메뉴 건너뛰기




Volumn 14, Issue 8, 2003, Pages 3065-3081

Activity and distribution of paxillin, focal adhesion kinase, and cadherin indicate cooperative roles during zebrafish morphogenesis

Author keywords

[No Author keywords available]

Indexed keywords

CADHERIN; COLLAGEN FIBER; FIBRONECTIN; FOCAL ADHESION KINASE; PAXILLIN; PROTEIN FAK; UNCLASSIFIED DRUG;

EID: 0041468624     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E02-08-0537     Document Type: Article
Times cited : (111)

References (63)
  • 1
    • 0025125917 scopus 로고
    • The mechanics of notochord elongation, straightening and stiffening in the embryo of Xenopus laevis
    • Adams, D.S., Keller, R., and Ma, K. (1990). The mechanics of notochord elongation, straightening and stiffening in the embryo of Xenopus laevis. Development 110, 115-130.
    • (1990) Development , vol.110 , pp. 115-130
    • Adams, D.S.1    Keller, R.2    Ma, K.3
  • 6
    • 0018156935 scopus 로고
    • Contact relations, surface activity, and cortical microfilaments in marginal cells of the enveloping layer of the yolk syncytial and yolk cytoplasmic layers of Fundulus before and during epiboly
    • Betchaku, T., and Trinkaus, J.P. (1978). Contact relations, surface activity, and cortical microfilaments in marginal cells of the enveloping layer of the yolk syncytial and yolk cytoplasmic layers of Fundulus before and during epiboly. J. Exp. Zool. 206, 381-426.
    • (1978) J. Exp. Zool. , vol.206 , pp. 381-426
    • Betchaku, T.1    Trinkaus, J.P.2
  • 7
    • 0027940284 scopus 로고
    • Structure and distribution of N-cadherin in developing zebrafish embryos: Morphogenetic effects of ectopic over-expression
    • Bitzur, S., Kam, Z., and Geiger, B. (1994). Structure and distribution of N-cadherin in developing zebrafish embryos: morphogenetic effects of ectopic over-expression. Dev. Dyn. 201, 121-136.
    • (1994) Dev. Dyn , vol.201 , pp. 121-136
    • Bitzur, S.1    Kam, Z.2    Geiger, B.3
  • 8
    • 0031822185 scopus 로고    scopus 로고
    • Paxillin LD motifs may define a new family of protein recognition domains
    • Brown, M.C., Curtis, M.S., and Turner, C.E. (1998). Paxillin LD motifs may define a new family of protein recognition domains. Nat. Struct. Biol. 5, 677-678.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 677-678
    • Brown, M.C.1    Curtis, M.S.2    Turner, C.E.3
  • 9
    • 0035999990 scopus 로고    scopus 로고
    • Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesion involves a multistep activation pathway
    • Brown, M.C., West, K.A., and Turner, C.E. (2002). Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesion involves a multistep activation pathway. Mol. Biol. Cell 13, 1550-1565.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1550-1565
    • Brown, M.C.1    West, K.A.2    Turner, C.E.3
  • 10
    • 0036205320 scopus 로고    scopus 로고
    • SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading
    • Cary, L.A., Klinghoffer, R.A., Sachsenmaier, C., and Cooper, J.A. (2002). SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading. Mol. Cell. Biol. 22, 2427-2440.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2427-2440
    • Cary, L.A.1    Klinghoffer, R.A.2    Sachsenmaier, C.3    Cooper, J.A.4
  • 12
    • 0028989016 scopus 로고
    • Notch1 is required for the coordinate segmentation of somites
    • Conlon, R.A., Reaume, A.G., and Rossant, J. (1995). Notch1 is required for the coordinate segmentation of somites. Development 121, 1533-1545.
    • (1995) Development , vol.121 , pp. 1533-1545
    • Conlon, R.A.1    Reaume, A.G.2    Rossant, J.3
  • 13
    • 0003116087 scopus 로고    scopus 로고
    • Morphogenetic cell behaviors and specification of cell fate during early teleost development, in Motion Analysis of Living Cells, ed
    • Cooper, M.S., and Kimmel, C.B. (1998). Morphogenetic cell behaviors and specification of cell fate during early teleost development, in Motion Analysis of Living Cells, ed. D.R. Soll and D. Wessels, New York: Wiley-Liss, 177-220.
