메뉴 건너뛰기




Volumn 6, Issue 3, 2004, Pages 243-254

Enterohaemorrhagic and enteropathogenic Escherichia coli use different mechanisms for actin pedestal formation that converge on N-WASP

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; F ACTIN; WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 1342284070     PISSN: 14625814     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1462-5822.2004.00364.x     Document Type: Article
Times cited : (62)

References (59)
  • 1
    • 0033609388 scopus 로고    scopus 로고
    • Structure of Cdc42 in complex with the GTPase-binding domain of the 'Wiskott-Aldrich syndrome' protein
    • Abdul-Manan, N., Aghazadeh, B., Liu, G.A., Majumdar, A., Ouerfelli, O., Siminovitch, K.A., and Rosen, M.K. (1999) Structure of Cdc42 in complex with the GTPase-binding domain of the 'Wiskott-Aldrich syndrome' protein. Nature 399: 379-383.
    • (1999) Nature , vol.399 , pp. 379-383
    • Abdul-Manan, N.1    Aghazadeh, B.2    Liu, G.A.3    Majumdar, A.4    Ouerfelli, O.5    Siminovitch, K.A.6    Rosen, M.K.7
  • 2
    • 0032538914 scopus 로고    scopus 로고
    • Two enteropathogenic Escherichia coli type II secreted proteins, EspA and EspB, are virulence factors
    • Abe, A., Heczko, U., Hegele, R.G., and Brett Finlay, B. (1998) Two enteropathogenic Escherichia coli type II secreted proteins, EspA and EspB, are virulence factors. J Exp Med 188: 1907-1916.
    • (1998) J. Exp. Med. , vol.188 , pp. 1907-1916
    • Abe, A.1    Heczko, U.2    Hegele, R.G.3    Brett Finlay, B.4
  • 3
    • 0032516877 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck
    • Anton, I.M., Lu, W., Mayer, B.J., Ramesh, N., and Geha, R.S. (1998) The Wiskott-Aldrich syndrome protein-interacting protein (WIP) binds to the adaptor protein Nck. J Biol Chem 273: 20992-20995.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20992-20995
    • Anton, I.M.1    Lu, W.2    Mayer, B.J.3    Ramesh, N.4    Geha, R.S.5
  • 4
    • 0032036390 scopus 로고    scopus 로고
    • Agents that inhibit Rho, Rac, and Cdc42 do not block formation of actin pedestals in HeLa cells infected with enteropathogenic Escherichia coli
    • Ben-Ami, G., Ozeri, V., Hanski, E., Hofmann, F., Aktories, K., Hahn, K.M., et al. (1998) Agents that inhibit Rho, Rac, and Cdc42 do not block formation of actin pedestals in HeLa cells infected with enteropathogenic Escherichia coli. Infect Immun 66: 1755-1758.
    • (1998) Infect. Immun. , vol.66 , pp. 1755-1758
    • Ben-Ami, G.1    Ozeri, V.2    Hanski, E.3    Hofmann, F.4    Aktories, K.5    Hahn, K.M.6
  • 5
    • 0037020265 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-biphosphate (PIP2)-induced vesicle movement depends on N-WASP and involves Nck, WIP, and Grb2
    • Benesch, S., Lommel, S., Steffen, A., Stradal, T.E., Scaplehorn, N., Way, M., et al. (2002) Phosphatidylinositol 4,5-biphosphate (PIP2)-induced vesicle movement depends on N-WASP and involves Nck, WIP, and Grb2. J Biol Chem 277: 37771-37776.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37771-37776
    • Benesch, S.1    Lommel, S.2    Steffen, A.3    Stradal, T.E.4    Scaplehorn, N.5    Way, M.6
  • 6
    • 0037330293 scopus 로고    scopus 로고
    • Tails of two Tirs: Actin pedestal formation by enteropathogenic E. coli and enterohemorrhagic E. coli O157:H7
    • Campellone, K.G., and Leong, J.M. (2003) Tails of two Tirs: actin pedestal formation by enteropathogenic E. coli and enterohemorrhagic E. coli O157:H7. Curr Opin Microbiol 6: 82-90.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 82-90
    • Campellone, K.G.1    Leong, J.M.2
  • 7
    • 0036223873 scopus 로고    scopus 로고
    • A tyrosine-phosphorylated 12-amino-acid sequence of enteropathogenic Escherichia coli Tir binds the host adaptor protein Nck and is required for Nck localization to actin pedestals
    • Campellone, K.G., Giese, A., Tipper, D.J., and Leong, J.M. (2002) A tyrosine-phosphorylated 12-amino-acid sequence of enteropathogenic Escherichia coli Tir binds the host adaptor protein Nck and is required for Nck localization to actin pedestals. Mol Microbiol 43: 1227-1241.
