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Volumn 179, Issue 4, 2007, Pages 777-791

Cofilin determines the migration behavior and turning frequency of metastatic cancer cells

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN RELATED PROTEIN 2-3 COMPLEX; COFILIN; EPIDERMAL GROWTH FACTOR; F ACTIN;

EID: 36348968323     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200707009     Document Type: Article
Times cited : (167)

References (54)
  • 1
    • 0034536444 scopus 로고    scopus 로고
    • The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes
    • Ambach, A., J. Saunus, M. Konstandin, S. Wesselborg, S.C. Meuer, and Y. Samstag. 2000. The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes. Eur. J. Immunol. 30:3422-3431.
    • (2000) Eur. J. Immunol , vol.30 , pp. 3422-3431
    • Ambach, A.1    Saunus, J.2    Konstandin, M.3    Wesselborg, S.4    Meuer, S.C.5    Samstag, Y.6
  • 2
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin
    • Andrianantoandro, E., and T.D. Pollard. 2006. Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol. Cell. 24:13-23.
    • (2006) Mol. Cell , vol.24 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 3
    • 17144460611 scopus 로고    scopus 로고
    • Regulation of protrusion shape and adhesion to the substratum during chemotactic responses of mammalian carcinoma cells
    • Bailly, M., L. Yan, G.M. Whitesides, J.S. Condeelis, and J.E. Segall. 1998. Regulation of protrusion shape and adhesion to the substratum during chemotactic responses of mammalian carcinoma cells. Exp. Cell Res. 241:285-299.
    • (1998) Exp. Cell Res , vol.241 , pp. 285-299
    • Bailly, M.1    Yan, L.2    Whitesides, G.M.3    Condeelis, J.S.4    Segall, J.E.5
  • 4
    • 0344299281 scopus 로고    scopus 로고
    • Relationship between Arp2/3 complex and the barbed ends of actin filaments at the leading edge of carcinoma cells after epidermal growth factor stimulation
    • Bailly, M., F. Macaluso, M. Cammer, A. Chan, J.E. Segall, and J.S. Condeelis. 1999. Relationship between Arp2/3 complex and the barbed ends of actin filaments at the leading edge of carcinoma cells after epidermal growth factor stimulation. J. Cell Biol. 145:331-345.
    • (1999) J. Cell Biol , vol.145 , pp. 331-345
    • Bailly, M.1    Macaluso, F.2    Cammer, M.3    Chan, A.4    Segall, J.E.5    Condeelis, J.S.6
  • 5
    • 0035928737 scopus 로고    scopus 로고
    • Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin
    • Blanchoin, L., T.D. Pollard, and S.E. Hitchcock-DeGregori. 2001. Inhibition of the Arp2/3 complex-nucleated actin polymerization and branch formation by tropomyosin. Curr. Biol. 11:1300-1304.
    • (2001) Curr. Biol , vol.11 , pp. 1300-1304
    • Blanchoin, L.1    Pollard, T.D.2    Hitchcock-DeGregori, S.E.3
  • 6
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/ cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • Carlier, M.F., V. Laurent, J. Santolini, R. Melki, D. Didry, G.X. Xia, Y. Hong, N.H. Chua, and D. Pantaloni. 1997. Actin depolymerizing factor (ADF/ cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell Biol. 136:1307-1322.
    • (1997) J. Cell Biol , vol.136 , pp. 1307-1322
    • Carlier, M.F.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Didry, D.5    Xia, G.X.6    Hong, Y.7    Chua, N.H.8    Pantaloni, D.9
  • 7
    • 0034614942 scopus 로고    scopus 로고
    • Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion
    • Chan, A.Y., M. Bailly, N. Zebda, J.E. Segall, and J.S. Condeelis. 2000. Role of cofilin in epidermal growth factor-stimulated actin polymerization and lamellipod protrusion. J. Cell Biol. 148:531-542.
    • (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
  • 8
    • 0345059766 scopus 로고    scopus 로고
    • Intravital imaging of cell movement in tumours
    • Condeelis, J., and J.E. Segall. 2003. Intravital imaging of cell movement in tumours. Nat. Rev. Cancer. 3:921-930.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 921-930
    • Condeelis, J.1    Segall, J.E.2
  • 9
    • 28444472417 scopus 로고    scopus 로고
    • The great escape: When cancer cells hijack the genes for chemotaxis and motility
    • Condeelis, J., R.H. Singer, and J.E. Segall. 2005. The great escape: when cancer cells hijack the genes for chemotaxis and motility. Annu. Rev. Cell Dev. Biol. 21:695-718.
