메뉴 건너뛰기




Volumn 17, Issue 10, 2006, Pages 4564-4575

WASP-interacting protein is important for actin filament elongation and prompt pseudopod formation in response to a dynamic chemoattractant gradient

Author keywords

[No Author keywords available]

Indexed keywords

CHEMOATTRACTANT; CYCLIC AMP; F ACTIN; UNCLASSIFIED DRUG; WASP INTERACTING PROTEIN;

EID: 33749489509     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-10-0994     Document Type: Article
Times cited : (8)

References (50)
  • 1
    • 0001102239 scopus 로고
    • Pedigree demonstrating a sex linked recessive condition characterized by draining ears, eczematoid dermatitis, and bloody diarrhea
    • Aldrich, R. A., Steinberg, A. G., and Campbell, D. C. (1954). Pedigree demonstrating a sex linked recessive condition characterized by draining ears, eczematoid dermatitis, and bloody diarrhea. Pediatrics 13, 133-139.
    • (1954) Pediatrics , vol.13 , pp. 133-139
    • Aldrich, R.A.1    Steinberg, A.G.2    Campbell, D.C.3
  • 2
    • 0034829818 scopus 로고    scopus 로고
    • Chemokines in pathology and medicine
    • Bagiolini, M. (2001). Chemokines in pathology and medicine. J. Intern. Med. 250, 91-104.
    • (2001) J. Intern. Med. , vol.250 , pp. 91-104
    • Bagiolini, M.1
  • 3
    • 0032494137 scopus 로고    scopus 로고
    • SCAR, a WASP-related protein, isolated as a suppressor of receptor defects in late Dictyostelium development
    • Bear, J. E., Rawls, J. F., and Saxe, C. L. (1998). SCAR, a WASP-related protein, isolated as a suppressor of receptor defects in late Dictyostelium development. J. Cell Biol. 142, 1325-1335.
    • (1998) J. Cell Biol. , vol.142 , pp. 1325-1335
    • Bear, J.E.1    Rawls, J.F.2    Saxe, C.L.3
  • 4
    • 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., Wellland, J., and Rottner, K. (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    Wellland, J.7    Rottner, K.8
  • 5
    • 1642365541 scopus 로고    scopus 로고
    • Cascade pathway of filopodia formation downstream of SCAR
    • Biyasheva, A., Svitkina, T., Kunda, P., Baum, B., and Borisy, G. (2004). Cascade pathway of filopodia formation downstream of SCAR. J. Cell Sci. 117, 837-848.
    • (2004) J. Cell Sci. , vol.117 , pp. 837-848
    • Biyasheva, A.1    Svitkina, T.2    Kunda, P.3    Baum, B.4    Borisy, G.5
  • 6
    • 0042921214 scopus 로고    scopus 로고
    • PIR121 regulates pseudopod dynamics and SCAR activity in Dictyostelium
    • Blagg, S. L., Stewart, M., Sambles, C., and Insall, R. H. (2003). PIR121 regulates pseudopod dynamics and SCAR activity in Dictyostelium. Curr. Biol. 13, 1480-1487.
    • (2003) Curr. Biol. , vol.13 , pp. 1480-1487
    • Blagg, S.L.1    Stewart, M.2    Sambles, C.3    Insall, R.H.4
  • 7
    • 2342564406 scopus 로고    scopus 로고
    • Solving the WAVE function
    • Blagg, S. L., and Insall, R. H. (2004). Solving the WAVE function. Nat. Cell Biol. 6, 279-281.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 279-281
    • Blagg, S.L.1    Insall, R.H.2
  • 8
    • 0344796392 scopus 로고    scopus 로고
    • Two phases of actin polymerization display different dependencies on PI(3,4,5)P3 accumulation and have unique roles during chemotaxis
    • Chen, L., Janetopoulos, C., Huang, Y. E., Iijima, M., Borleis, J., and Devreotes, P. N. (2003). Two phases of actin polymerization display different dependencies on PI(3,4,5)P3 accumulation and have unique roles during chemotaxis. Mol. Biol. Cell 14, 5028-5037.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 5028-5037
    • Chen, L.1    Janetopoulos, C.2    Huang, Y.E.3    Iijima, M.4    Borleis, J.5    Devreotes, P.N.6
  • 9
    • 0035449609 scopus 로고    scopus 로고
    • Signaling pathways controlling cell polarity and chemotaxis
    • Chung, C. Y., Funamoto, S., and Firtel, R. A. (2001). Signaling pathways controlling cell polarity and chemotaxis. Trends Biochem. Sci. 26, 557-566.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 557-566
    • Chung, C.Y.1    Funamoto, S.2    Firtel, R.A.3
  • 10
    • 0033230933 scopus 로고    scopus 로고
    • PAKa, a putative PAK family member, is required for cytokinesis and the regulation of the cytoskeleton in Dictyostelium discoideum cells during chemotaxis
    • Chung, C. Y., and Firtel, R. A. (1999). PAKa, a putative PAK family member, is required for cytokinesis and the regulation of the cytoskeleton in Dictyostelium discoideum cells during chemotaxis. J. Cell Biol. 147, 559-575.