    • (2002) Mol. Microbiol. , vol.43 , pp. 1227-1241
    • Campellone, K.G.1    Giese, A.2    Tipper, D.J.3    Leong, J.M.4
  • 8
    • 0034698158 scopus 로고    scopus 로고
    • GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex
    • Carlier, M.F., Nioche, P., Broutin-L'Hermite, I., Boujemaa, R., Le Clainche, C., Egile, C., et al. (2000) GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex. J Biol Chem 275: 21946-21952.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21946-21952
    • Carlier, M.F.1    Nioche, P.2    Broutin-L'Hermite, I.3    Boujemaa, R.4    Le Clainche, C.5    Egile, C.6
  • 9
    • 0036468733 scopus 로고    scopus 로고
    • Regulation of Wiskoft-Aldrich syndrome protein and related molecules
    • Caron, E. (2002) Regulation of Wiskoft-Aldrich syndrome protein and related molecules. Curr Opin Cell Biol 14: 82-87.
    • (2002) Curr. Opin. Cell. Biol. , vol.14 , pp. 82-87
    • Caron, E.1
  • 10
    • 0037160142 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich syndrome protein
    • Cory, G.O., Garg, R., Cramer, R., and Ridley, A.J. (2002) Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. Wiskott-Aldrich syndrome protein. J Biol Chem 277: 45115-45121.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45115-45121
    • Cory, G.O.1    Garg, R.2    Cramer, R.3    Ridley, A.J.4
  • 11
    • 0031695107 scopus 로고    scopus 로고
    • Escherichia coli O157:H7 requires intimin for enteropathogenicity in calves
    • Dean-Nystrom, E.A., Bosworth, B.T., Moon, H.W., and O'Brien, A.D. (1998) Escherichia coli O157:H7 requires intimin for enteropathogenicity in calves. Infect Immun 66: 4560-4563.
    • (1998) Infect. Immun. , vol.66 , pp. 4560-4563
    • Dean-Nystrom, E.A.1    Bosworth, B.T.2    Moon, H.W.3    O'Brien, A.D.4
  • 12
    • 0031960239 scopus 로고    scopus 로고
    • EspE, a novel secreted protein of attaching and effacing bacteria, is directly translocated into infected host cells, where it appears as a tyrosine-phosphorylated 90 kDa protein
    • Deibel, C., Kramer, S., Chakraborty, T., and Ebel, F. (1998) EspE, a novel secreted protein of attaching and effacing bacteria, is directly translocated into infected host cells, where it appears as a tyrosine-phosphorylated 90 kDa protein. Mol Microbiol 28: 463-474.
    • (1998) Mol. Microbiol. , vol.28 , pp. 463-474
    • Deibel, C.1    Kramer, S.2    Chakraborty, T.3    Ebel, F.4
  • 13
    • 0032959551 scopus 로고    scopus 로고
    • Enterohemorrhagic Escherichia coli O157:H7 produces Tir, which is translocated to the host cell membrane but is not tyrosine phosphorylated
    • DeVinney, R., Stein, M., Reinscheid, D., Abe, A., Ruschkowski, S., and Finlay, B.B. (1999) Enterohemorrhagic Escherichia coli O157:H7 produces Tir, which is translocated to the host cell membrane but is not tyrosine phosphorylated. Infect Immun 67: 2389-2398.
    • (1999) Infect. Immun. , vol.67 , pp. 2389-2398
    • DeVinney, R.1    Stein, M.2    Reinscheid, D.3    Abe, A.4    Ruschkowski, S.5    Finlay, B.B.6
  • 14
    • 0034800491 scopus 로고    scopus 로고
    • Enterohaemorrhagic and enteropathogenic Escherichia coli use a different Tir-based mechanism for pedestal formation
    • DeVinney, R., Puente, J.L., Gauthier, A., Goosney, D., and Finlay, B.B. (2001) Enterohaemorrhagic and enteropathogenic Escherichia coli use a different Tir-based mechanism for pedestal formation. Mol Microbiol 41: 1445-1458.