    • (2005) Annu. Rev. Cell Dev. Biol , vol.21 , pp. 695-718
    • Condeelis, J.1    Singer, R.H.2    Segall, J.E.3
  • 10
    • 12244303674 scopus 로고    scopus 로고
    • ADF/cofilin controls cell polarity during fibroblast migration
    • Dawe, H.R., L.S. Minamide, J.R. Bamburg, and L.P. Cramer. 2003. ADF/cofilin controls cell polarity during fibroblast migration. Curr Biol. 13:252-257.
    • (2003) Curr Biol , vol.13 , pp. 252-257
    • Dawe, H.R.1    Minamide, L.S.2    Bamburg, J.R.3    Cramer, L.P.4
  • 11
    • 0036912348 scopus 로고    scopus 로고
    • Spatial regulation of actin dynamics: A tropomyosin-free, actin-rich compartment at the leading edge
    • DesMarais, V., I. Ichetovkin, J. Condeelis, and S.E. Hitchcock-DeGregori. 2002. Spatial regulation of actin dynamics: a tropomyosin-free, actin-rich compartment at the leading edge. J. Cell Sci. 115:4649-4660.
    • (2002) J. Cell Sci , vol.115 , pp. 4649-4660
    • DesMarais, V.1    Ichetovkin, I.2    Condeelis, J.3    Hitchcock-DeGregori, S.E.4
  • 12
    • 4444339659 scopus 로고    scopus 로고
    • Synergistic interaction between the Arp2/3 complex and cofilin drives stimulated lamellipod extension
    • DesMarais, V., F. Macaluso, J. Condeelis, and M. Bailly. 2004. Synergistic interaction between the Arp2/3 complex and cofilin drives stimulated lamellipod extension. J. Cell Sci. 117:3499-3510.
    • (2004) J. Cell Sci , vol.117 , pp. 3499-3510
    • DesMarais, V.1    Macaluso, F.2    Condeelis, J.3    Bailly, M.4
  • 13
    • 28044449941 scopus 로고    scopus 로고
    • Arp2/3 complex-deficient mouse fibroblasts are viable and have normal leading-edge actin structure and function
    • Di Nardo, A., G. Cicchetti, H. Falet, J.H. Hartwig, T.P. Stossel, and D.J. Kwiatkowski. 2005. Arp2/3 complex-deficient mouse fibroblasts are viable and have normal leading-edge actin structure and function. Proc. Natl. Acad. Sci. USA. 102:16263-16268.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16263-16268
    • Di Nardo, A.1    Cicchetti, G.2    Falet, H.3    Hartwig, J.H.4    Stossel, T.P.5    Kwiatkowski, D.J.6
  • 15
    • 2342436150 scopus 로고    scopus 로고
    • Cofilin promotes actin polymerization and defines the direction of cell motility
    • Ghosh, M., X. Song, G. Mouneimne, M. Sidani, D.S. Lawrence, and J.S. Condeelis. 2004. Cofilin promotes actin polymerization and defines the direction of cell motility. Science. 304:743-746.
    • (2004) Science , vol.304 , pp. 743-746
    • Ghosh, M.1    Song, X.2    Mouneimne, G.3    Sidani, M.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 16
    • 12344250639 scopus 로고    scopus 로고
    • Chronophin, a novel HADtype serine protein phosphatase, regulates cofilin-dependent actin dynamics
    • Gohla, A., J. Birkenfeld, and G.M. Bokoch. 2005. Chronophin, a novel HADtype serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat. Cell Biol. 7:21-29.
    • (2005) Nat. Cell Biol , vol.7 , pp. 21-29
    • Gohla, A.1    Birkenfeld, J.2    Bokoch, G.M.3
  • 18
    • 12844269159 scopus 로고    scopus 로고
    • Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells
    • Hotulainen, P., E. Paunola, M.K. Vartiainen, and P. Lappalainen. 2005. Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells. Mol. Biol. Cell. 16:649-664.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 649-664
    • Hotulainen, P.1    Paunola, E.2    Vartiainen, M.K.3    Lappalainen, P.4
  • 20
    • 0037039167 scopus 로고    scopus 로고
    • Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex
    • Ichetovkin, I., W. Grant, and J. Condeelis. 2002. Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex. Curr. Biol. 12:79-84.