    • (1999) J. Cell Biol. , vol.147 , pp. 559-575
    • Chung, C.Y.1    Firtel, R.A.2
  • 12
    • 0024147085 scopus 로고
    • Chemotaxis in eukaryotic cells: A focus on leukocytes and Dictyostelium
    • Devreotes, P. N., and Zigmond, S. H. (1988). Chemotaxis in eukaryotic cells: a focus on leukocytes and Dictyostelium. Annu. Rev. Cell Biol. 4, 649-686.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 649-686
    • Devreotes, P.N.1    Zigmond, S.H.2
  • 13
    • 0033617576 scopus 로고    scopus 로고
    • A cell's sense of direction
    • Devreotes, P., and Parent, O. (1999). A cell's sense of direction. Science 284, 765-770.
    • (1999) Science , vol.284 , pp. 765-770
    • Devreotes, P.1    Parent, O.2
  • 14
    • 0033948436 scopus 로고    scopus 로고
    • The molecular genetics of chemotaxis: Sensing and responding to chemoattractant gradients
    • Firtel, R. A., and Chung, C. Y. (2000). The molecular genetics of chemotaxis: sensing and responding to chemoattractant gradients. BioEssays 22, 603-615.
    • (2000) BioEssays , vol.22 , pp. 603-615
    • Firtel, R.A.1    Chung, C.Y.2
  • 15
    • 0020073481 scopus 로고
    • Cell behavior in Dictyostelium discoideum: Preaggregation response to localized cAMP pulses
    • Futrelle, R. P., Traut, F. J., and McKee, W. G. (1982). Cell behavior in Dictyostelium discoideum: preaggregation response to localized cAMP pulses. J. Biol. Chem. 92, 807-821.
    • (1982) J. Biol. Chem. , vol.92 , pp. 807-821
    • Futrelle, R.P.1    Traut, F.J.2    McKee, W.G.3
  • 16
    • 31544454208 scopus 로고    scopus 로고
    • WIP and WASP play complementary roles in T cell homing and chemotaxis to SDF-1a
    • Gallego, M. D., Fuente, M. A., Anton, I. M., Snapper, S., Fuhlbrigge, R., and Geha, R. S. (2006). WIP and WASP play complementary roles in T cell homing and chemotaxis to SDF-1a. Int. Immun. 18, 221-232.
    • (2006) Int. Immun. , vol.18 , pp. 221-232
    • Gallego, M.D.1    Fuente, M.A.2    Anton, I.M.3    Snapper, S.4    Fuhlbrigge, R.5    Geha, R.S.6
  • 17
    • 0037147305 scopus 로고    scopus 로고
    • Requirement of a vasodilator-stimulated phosphoprotein family member for cell adhesion, the formation of filopodia, and chemotaxis in Dictyostelium
    • Han, Y., Chung, C. Y., Wessels, D., Stephens, S., Titus, M. A., Soll, D. R., and Firtel, R. (2002). Requirement of a vasodilator-stimulated phosphoprotein family member for cell adhesion, the formation of filopodia, and chemotaxis in Dictyostelium. J. Biol. Chem. 277, 49877-49887.
