18 , Issue.14 , pp. 3909-3923
    • Ng, T.1    Shima, D.2    Squire, A.3    Bastiaens, P.I.4    Gschmeissner, S.5    Humphries, M.J.6    Parker, P.J.7
  • 50
    • 0025291522 scopus 로고
    • An interaction between a-actinin and the β 1 integrin subunit in vitro
    • Otey CA, Pavalko FM, Burridge K. 1990. An interaction between a-actinin and the β 1 integrin subunit in vitro. J Cell Biol 111(2):721-729.
    • (1990) J Cell Biol , vol.111 , Issue.2 , pp. 721-729
    • Otey, C.A.1    Pavalko, F.M.2    Burridge, K.3
  • 51
    • 0027454485 scopus 로고
    • Mapping of the aactinin binding site within the β-1 integrin cytoplasmic domain
    • Otey CA, Vasquez GB, Burridge K, Erickson BW. 1993. Mapping of the aactinin binding site within the β-1 integrin cytoplasmic domain. J Biol Chem 268(28):21193-21197.
    • (1993) J Biol Chem , vol.268 , Issue.28 , pp. 21193-21197
    • Otey, C.A.1    Vasquez, G.B.2    Burridge, K.3    Erickson, B.W.4
  • 52
    • 49549096455 scopus 로고    scopus 로고
    • BioImageXD solfware in bact analysis of integrin interactions
    • Pahajoki KA, Kankaanpää PP, Heino JJ. 2008. BioImageXD solfware in bact analysis of integrin interactions. Microsc Microanal 14:596-597.
    • (2008) Microsc Microanal , vol.14 , pp. 596-597
    • Pahajoki, K.A.1    Kankaanpää, P.P.2    Heino, J.J.3
  • 53
    • 0027317933 scopus 로고
    • Activation of human neutrophils induces an interaction between the integrin-b-2-subunit (CD18) and the actin binding protein a-actinin
    • Pavalko FM, Laroche SM. 1993. Activation of human neutrophils induces an interaction between the integrin-b-2-subunit (CD18) and the actin binding protein a-actinin. J Immunol 151(7):3795-3807.
    • (1993) J Immunol , vol.151 , Issue.7 , pp. 3795-3807
    • Pavalko, F.M.1    Laroche, S.M.2
  • 54
    • 0032860769 scopus 로고    scopus 로고
    • Calpain cleavage of integrin b cytoplasmic domains
    • Pfaff M, Du X, Ginsberg MH. 1999. Calpain cleavage of integrin b cytoplasmic domains. FEBS Lett 460(1):17-22.
    • (1999) FEBS Lett , vol.460 , Issue.1 , pp. 17-22
    • Pfaff, M.1    Du, X.2    Ginsberg, M.H.3
  • 55
  • 56
    • 0032509204 scopus 로고    scopus 로고
    • Cytoskeletal interactions with the leukocyte integrin b2 cytoplasmic tail. Activation-dependent regulation of associations with talin and a-actinin
    • Sampath R, Gallagher PJ, Pavalko FM. 1998. Cytoskeletal interactions with the leukocyte integrin b2 cytoplasmic tail. Activation-dependent regulation of associations with talin and a-actinin. J Biol Chem 273(50):33588-33594.
    • (1998) J Biol Chem , vol.273 , Issue.50 , pp. 33588-33594
    • Sampath, R.1    Gallagher, P.J.2    Pavalko, F.M.3
  • 57
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von Jagow G. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166(2):368-379.
    • (1987) Anal Biochem , vol.166 , Issue.2 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 58
    • 0028958438 scopus 로고
    • Direct interaction of filamin (ABP-280) with the b 2-integrin subunit CD18
    • Sharma CP, Ezzell RM, Arnaout MA. 1995. Direct interaction of filamin (ABP-280) with the b 2-integrin subunit CD18. J Immunol 154(7): 3461-3470.
    • (1995) J Immunol , vol.154 , Issue.7 , pp. 3461-3470
    • Sharma, C.P.1    Ezzell, R.M.2    Arnaout, M.A.3
  • 59
    • 0028933571 scopus 로고
    • Complete primary structure and phosphorylation site of the 65-kDa macrophage protein phosphorylated by stimulation with bacterial lipopolysaccharide
    • Shinomiya H, Hagi A, Fukuzumi M, Mizobuchi M, Hirata H, Utsumi S. 1995. Complete primary structure and phosphorylation site of the 65-kDa macrophage protein phosphorylated by stimulation with bacterial lipopolysaccharide. J Immunol 154(7):3471-3478.
    • (1995) J Immunol , vol.154 , Issue.7 , pp. 3471-3478
    • Shinomiya, H.1    Hagi, A.2    Fukuzumi, M.3    Mizobuchi, M.4    Hirata, H.5    Utsumi, S.6
  • 61
    • 0032504209 scopus 로고    scopus 로고
    • Human b-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Iba
    • Takafuta T, Wu G, Murphy GF, Shapiro SS. 1998. Human b-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Iba. J Biol Chem 273(28):17531-17538.
    • (1998) J Biol Chem , vol.273 , Issue.28 , pp. 17531-17538
    • Takafuta, T.1    Wu, G.2    Murphy, G.F.3    Shapiro, S.S.4
  • 63
    • 0035957962 scopus 로고    scopus 로고
    • L-plastin peptide activation of avb3- mediated adhesion requires integrin conformational change and actin filament disassembly
    • Wang J, Chen H, Brown EJ. 2001. L-plastin peptide activation of avb3- mediated adhesion requires integrin conformational change and actin filament disassembly. J Biol Chem 276(17):14474-14481.
    • (2001) J Biol Chem , vol.276 , Issue.17 , pp. 14474-14481
    • Wang, J.1    Chen, H.2    Brown, E.J.3
  • 64
    • 4444254413 scopus 로고    scopus 로고
    • Yeast actin patches are networks of branched actin filaments
    • Young ME, Cooper JA, Bridgman PC. 2004. Yeast actin patches are networks of branched actin filaments. J Cell Biol 166(5):629-635.
    • (2004) J Cell Biol , vol.166 , Issue.5 , pp. 629-635
    • Young, M.E.1    Cooper, J.A.2    Bridgman, P.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.