    • (1998) D.R. Soll and D. Wessels, New York: Wiley-Liss , pp. 177-220
    • Cooper, M.S.1    Kimmel, C.B.2
  • 14
    • 0031735369 scopus 로고    scopus 로고
    • Medial cell mixing during axial morphogenesis of the amphibian embryo requires cadherin function
    • Delarue, M., Saez, F.J., Boucaut, J.-C., Thiery, J.-P., and Broders, F. (1998). Medial cell mixing during axial morphogenesis of the amphibian embryo requires cadherin function. Dev. Dyn. 213, 248-260.
    • (1998) Dev. Dyn. , vol.213 , pp. 248-260
    • Delarue, M.1    Saez, F.J.2    Boucaut, J.-C.3    Thiery, J.-P.4    Broders, F.5
  • 16
    • 0028783271 scopus 로고
    • Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase
    • Furuta, Y., Ilic, D., Kanazawa, S., Takeda, N., Yamamoto, T., and Aizawa, S. (1995). Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK. Oncogene 11, 1989-1995.
    • (1995) FAK. Oncogene , vol.11 , pp. 1989-1995
    • Furuta, Y.1    Ilic, D.2    Kanazawa, S.3    Takeda, N.4    Yamamoto, T.5    Aizawa, S.6
  • 18
    • 0029804825 scopus 로고    scopus 로고
    • Mesodermal development in mouse embryos mutant for fibronectin
    • Georges-Labouesse, E.N., George, E.L., Rayburn, H., and Hynes, R.O. (1996). Mesodermal development in mouse embryos mutant for fibronectin. Dev. Dyn. 207, 145-156.
    • (1996) Dev. Dyn. , vol.207 , pp. 145-156
    • Georges-Labouesse, E.N.1    George, E.L.2    Rayburn, H.3    Hynes, R.O.4
  • 19
    • 0030272089 scopus 로고    scopus 로고
    • Immunohistochemical localization of type I and II collagens in the involuting chick notochords in vivo and in vitro
    • Ghanem, E. (1996). Immunohistochemical localization of type I and II collagens in the involuting chick notochords in vivo and in vitro. Cell Biol. Int. 20, 681-685.
    • (1996) Cell Biol. Int. , vol.20 , pp. 681-685
    • Ghanem, E.1
  • 20
    • 0034614941 scopus 로고    scopus 로고
    • Regulation of cadherin adhesive activity
    • Gumbiner, B.M. (2000). Regulation of cadherin adhesive activity. J. Cell Biol. 148, 399-403.
    • (2000) J. Cell Biol. , vol.148 , pp. 399-403
    • Gumbiner, B.M.1
  • 21
    • 0036142219 scopus 로고    scopus 로고
    • The adapter protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling
    • Hagel, M., George, E.L., Kim, A., Tamimi, R., Opitz, S.L., Turner, C.E., Imamoto, A., and Thomas, S.M. (2002). The adapter protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling. Mol. Cell. Biol. 22, 901-915.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 901-915
    • Hagel, M.1    George, E.L.2    Kim, A.3    Tamimi, R.4    Opitz, S.L.5    Turner, C.E.6    Imamoto, A.7    Thomas, S.M.8
  • 22
    • 0031081425 scopus 로고    scopus 로고
    • Signaling through focal adhesion kinase
    • Hanks, S.K., and Polte, T.R. (1997). Signaling through focal adhesion kinase. Bioessays 19, 137-145.
    • (1997) Bioessays , vol.19 , pp. 137-145
    • Hanks, S.K.1    Polte, T.R.2
  • 23
    • 0034618651 scopus 로고    scopus 로고
    • Somites in zebrafish doubly mutant for knypek and trilobite from without internal mesenchymal cells or compaction
    • Henry, C.A., Hall, L.A., Hille, M.B., Solnica-Krezel, L., and Cooper, M.S. (2000). Somites in zebrafish doubly mutant for knypek and trilobite from without internal mesenchymal cells or compaction. Curr. Biol. 10, 1063-1066.
    • (2000) Curr. Biol. , vol.10 , pp. 1063-1066
    • Henry, C.A.1    Hall, L.A.2    Hille, M.B.3    Solnica-Krezel, L.4    Cooper, M.S.5
  • 24
  • 25
    • 0036679340 scopus 로고    scopus 로고
    • Two linked hairy/Enhancer of split-related Zebrafish genes, her1 and her7, function together to refine alternating somite boundaries
    • Henry, C.A., et al. (2002). Two linked hairy/Enhancer of split-related Zebrafish genes, her1 and her7, function together to refine alternating somite boundaries. Development 129, 3693-3704.
    • (2002) Development , vol.129 , pp. 3693-3704
    • Henry, C.A.1
  • 26
    • 0029153296 scopus 로고
    • Molecular analysis and developmental expression of the focal adhesion kinase pp125FAK in Xenopus laevis