    • (2002) J. Biol. Chem. , vol.277 , pp. 49877-49887
    • Han, Y.1    Chung, C.Y.2    Wessels, D.3    Stephens, S.4    Titus, M.A.5    Soll, D.R.6    Firtel, R.7
  • 18
    • 33845932606 scopus 로고    scopus 로고
    • Role of RacC for the regulation of WASP activity and P13 kinase localization during chemotaxis of Dictyostelium
    • in press
    • Han, J. W., Leeper, L., Rivero, F., and Chung, C. Y. (2006). Role of RacC for the regulation of WASP activity and P13 kinase localization during chemotaxis of Dictyostelium. J. Biol. Chem. (in press).
    • (2006) J. Biol. Chem.
    • Han, J.W.1    Leeper, L.2    Rivero, F.3    Chung, C.Y.4
  • 19
    • 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. H., 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.H.1    Rohatgi, R.2    Ma, L.3    Kirschner, M.W.4
  • 20
    • 0344827286 scopus 로고    scopus 로고
    • A pathway for association of receptors, adaptors, and actin during endocytic internalization
    • Kaksonen, M., Sun, Y., and Drubin, D. G. (2003). A pathway for association of receptors, adaptors, and actin during endocytic internalization. Cell 115, 475-487.
    • (2003) Cell , vol.115 , pp. 475-487
    • Kaksonen, M.1    Sun, Y.2    Drubin, D.G.3
  • 21
    • 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
  • 22
    • 4644220799 scopus 로고    scopus 로고
    • Two novel mutations of Wiskott-Aldrich syndrome: The molecular prediction of interaction between the mutated WASP L101P with WASP-interacting protein by molecular modeling
    • Kim, M. K., Kim, K. S., Kim, D. S., Choi, I. H., Moon, T., Yoon, C. N., and Shin, J. (2004). Two novel mutations of Wiskott-Aldrich syndrome: the molecular prediction of interaction between the mutated WASP L101P with WASP-interacting protein by molecular modeling. Biochim. Biophys. Acta 14, 134-140.
    • (2004) Biochim. Biophys. Acta , vol.14 , pp. 134-140
    • Kim, M.K.1    Kim, K.S.2    Kim, D.S.3    Choi, I.H.4    Moon, T.5    Yoon, C.N.6    Shin, J.7
  • 24
    • 0033868390 scopus 로고    scopus 로고
    • From the growth cone surface to the cytoskeleton: One journey, many paths
    • Korey, C. A., and Van Vactor, D. (2000). From the growth cone surface to the cytoskeleton: one journey, many paths. J. Neurobiol. 44, 184-193.
    • (2000) J. Neurobiol. , vol.44 , pp. 184-193
    • Korey, C.A.1    Van Vactor, D.2
  • 25
    • 0036179411 scopus 로고    scopus 로고
    • RNAi in Dictyostelium: The role of RNA-directed RNA polymerases and double-stranded RNase
    • Martens, H., Novotny, J., Oberstrass, J., Steck, T. L., Postlethwait, P., and Nellen, W. (2002). RNAi in Dictyostelium: the role of RNA-directed RNA polymerases and double-stranded RNase. Mol. Biol. Cell 13, 445-453.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 445-453
    • Martens, H.1    Novotny, J.2    Oberstrass, J.3    Steck, T.L.4    Postlethwait, P.5    Nellen, W.6
  • 26
    • 0035003138 scopus 로고    scopus 로고
    • WIP regulates N-WASP-mediated actin polymerization and filopodium formation
    • Martinez-Quiles, N., et al. (2001). WIP regulates N-WASP-mediated actin polymerization and filopodium formation. Nat. Cell Biol. 3, 484-491.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 484-491
    • Martinez-Quiles, N.1
  • 27
    • 0033560747 scopus 로고    scopus 로고
    • Chemoattractant-mediated transient activation and membrane localization of Akt/PKB is required for efficient chemotaxis to cAMP in Dictyostelium
    • Meili, R., Ellsworth, C., Lee, S., Reddy, T.B.K., Ma, H., and Firtel, R. A. (1999). Chemoattractant-mediated transient activation and membrane localization of Akt/PKB is required for efficient chemotaxis to cAMP in Dictyostelium. EMBO J. 18, 2092-2105.
    • (1999) EMBO J. , vol.18 , pp. 2092-2105
    • Meili, R.1    Ellsworth, C.2    Lee, S.3    Reddy, T.B.K.4    Ma, H.5    Firtel, R.A.6
  • 28
    • 0029815611 scopus 로고    scopus 로고
    • N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases
    • Miki, H., Miura, K., and Takenawa, T. (1996). N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases. EMBO J. 15, 5326-5335.