    • (2001) Mol. Microbiol. , vol.41 , pp. 1445-1458
    • DeVinney, R.1    Puente, J.L.2    Gauthier, A.3    Goosney, D.4    Finlay, B.B.5
  • 15
    • 0027164517 scopus 로고
    • The role of the eae gene of enterohemorrhagic Escherichia coli in intimate attachment in vitro and in a porcine model
    • Donnenberg, M.S., Tzipori, S., McKee, M.L., O'Brien, A.D., Alroy, J., and Kaper, J.B. (1993) The role of the eae gene of enterohemorrhagic Escherichia coli in intimate attachment in vitro and in a porcine model. J Clin Invest 92: 1418-1424.
    • (1993) J. Clin. Invest. , vol.92 , pp. 1418-1424
    • Donnenberg, M.S.1    Tzipori, S.2    McKee, M.L.3    O'Brien, A.D.4    Alroy, J.5    Kaper, J.B.6
  • 16
    • 0035182168 scopus 로고    scopus 로고
    • Surfing pathogens and the lessons learned for actin polymerization
    • Frischknecht, F., and Way, M. (2001) Surfing pathogens and the lessons learned for actin polymerization. Trends Cell Biol 11: 30-38.
    • (2001) Trends. Cell. Biol. , vol.11 , pp. 30-38
    • Frischknecht, F.1    Way, M.2
  • 18
    • 0035059331 scopus 로고    scopus 로고
    • Recruitment of cytoskeletal and signaling proteins to enteropathogenic and enterohemorrhagic Escherichia coli pedestals
    • Goosney, D.L., DeVinney, R., and Finlay, B.B. (2001) Recruitment of cytoskeletal and signaling proteins to enteropathogenic and enterohemorrhagic Escherichia coli pedestals. Infect Immun 69: 3315-3322.
    • (2001) Infect. Immun. , vol.69 , pp. 3315-3322
    • Goosney, D.L.1    DeVinney, R.2    Finlay, B.B.3
  • 20
    • 0034842129 scopus 로고    scopus 로고
    • Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cells
    • Gruenheid, S., DeVinney, R., Bladt, F., Goosney, D., Gelkop, S., Gish, G.D., et al. (2001) Enteropathogenic E. coli Tir binds Nck to initiate actin pedestal formation in host cells. Nature Cell Biol 3: 856-859.
    • (2001) Nature Cell Biol. , vol.3 , pp. 856-859
    • Gruenheid, S.1    DeVinney, R.2    Bladt, F.3    Goosney, D.4    Gelkop, S.5    Gish, G.D.6
  • 22
    • 0035949469 scopus 로고    scopus 로고
    • CR16 forms a complex with N-WASP in brain and is a novel member of a conserved proline-rich actin-binding protein family
    • Ho, H.Y., Rohatgi, R., Ma, L., and Kirschner, M.W. (2001) CR16 forms a complex with N-WASP in brain and is a novel member of a conserved proline-rich actin-binding protein family. Proc Natl Acad Sci USA 98: 11306-11311.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11306-11311
    • Ho, H.Y.1    Rohatgi, R.2    Ma, L.3    Kirschner, M.W.4
  • 23
    • 0034682705 scopus 로고    scopus 로고
    • Flipping the switch: The structural basis for signaling through the CRIB motif
    • Hoffman, G.R., and Cerione, R.A. (2000) Flipping the switch: the structural basis for signaling through the CRIB motif. Cell 102: 403-406.
    • (2000) Cell , vol.102 , pp. 403-406
    • Hoffman, G.R.1    Cerione, R.A.2
  • 24
    • 0029151311 scopus 로고
    • Signal transduction responses following adhesion of verocytotoxin-producing Escherichia coli
    • Ismaili, A., Philpott, D.J., Dytoc, M.T., and Sherman, P.M. (1995) Signal transduction responses following adhesion of verocytotoxin-producing Escherichia coli. Infect Immun 63: 3316-3326.