    • (2002) Curr. Biol , vol.12 , pp. 79-84
    • Ichetovkin, I.1    Grant, W.2    Condeelis, J.3
  • 21
    • 33847315536 scopus 로고    scopus 로고
    • Spatial and temporal relationships between actin-filament nucleation, capping, and disassembly
    • Iwasa, J.H., and R.D. Mullins. 2007. Spatial and temporal relationships between actin-filament nucleation, capping, and disassembly. Curr. Biol. 17:395-406.
    • (2007) Curr. Biol , vol.17 , pp. 395-406
    • Iwasa, J.H.1    Mullins, R.D.2
  • 24
    • 0036264824 scopus 로고    scopus 로고
    • The ADF/cofilin family: Actin-remodeling proteins
    • 3:reviews3007
    • Maciver, S.K., and P.J. Hussey. 2002. The ADF/cofilin family: actin-remodeling proteins. Genome Biol. 3:reviews3007.
    • (2002) Genome Biol
    • Maciver, S.K.1    Hussey, P.J.2
  • 25
    • 0031952055 scopus 로고    scopus 로고
    • Actin depolymerizing factor and cofilin phosphorylation dynamics: Response to signals that regulate neurite extension
    • Meberg, P.J., S. Ono, L.S. Minamide, M. Takahashi, and J.R. Bamburg. 1998. Actin depolymerizing factor and cofilin phosphorylation dynamics: response to signals that regulate neurite extension. Cell Motil. Cytoskeleton. 39:172-190.
    • (1998) Cell Motil. Cytoskeleton , vol.39 , pp. 172-190
    • Meberg, P.J.1    Ono, S.2    Minamide, L.S.3    Takahashi, M.4    Bamburg, J.R.5
  • 26
    • 21044455752 scopus 로고    scopus 로고
    • Localization of all seven messenger RNAs for the actin-polymerization nucleator Arp2/3 complex in the protrusions of fibroblasts
    • Mingle, L.A., N.N. Okuhama, J. Shi, R.H. Singer, J. Condeelis, and G. Liu. 2005. Localization of all seven messenger RNAs for the actin-polymerization nucleator Arp2/3 complex in the protrusions of fibroblasts. J. Cell Sci. 118:2425-2433.
    • (2005) J. Cell Sci , vol.118 , pp. 2425-2433
    • Mingle, L.A.1    Okuhama, N.N.2    Shi, J.3    Singer, R.H.4    Condeelis, J.5    Liu, G.6
  • 27
    • 0028335706 scopus 로고
    • Identification of a human cDNA encoding a novel protein kinase with two repeats of the LIM/double zinc finger motif
    • Mizuno, K., I. Okano, K. Ohashi, K. Nunoue, K. Kuma, T. Miyata, and T. Nakamura. 1994. Identification of a human cDNA encoding a novel protein kinase with two repeats of the LIM/double zinc finger motif. Oncogene. 9:1605-1612.
    • (1994) Oncogene , vol.9 , pp. 1605-1612
    • Mizuno, K.1    Okano, I.2    Ohashi, K.3    Nunoue, K.4    Kuma, K.5    Miyata, T.6    Nakamura, T.7
  • 29
    • 33750948427 scopus 로고    scopus 로고
    • Spatial and temporal control of cofilin activity is required for directional sensing during chemotaxis
    • Mouneimne, G., V. Desmarais, M. Sidani, E. Scemes, W. Wang, X. Song, R. Eddy, and J. Condeelis. 2006. Spatial and temporal control of cofilin activity is required for directional sensing during chemotaxis. Curr. Biol. 16:2193-2205.
    • (2006) Curr. Biol , vol.16 , pp. 2193-2205
    • Mouneimne, G.1    Desmarais, V.2    Sidani, M.3    Scemes, E.4    Wang, W.5    Song, X.6    Eddy, R.7    Condeelis, J.8
  • 30
    • 0037169335 scopus 로고    scopus 로고
    • Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin
    • Niwa, R., K. Nagata-Ohashi, M. Takeichi, K. Mizuno, and T. Uemura. 2002. Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell. 108:233-246.
    • (2002) Cell , vol.108 , pp. 233-246
    • Niwa, R.1    Nagata-Ohashi, K.2    Takeichi, M.3    Mizuno, K.4    Uemura, T.5
  • 31
    • 0029166671 scopus 로고
    • Rho, rac and cdc42 GTPases: Regulators of actin structures, cell adhesion and motility
    • Nobes, C.D., and A. Hall. 1995. Rho, rac and cdc42 GTPases: regulators of actin structures, cell adhesion and motility. Biochem. Soc. Trans. 23:456-459.