    • (1996) EMBO J. , vol.15 , pp. 5326-5335
    • Miki, H.1    Miura, K.2    Takenawa, T.3
  • 30
    • 18244378218 scopus 로고    scopus 로고
    • A Dictyostelium homolog of WASP is required for polarized F-actin assembly during chemotaxis
    • Myers, S. A., Han, J. W., Lee, Y., Firtel, R. A., and Chung, C. Y. (2005). A Dictyostelium homolog of WASP is required for polarized F-actin assembly during chemotaxis. Mol. Biol. Cell 16, 2191-2206.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2191-2206
    • Myers, S.A.1    Han, J.W.2    Lee, Y.3    Firtel, R.A.4    Chung, C.Y.5
  • 31
    • 0037138384 scopus 로고    scopus 로고
    • WH2 domain: A small, versatile adapter for actin monomers
    • Paunola, E., Mattila, P. K., and Lappalainen, P. (2002). WH2 domain: a small, versatile adapter for actin monomers. FEBS Lett. 513, 92-97.
    • (2002) FEBS Lett. , vol.513 , pp. 92-97
    • Paunola, E.1    Mattila, P.K.2    Lappalainen, P.3
  • 32
    • 0033553508 scopus 로고    scopus 로고
    • Structure of the Enabled/VASP homology 1 domain-peptide complex: A key component in the spatial control of actin assembly
    • Prehoda, K. E., Lee, D. J., and Lim, W. A. (1999). Structure of the Enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly. Cell 97, 471-480.
    • (1999) Cell , vol.97 , pp. 471-480
    • Prehoda, K.E.1    Lee, D.J.2    Lim, W.A.3
  • 33
    • 0031446340 scopus 로고    scopus 로고
    • WIP, a protein associated with Wiskott-Aldrich Syndrome protein, induces actin polymerization and redistribution in lymphoid cells
    • Ramesh, N., Anton, I. M., Hartwig, J. H., and Geha, R. S. (1997). WIP, a protein associated with Wiskott-Aldrich Syndrome protein, induces actin polymerization and redistribution in lymphoid cells. Proc. Natl. Acad. Sci. USA 94, 14671-14676.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14671-14676
    • Ramesh, N.1    Anton, I.M.2    Hartwig, J.H.3    Geha, R.S.4
  • 34
    • 0033669220 scopus 로고    scopus 로고
    • Structural basis of Wiskott-Aldrich syndrome causing mutations in the WH1 domain
    • Rong, S. B., and Vihinen, M. (2000). Structural basis of Wiskott-Aldrich syndrome causing mutations in the WH1 domain. J. Mol. Med. 78, 530-537.
    • (2000) J. Mol. Med. , vol.78 , pp. 530-537
    • Rong, S.B.1    Vihinen, M.2
  • 36
    • 20444426470 scopus 로고    scopus 로고
    • The diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia
    • Schirenbeck, A., Bretschneider, T., Arasada, R., Schleicher, M., and Faix, J. (2005). The diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia. Nat. Cell Biol. 7, 619-625.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 619-625
    • Schirenbeck, A.1    Bretschneider, T.2    Arasada, R.3    Schleicher, M.4    Faix, J.5
  • 37
    • 0032118427 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein-deficient mice reveal a role for WASP in T but not B cell activation
    • Snapper, S. B., et al. (1998). Wiskott-Aldrich syndrome protein-deficient mice reveal a role for WASP in T but not B cell activation. Immunity 9, 81-91.
    • (1998) Immunity , vol.9 , pp. 81-91
    • Snapper, S.B.1
  • 38
    • 0033012399 scopus 로고    scopus 로고
    • The Wiskott-Aldrich Syndrome protein (WASP): Roles in signaling and cytoskeletal organization
    • Snapper, S. B., and Rosen, F. S. (1999). The Wiskott-Aldrich Syndrome protein (WASP): roles in signaling and cytoskeletal organization. Annu. Rev. Immunol. 17, 905-929.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 905-929
    • Snapper, S.B.1    Rosen, F.S.2
  • 39
    • 0033561727 scopus 로고    scopus 로고
    • Mutations that cause the Wiskott-Aldrich syndrome impair the interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein
    • Stewart, D. M., Tian, L., and Nelson, D. L. (1999). Mutations that cause the Wiskott-Aldrich syndrome impair the interaction of Wiskott-Aldrich syndrome protein (WASP) with WASP interacting protein. J. Immunol. 162, 5019-5024.