    • Hens, M.D., and DeSimone, D.W. (1995). Molecular analysis and developmental expression of the focal adhesion kinase pp125FAK in Xenopus laevis. Dev. Biol. 170, 274-288.
    • (1995) Dev. Biol. , vol.170 , pp. 274-288
    • Hens, M.D.1    DeSimone, D.W.2
  • 27
    • 0036332729 scopus 로고    scopus 로고
    • her1 and the notch pathway function within the oscillator mechanism that regulates zebrafish somitogenesis
    • Holley, S.A., Jülich, D., Rauch, G.-J., Geisler, R., and Nüsslein-Volhard, C. (2002). her1 and the notch pathway function within the oscillator mechanism that regulates zebrafish somitogenesis. Development 129, 1175-1183.
    • (2002) Development , vol.129 , pp. 1175-1183
    • Holley, S.A.1    Jülich, D.2    Rauch, G.-J.3    Geisler, R.4    Nüsslein-Volhard, C.5
  • 28
    • 0036228744 scopus 로고    scopus 로고
    • Intercellular adhesion, signalling and the cytoskeleton
    • Jamora, C., and Fuchs, E. (2002). Intercellular adhesion, signalling and the cytoskeleton. Nat. Cell Biol. 4, 101-108.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 101-108
    • Jamora, C.1    Fuchs, E.2
  • 29
    • 0027095634 scopus 로고
    • Mitotic domains in the early embryo of the zebrafish
    • Kane, D.A., Warga, R.M., and Kimmel, C.B. (1992). Mitotic domains in the early embryo of the zebrafish. Nature 360, 735-737.
    • (1992) Nature , vol.360 , pp. 735-737
    • Kane, D.A.1    Warga, R.M.2    Kimmel, C.B.3
  • 30
  • 32
    • 0025280180 scopus 로고
    • Distribution of integrins and their ligands in the trunk of Xenopus laevis during neural crest cell migration
    • Krotoski, D., and Bronner-Fraser, M. (1990). Distribution of integrins and their ligands in the trunk of Xenopus laevis during neural crest cell migration. J. Exp. Zool. 253, 139-150.
    • (1990) J. Exp. Zool. , vol.253 , pp. 139-150
    • Krotoski, D.1    Bronner-Fraser, M.2
  • 33
    • 0028858038 scopus 로고
    • Disruption of gastrulation movements in Xenopus by a dominant-negative mutant for C-cadherin
    • Lee, C.-H., and Gumbiner, B.M. (1995). Disruption of gastrulation movements in Xenopus by a dominant-negative mutant for C-cadherin. Dev. Biol. 171, 363-373.
    • (1995) Dev. Biol. , vol.171 , pp. 363-373
    • Lee, C.-H.1    Gumbiner, B.M.2
  • 35
    • 0031049279 scopus 로고    scopus 로고
    • Expression of genes encoding the collagen-binding heat shock protein (Hsp47) and type II collage in developing zebrafish embryos
    • Lele, Z., and Krone, P.H. (1997). Expression of genes encoding the collagen-binding heat shock protein (Hsp47) and type II collage in developing zebrafish embryos. Mech. Dev. 61, 89-98.
    • (1997) Mech. Dev. , vol.61 , pp. 89-98
    • Lele, Z.1    Krone, P.H.2
  • 36
    • 0028293208 scopus 로고
    • Selective disruption of E-cadherin function in early Xenopus embryos by a dominant negative mutant
    • Levine, E., Lee, C.H., Kintner, C., and Gumbiner, B.M. (1994). Selective disruption of E-cadherin function in early Xenopus embryos by a dominant negative mutant. Development 120, 901-909.
    • (1994) Development , vol.120 , pp. 901-909
    • Levine, E.1    Lee, C.H.2    Kintner, C.3    Gumbiner, B.M.4
  • 39
    • 0034725624 scopus 로고    scopus 로고
    • v-Src induces tyrosine phosphorylation of focal adhesion kinase independently of tyrosine 397 and formation of a complex with Src
    • McLean, G.W., Fincham, V.J., and Frame, M.C. (2000). v-Src induces tyrosine phosphorylation of focal adhesion kinase independently of tyrosine 397 and formation of a complex with Src. J. Biol. Chem. 275, 23333-23339.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23333-23339
    • McLean, G.W.1    Fincham, V.J.2    Frame, M.C.3
  • 40
    • 0035963486 scopus 로고    scopus 로고
    • mRNA sequence of the Xenopus laevis paxillin gene and its expression
    • Ogawa, M., Hiraoka, Y., Taniguchi, K., Sakai, Y., and Aiso, S. (2001). mRNA sequence of the Xenopus laevis paxillin gene and its expression. Biochim. Biophys. Acta 1519, 235-240.