    • (1995) Infect. Immun. , vol.63 , pp. 3316-3326
    • Ismaili, A.1    Philpott, D.J.2    Dytoc, M.T.3    Sherman, P.M.4
  • 26
    • 0036083157 scopus 로고    scopus 로고
    • WICH, a novel verprolin homology domain-containing protein that functions cooperatively with N-WASP in actin-microspike formation
    • Kato, M., Miki, H., Kurita, S., Endo, T., Nakagawa, H., Miyamoto, S., and Takenawa, T. (2002) WICH, a novel verprolin homology domain-containing protein that functions cooperatively with N-WASP in actin-microspike formation. Biochem Biophys Res Commun 291: 41-47.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 41-47
    • Kato, M.1    Miki, H.2    Kurita, S.3    Endo, T.4    Nakagawa, H.5    Miyamoto, S.6    Takenawa, T.7
  • 27
    • 0033002855 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 474 of the enteropathogenic Escherichia coli (EPEC) Tir receptor molecule is essential for actin nucleating activity and is preceded by additional host modifications
    • Kenny, B. (1999) Phosphorylation of tyrosine 474 of the enteropathogenic Escherichia coli (EPEC) Tir receptor molecule is essential for actin nucleating activity and is preceded by additional host modifications. Mol Microbiol 31: 1229-1241.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1229-1241
    • Kenny, B.1
  • 28
    • 0030701868 scopus 로고    scopus 로고
    • Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells
    • Kenny, B., DeVinney, R., Stein, M., Reinscheid, D.J., Frey, E.A., and Finlay, B.B. (1997) Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. Cell 91: 511-520.
    • (1997) Cell , vol.91 , pp. 511-520
    • Kenny, B.1    DeVinney, R.2    Stein, M.3    Reinscheid, D.J.4    Frey, E.A.5    Finlay, B.B.6
  • 29
    • 0024565478 scopus 로고
    • Actin accumulation at sites of bacterial adhesion to tissue culture cells: Basis of a new diagnostic test for enteropathogenic and enterohemorrhagic Escherichia coli
    • Knutton, S., Baldwin, T., Williams, P.H., and McNeish, A.S. (1989) Actin accumulation at sites of bacterial adhesion to tissue culture cells: basis of a new diagnostic test for enteropathogenic and enterohemorrhagic Escherichia coli. Infect Immun 57: 1290-1298.
    • (1989) Infect. Immun. , vol.57 , pp. 1290-1298
    • Knutton, S.1    Baldwin, T.2    Williams, P.H.3    McNeish, A.S.4
  • 30
    • 0018148992 scopus 로고
    • Escherichia coli strains that cause diarrhoea but do not produce heat-labile or heat-stable enterotoxins and are non-invasive
    • Levine, M.M., Bergquist, E.J., Nalin, D.R., Waterman, D.H., Hornick, R.B., Young, C.R., and Sotman, S. (1978) Escherichia coli strains that cause diarrhoea but do not produce heat-labile or heat-stable enterotoxins and are non-invasive. Lancet 1: 1119-1122.
    • (1978) Lancet , vol.1 , pp. 1119-1122
    • Levine, M.M.1    Bergquist, E.J.2    Nalin, D.R.3    Waterman, D.H.4    Hornick, R.B.5    Young, C.R.6    Sotman, S.7
  • 31
    • 0034769365 scopus 로고    scopus 로고
    • Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells
    • Lommel, S., Benesch, S., Rottner, K., Franz, T., Wehland, J., and Kuhn, R. (2001) Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells. EMBO Rep 2: 850-857.
    • (2001) EMBO Rep. , vol.2 , pp. 850-857
    • Lommel, S.1    Benesch, S.2    Rottner, K.3    Franz, T.4    Wehland, J.5    Kuhn, R.6
  • 32
    • 0031025080 scopus 로고    scopus 로고
    • A cloned pathogenicity island from enteropathogenic Escherichia coli confers the attaching and effacing phenotype on E. coli K-12
    • McDaniel, T.K., and Kaper, J.B. (1997) A cloned pathogenicity island from enteropathogenic Escherichia coli confers the attaching and effacing phenotype on E. coli K-12. Mol Microbiol 23: 399-407.
    • (1997) Mol. Microbiol. , vol.23 , pp. 399-407
    • McDaniel, T.K.1    Kaper, J.B.2
  • 33
    • 0028945803 scopus 로고
    • A genetic locus of enterocyte effacement conserved among diverse enterobacterial pathogens
    • McDaniel, T.K., Jarvis, K.G., Donnenberg, M.S., and Kaper, J.B. (1995) A genetic locus of enterocyte effacement conserved among diverse enterobacterial pathogens. Proc Natl Acad Sci USA 92: 1664-1668.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1664-1668
    • McDaniel, T.K.1    Jarvis, K.G.2    Donnenberg, M.S.3    Kaper, J.B.4
  • 34
    • 0029121425 scopus 로고
    • Enterohemorrhagic Escherichia coli O157:H7 requires intimin to colonize the gnotobiotic pig intestine and to adhere to HEp-2 cells
    • McKee, M.L., Melton-Celsa, A.R., Moxley, R.A., Francis, D.H., and O'Brien, A.D. (1995) Enterohemorrhagic Escherichia coli O157:H7 requires intimin to colonize the gnotobiotic pig intestine and to adhere to HEp-2 cells. Infect Immun 63: 3739-3744.