    • (1995) Biochem. Soc. Trans , vol.23 , pp. 456-459
    • Nobes, C.D.1    Hall, A.2
  • 32
    • 0029594144 scopus 로고
    • Identification and characterization of a novel family of serine/threonine kinases containing two N-terminal LIM motifs
    • Okano, I., J. Hiraoka, H. Otera, K. Nunoue, K. Ohashi, S. Iwashita, M. Hirai, and K. Mizuno. 1995. Identification and characterization of a novel family of serine/threonine kinases containing two N-terminal LIM motifs. J. Biol. Chem. 270:31321-31330.
    • (1995) J. Biol. Chem , vol.270 , pp. 31321-31330
    • Okano, I.1    Hiraoka, J.2    Otera, H.3    Nunoue, K.4    Ohashi, K.5    Iwashita, S.6    Hirai, M.7    Mizuno, K.8
  • 33
    • 33847295719 scopus 로고    scopus 로고
    • Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics
    • Ono, S. 2007. Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics. Int. Rev. Cytol. 258:1-82.
    • (2007) Int. Rev. Cytol , vol.258 , pp. 1-82
    • Ono, S.1
  • 34
    • 0141433278 scopus 로고    scopus 로고
    • Molecular requirements for actin-based lamella formation in Drosophila S2 cells
    • Rogers, S.L., U. Wiedemann, N. Stuurman, and R.D. Vale. 2003. Molecular requirements for actin-based lamella formation in Drosophila S2 cells. J. Cell Biol. 162:1079-1088.
    • (2003) J. Cell Biol , vol.162 , pp. 1079-1088
    • Rogers, S.L.1    Wiedemann, U.2    Stuurman, N.3    Vale, R.D.4
  • 35
    • 0042354574 scopus 로고    scopus 로고
    • Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis
    • Sahai, E., and C.J. Marshall. 2003. Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis. Nat. Cell Biol. 5:711-719.
    • (2003) Nat. Cell Biol , vol.5 , pp. 711-719
    • Sahai, E.1    Marshall, C.J.2
  • 37
    • 0033559605 scopus 로고    scopus 로고
    • Correlation of beta-actin messenger RNA localization with metastatic potential in rat adenocarcinoma cell lines
    • Shestakova, E.A., J. Wyckoff, J. Jones, R.H. Singer, and J. Condeelis. 1999. Correlation of beta-actin messenger RNA localization with metastatic potential in rat adenocarcinoma cell lines. Cancer Res. 59:1202-1205.
    • (1999) Cancer Res , vol.59 , pp. 1202-1205
    • Shestakova, E.A.1    Wyckoff, J.2    Jones, J.3    Singer, R.H.4    Condeelis, J.5
  • 39
    • 0035903099 scopus 로고    scopus 로고
    • Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells
    • Toshima, J., J.Y. Toshima, K. Takeuchi, R. Mori, and K. Mizuno. 2001. Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells. J. Biol. Chem. 276:31449-31458.
    • (2001) J. Biol. Chem , vol.276 , pp. 31449-31458
    • Toshima, J.1    Toshima, J.Y.2    Takeuchi, K.3    Mori, R.4    Mizuno, K.5
  • 42
    • 34249281332 scopus 로고    scopus 로고
    • The cofilin pathway in breast cancer invasion and metastasis
    • Wang, W., R. Eddy, and J. Condeelis. 2007a. The cofilin pathway in breast cancer invasion and metastasis. Nat. Rev. Cancer. 7:429-440.
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 429-440
    • Wang, W.1    Eddy, R.2    Condeelis, J.3
  • 43
    • 34248586312 scopus 로고    scopus 로고
    • Coordinated regulation of pathways for enhanced cell motility and chemotaxis is conserved in rat and mouse mammary tumors
    • Wang, W., J.B. Wyckoff, S. Goswami, Y. Wang, M. Sidani, J.E. Segall, and J.S. Condeelis. 2007b. Coordinated regulation of pathways for enhanced cell motility and chemotaxis is conserved in rat and mouse mammary tumors. Cancer Res. 67:3505-3511.