    • (1999) J. Immunol. , vol.162 , pp. 5019-5024
    • Stewart, D.M.1    Tian, L.2    Nelson, D.L.3
  • 40
    • 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., Francke, U., and Abo, A. (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    Francke, U.7    Abo, A.8
  • 41
    • 0031416482 scopus 로고    scopus 로고
    • Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton
    • Vaduva, G., Martin, N. C., and Hopper, A. K. (1997). Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton. J. Cell Biol. 139, 1821-1833.
    • (1997) J. Cell Biol. , vol.139 , pp. 1821-1833
    • Vaduva, G.1    Martin, N.C.2    Hopper, A.K.3
  • 43
    • 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., 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.5    Preuss, U.6
  • 44
    • 0037112347 scopus 로고    scopus 로고
    • Structure of the N-WASP EVH1 domain-WIP complex: Insight into the molecular basis of Wiskott-Aldrich syndrome
    • Volkman, B. F., Prehoda, K. E., Scott, J. A., Peterson, F. C., and Lim, W. A. (2002). Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich syndrome. Cell 111, 565-576.
    • (2002) Cell , vol.111 , pp. 565-576
    • Volkman, B.F.1    Prehoda, K.E.2    Scott, J.A.3    Peterson, F.C.4    Lim, W.A.5
  • 45
    • 0033740788 scopus 로고    scopus 로고
    • Two tandem verprolin homology domains are necessary for a strong activation of Arp2/3 complex-induced actin polymerization and induction of microspike formation
    • Yamaguchi, H., Miki, H., Suetsugu, S., Ma, L., Kirschner, M. W., and Takenawa, T. (2000). Two tandem verprolin homology domains are necessary for a strong activation of Arp2/3 complex-induced actin polymerization and induction of microspike formation. Proc. Natl. Acad. Sci. USA 97, 12631-12636.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12631-12636
    • Yamaguchi, H.1    Miki, H.2    Suetsugu, S.3    Ma, L.4    Kirschner, M.W.5    Takenawa, T.6
  • 46
    • 0042815094 scopus 로고    scopus 로고
    • WAVE2 deficiency reveals distinct roles in embryogenesis and Rac-mediated actin-based motility
    • Yan, C., et al. (2003). WAVE2 deficiency reveals distinct roles in embryogenesis and Rac-mediated actin-based motility. EMBO J. 22, 3602-3612.
    • (2003) EMBO J. , vol.22 , pp. 3602-3612
    • Yan, C.1
  • 47
    • 0035846598 scopus 로고    scopus 로고
    • Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities
    • Zalevsky, J., Lempert, L., Kranitz, H., and Mullins, R. D. (2001). Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities. Curr. Biol. 11, 1903-1913.
    • (2001) Curr. Biol. , vol.11 , pp. 1903-1913
    • Zalevsky, J.1    Lempert, L.2    Kranitz, H.3    Mullins, R.D.4
  • 48
    • 0037125912 scopus 로고    scopus 로고
    • The WH1 and EVH1 domains of WASP and Ena/VASP family members bind distinct sequence motifs
    • Zetti, 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
    • Zetti, M.1    Way, M.2
  • 49
    • 0034683577 scopus 로고    scopus 로고
    • How WASP regulates actin polymerization
    • Zigmond, S. H. (2000). How WASP regulates actin polymerization. J. Cell Biol. 150, F117-F120.
    • (2000) J. Cell Biol. , vol.150
    • Zigmond, S.H.1
  • 50
    • 0030849454 scopus 로고    scopus 로고
    • Regulation of actin polymerization in cell-free systems by GTPγS and Cdc42
    • Zigmond, S. H., Joyce, M., Borleis, J., Bokoch, G. M., and Devreotes, P. N. (1997). Regulation of actin polymerization in cell-free systems by GTPγS and Cdc42. J. Cell Biol. 138, 363-374.
    • (1997) J. Cell Biol. , vol.138 , pp. 363-374
    • Zigmond, S.H.1    Joyce, M.2    Borleis, J.3    Bokoch, G.M.4    Devreotes, P.N.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.