    • (1995) Infect. Immun. , vol.63 , pp. 3739-3744
    • McKee, M.L.1    Melton-Celsa, A.R.2    Moxley, R.A.3    Francis, D.H.4    O'Brien, A.D.5
  • 35
    • 0034018023 scopus 로고    scopus 로고
    • Role of tir and intimin in the virulence of rabbit enteropathogenic Escherichia coli serotype O103:H2
    • Marches, O., Nougayrede, J.P., Boullier, S., Mainil, J., Charlier, G., Raymond, I., et al. (2000) Role of tir and intimin in the virulence of rabbit enteropathogenic Escherichia coli serotype O103:H2. Infect Immun 68: 2171-2182.
    • (2000) Infect. Immun. , vol.68 , pp. 2171-2182
    • Marches, O.1    Nougayrede, J.P.2    Boullier, S.3    Mainil, J.4    Charlier, G.5    Raymond, I.6
  • 37
    • 0031952518 scopus 로고    scopus 로고
    • Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP
    • Miki, H., Sasaki, T., Takai, Y., and Takenawa, T. (1998) Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP. Nature 391: 93-96.
    • (1998) Nature , vol.391 , pp. 93-96
    • Miki, H.1    Sasaki, T.2    Takai, Y.3    Takenawa, T.4
  • 38
    • 0020508377 scopus 로고
    • Attaching and effacing activities of rabbit and human enteropathogenic Escherichia coli in pig and rabbit intestines
    • Moon, H.W., Whipp, S.C., Argenzio, R.A., Levine, M.M., and Giannella, R.A. (1983) Attaching and effacing activities of rabbit and human enteropathogenic Escherichia coli in pig and rabbit intestines. Infect Immun 41: 1340-1351.
    • (1983) Infect. Immun. , vol.41 , pp. 1340-1351
    • Moon, H.W.1    Whipp, S.C.2    Argenzio, R.A.3    Levine, M.M.4    Giannella, R.A.5
  • 43
    • 0034721696 scopus 로고    scopus 로고
    • Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex
    • Prehoda, K.E., Scott, J.A., Dyche Mullins, R., and Lim, W.A. (2000) Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science 290: 801-806.
    • (2000) Science , vol.290 , pp. 801-806
    • Prehoda, K.E.1    Scott, J.A.2    Dyche Mullins, R.3    Lim, W.A.4
  • 44
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi, R., Ma, L., Miki, H., Lopez, M., Kirchhausen, T., Takenawa, T., and Kirschner, M.W. (1999) The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97: 221-231.
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5    Takenawa, T.6    Kirschner, M.W.7
  • 45
    • 0034683746 scopus 로고    scopus 로고
    • Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate
    • Rohatgi, R., Ho, H.Y., and Kirschner, M.W. (2000) Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate. J Cell Biol 150: 1299-1310.
    • (2000) J. Cell. Biol. , vol.150 , pp. 1299-1310
    • Rohatgi, R.1    Ho, H.Y.2    Kirschner, M.W.3
  • 46
    • 0035854732 scopus 로고    scopus 로고
    • Nck and Phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway
    • Rohatgi, R., Nollau, P., Ho, H.Y., Kirschner, M.W., and Mayer, B.J. (2001) Nck and Phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway. J Biol Chem 276: 26448-26452.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26448-26452
    • Rohatgi, R.1    Nollau, P.2    Ho, H.Y.3    Kirschner, M.W.4    Mayer, B.J.5
  • 47
    • 0032541137 scopus 로고    scopus 로고
    • The Cdc42/Rac interactive binding region motif of the Wiskott Aldrich syndrome protein (WASP) is necessary but not sufficient for tight binding to Cdc42 and structure formation
    • Rudolph, M.G., Bayer, P., Abo, A., Kuhlmann, J., Vetter, I.R., and Wittinghofer, A. (1998) The Cdc42/Rac interactive binding region motif of the Wiskott Aldrich syndrome protein (WASP) is necessary but not sufficient for tight binding to Cdc42 and structure formation. J Biol Chem 273: 18067-18076.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18067-18076
    • Rudolph, M.G.1    Bayer, P.2    Abo, A.3    Kuhlmann, J.4    Vetter, I.R.5    Wittinghofer, A.6
  • 48
    • 0034795423 scopus 로고    scopus 로고
    • N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility
    • Snapper, S.B., Takeshima, F., Anton, I., Liu, C.H., Thomas, S.M., Nguyen, D., et al. (2001) N-WASP deficiency reveals distinct pathways for cell surface projections and microbial actin-based motility. Nature Cell Biol 3: 897-904.