    • (2007) Cancer Res , vol.67 , pp. 3505-3511
    • Wang, W.1    Wyckoff, J.B.2    Goswami, S.3    Wang, Y.4    Sidani, M.5    Segall, J.E.6    Condeelis, J.S.7
  • 44
    • 0032462246 scopus 로고    scopus 로고
    • A computer-assisted system for reconstructing and interpreting the dynamic three-dimensional relationships of the outer surface, nucleus and pseudopods of crawling cells
    • Wessels, D., E. Voss, N. Von Bergen, R. Burns, J. Stites, and D.R. Soll. 1998. A computer-assisted system for reconstructing and interpreting the dynamic three-dimensional relationships of the outer surface, nucleus and pseudopods of crawling cells. Cell Motil. Cytoskeleton. 41:225-246.
    • (1998) Cell Motil. Cytoskeleton , vol.41 , pp. 225-246
    • Wessels, D.1    Voss, E.2    Von Bergen, N.3    Burns, R.4    Stites, J.5    Soll, D.R.6
  • 46
    • 33746562929 scopus 로고    scopus 로고
    • ROCK- and myosin-dependent matrix deformation enables protease-independent tumor-cell invasion in vivo
    • Wyckoff, J.B., S.E. Pinner, S. Gschmeissner, J.S. Condeelis, and E. Sahai. 2006. ROCK- and myosin-dependent matrix deformation enables protease-independent tumor-cell invasion in vivo. Curr. Biol. 16:1515-1523.
    • (2006) Curr. Biol , vol.16 , pp. 1515-1523
    • Wyckoff, J.B.1    Pinner, S.E.2    Gschmeissner, S.3    Condeelis, J.S.4    Sahai, E.5
  • 48
    • 34247468876 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton in cancer cell migration and invasion
    • Yamaguchi, H., and J. Condeelis. 2007. Regulation of the actin cytoskeleton in cancer cell migration and invasion. Biochim. Biophys. Acta. 1773:642-652.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 642-652
    • Yamaguchi, H.1    Condeelis, J.2
  • 50
    • 0025277362 scopus 로고
    • Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides
    • Yonezawa, N., E. Nishida, K. Iida, I. Yahara, and H. Sakai. 1990. Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides. J. Biol. Chem. 265:8382-8386.
    • (1990) J. Biol. Chem , vol.265 , pp. 8382-8386
    • Yonezawa, N.1    Nishida, E.2    Iida, K.3    Yahara, I.4    Sakai, H.5
  • 51
    • 0026044059 scopus 로고
    • A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin
    • Yonezawa, N., Y. Homma, I. Yahara, H. Sakai, and E. Nishida. 1991. A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin. J. Biol. Chem. 266:17218-17221.
    • (1991) J. Biol. Chem , vol.266 , pp. 17218-17221
    • Yonezawa, N.1    Homma, Y.2    Yahara, I.3    Sakai, H.4    Nishida, E.5
  • 52
    • 0034722329 scopus 로고    scopus 로고
    • Phosphorylation of ADF/cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequent lamellipod extension
    • Zebda, N., O. Bernard, M. Bailly, S. Welti, D.S. Lawrence, and J.S. Condeelis. 2000. Phosphorylation of ADF/cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequent lamellipod extension. J. Cell Biol. 151:1119-1128.
    • (2000) J. Cell Biol , vol.151 , pp. 1119-1128
    • Zebda, N.1    Bernard, O.2    Bailly, M.3    Welti, S.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 53
    • 12244262321 scopus 로고    scopus 로고
    • Products of phosphoinositide specific phospholipase C can trigger dephosphorylation of cofilin in chemoattractant stimulated neutrophils
    • Zhan, Q., J.R. Bamburg, and J.A. Badwey. 2003. Products of phosphoinositide specific phospholipase C can trigger dephosphorylation of cofilin in chemoattractant stimulated neutrophils. Cell Motil. Cytoskeleton. 54:1-15.
    • (2003) Cell Motil. Cytoskeleton , vol.54 , pp. 1-15
    • Zhan, Q.1    Bamburg, J.R.2    Badwey, J.A.3
  • 54
    • 0037089078 scopus 로고    scopus 로고
    • Phosphorylation of the myosin regulatory light chain plays a role in motility and polarity during Dictyostelium chemotaxis
    • Zhang, H., D. Wessels, P. Fey, K. Daniels, R.L. Chisholm, and D.R. Soll. 2002. Phosphorylation of the myosin regulatory light chain plays a role in motility and polarity during Dictyostelium chemotaxis. J. Cell Sci. 115:1733-1747.
    • (2002) J. Cell Sci , vol.115 , pp. 1733-1747
    • Zhang, H.1    Wessels, D.2    Fey, P.3    Daniels, K.4    Chisholm, R.L.5    Soll, D.R.6


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