    • (2001) Nature Cell Biol. , vol.3 , pp. 897-904
    • Snapper, S.B.1    Takeshima, F.2    Anton, I.3    Liu, C.H.4    Thomas, S.M.5    Nguyen, D.6
  • 49
  • 50
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons, M., Derry, J.M., Karlak, B., Jiang, S., Lemahieu, V., McCormick, F., et al. (1996) Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84: 723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    McCormick, F.6
  • 51
  • 52
    • 0036717243 scopus 로고    scopus 로고
    • WASp in immune-system organization and function
    • Thrasher, A.J. (2002) WASp in immune-system organization and function. Nature Rev Immunol 2: 635-646.
    • (2002) Nature Rev. Immunol. , vol.2 , pp. 635-646
    • Thrasher, A.J.1
  • 53
    • 0038392871 scopus 로고    scopus 로고
    • Contingent phosphorylation/dephosphorylation provides a mechanism of molecular memory in WASP
    • Torres, E., and Rosen, M.K. (2003) Contingent phosphorylation/dephosphorylation provides a mechanism of molecular memory in WASP. Mol Cell 11: 1215-1227.
    • (2003) Mol Cell. , vol.11 , pp. 1215-1227
    • Torres, E.1    Rosen, M.K.2
  • 55
    • 0029082455 scopus 로고
    • The role of the eaeA gene in diarrhea and neurological complications in a gnotobiotic piglet model of enterohemorrhagic Escherichia coli infection
    • Tzipori, S., Gunzer, F., Donnenberg, M.S., de Montigny, L., Kaper, J.B., and Donohue-Rolfe, A. (1995) The role of the eaeA gene in diarrhea and neurological complications in a gnotobiotic piglet model of enterohemorrhagic Escherichia coli infection. Infect Immun 63: 3621-3627.
    • (1995) Infect. Immun. , vol.63 , pp. 3621-3627
    • Tzipori, S.1    Gunzer, F.2    Donnenberg, M.S.3    de Montigny, L.4    Kaper, J.B.5    Donohue-Rolfe, A.6
  • 56
    • 0018922976 scopus 로고
    • Pathogenesis of Escherichia coli gastroenteritis in man - Another mechanism
    • Ulshen, M.H., and Rollo, J.L. (1980) Pathogenesis of Escherichia coli gastroenteritis in man - another mechanism. N Engl J Med 302: 99-101.
    • (1980) N. Engl. J. Med. , vol.302 , pp. 99-101
    • Ulshen, M.H.1    Rollo, J.L.2
  • 57
    • 0037016718 scopus 로고    scopus 로고
    • The rat homologue of Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP) associates with actin filaments, recruits N-WASP from the nucleus, and mediates mobilization of actin from stress fibers in favor of filopodia formation
    • Vetterkind, S., Miki, H., Takenawa, T., Klawitz, I, Scheidtmann, K.H., and Preuss, U. (2002) The rat homologue of Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP) associates with actin filaments, recruits N-WASP from the nucleus, and mediates mobilization of actin from stress fibers in favor of filopodia formation. J Biol Chem 277: 87-95.
    • (2002) J. Biol. Chem. , vol.277 , pp. 87-95
    • Vetterkind, S.1    Miki, H.2    Takenawa, T.3    Klawitz, I.4    Scheidtmann, K.H.5    Preuss, U.6
  • 59
    • 0037125912 scopus 로고    scopus 로고
    • The WH1 and EVH1 domains of WASP and Ena/VASP family members bind distinct sequence motifs
    • Zettl, M., and Way, M. (2002) The WH1 and EVH1 domains of WASP and Ena/VASP family members bind distinct sequence motifs. Curr Biol 12: 1617-1622.
    • (2002) Curr. Biol. , vol.12 , pp. 1617-1622
    • Zettl, M.1    Way, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.