    • (2001) Biochim. Biophys. Acta , vol.1519 , pp. 235-240
    • Ogawa, M.1    Hiraoka, Y.2    Taniguchi, K.3    Sakai, Y.4    Aiso, S.5
  • 42
    • 0028223702 scopus 로고
    • Focal adhesion kinase is abundant in developing blood vessels and elevation of its phosphotyrosine content in vascular smooth muscle cells is a rapid response to angiotensin II
    • Polte, T.R., Naftilan, A.J., and Hanks, S.K. (1994). Focal adhesion kinase is abundant in developing blood vessels and elevation of its phosphotyrosine content in vascular smooth muscle cells is a rapid response to angiotensin II. J. Cell. Biochem. 55, 106-119.
    • (1994) J. Cell. Biochem. , vol.55 , pp. 106-119
    • Polte, T.R.1    Naftilan, A.J.2    Hanks, S.K.3
  • 44
    • 0034307393 scopus 로고    scopus 로고
    • Transient nuclear localization of Fyn kinase during development in zebrafish
    • Rongish, B.J., and Kinsey, W.H. (2000). Transient nuclear localization of Fyn kinase during development in zebrafish. Anat. Rec. 260, 115-123.
    • (2000) Anat. Rec. , vol.260 , pp. 115-123
    • Rongish, B.J.1    Kinsey, W.H.2
  • 45
    • 0035671094 scopus 로고    scopus 로고
    • Fak regulates tyrosine phosphorylation of CAS, paxillin, and PYK2 in cells expressing v-Src, but is not a critical determinant of v-Src transformation
    • Roy, S., Ruest, P.J., and Hanks, S.K. (2002). Fak regulates tyrosine phosphorylation of CAS, paxillin, and PYK2 in cells expressing v-Src, but is not a critical determinant of v-Src transformation. J. Cell. Biochem. 84, 377-388.
    • (2002) J. Cell. Biochem. , vol.84 , pp. 377-388
    • Roy, S.1    Ruest, P.J.2    Hanks, S.K.3
  • 46
    • 0031915021 scopus 로고    scopus 로고
    • Integrin signaling and tyrosine phosphorylation: Just the FAKs?
    • Schlaepfer, D.D., and Hunter, T. (1998). Integrin signaling and tyrosine phosphorylation: just the FAKs? Trends Cell Biol. 8, 151-157.
    • (1998) Trends Cell Biol. , vol.8 , pp. 151-157
    • Schlaepfer, D.D.1    Hunter, T.2
  • 47
    • 0035575458 scopus 로고    scopus 로고
    • Integrin signaling revisited
    • Schwartz, M.A. (2001). Integrin signaling revisited. Trends Cell Biol. 11, 466-470.
    • (2001) Trends Cell Biol. , vol.11 , pp. 466-470
    • Schwartz, M.A.1
  • 48
    • 2442743988 scopus 로고    scopus 로고
    • ZO1 in corneal epithelium: Association to the zonula occludens and adherens junctions
    • Sugrue, S.P., and Zieske, J.D. (1997). ZO1 in corneal epithelium: association to the zonula occludens and adherens junctions. Exp. Eye Res. 64, 11-20.
    • (1997) Exp. Eye Res. , vol.64 , pp. 11-20
    • Sugrue, S.P.1    Zieske, J.D.2
  • 49
    • 12644303220 scopus 로고    scopus 로고
    • Mutations affecting development of the notochord in zebrafish
    • Stemple, D.L. (1996). Mutations affecting development of the notochord in zebrafish. Development 123, 117-128.
    • (1996) Development , vol.123 , pp. 117-128
    • Stemple, D.L.1
  • 50
    • 12444317792 scopus 로고    scopus 로고
    • Role of c-Yes kinase during gastrulation of the zebrafish embryos
    • Tsai, W., and Kinsey, W.H. (2002). Role of c-Yes kinase during gastrulation of the zebrafish embryos. Mol. Biol. Cell 13, 117a.
    • (2002) Mol. Biol. Cell , vol.13
    • Tsai, W.1    Kinsey, W.H.2
  • 51
    • 0031439110 scopus 로고    scopus 로고
    • The bovine papillomavirus E6 protein binds to the LD motif repeats of paxillin and blocks its interaction with vinculin and the focal adhesion kinase
    • Tong, X., Salgia, R., Li, J.-L., Griffin, J.D., and Howley, P.M. (1997). The bovine papillomavirus E6 protein binds to the LD motif repeats of paxillin and blocks its interaction with vinculin and the focal adhesion kinase. J. Biol. Chem. 272, 33373-33376.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33373-33376
    • Tong, X.1    Salgia, R.2    Li, J.-L.3    Griffin, J.D.4    Howley, P.M.5
  • 52
    • 0026042575 scopus 로고
    • Paxillin is a major phosphotyrosine-containing protein during embryonic development
    • Turner, C.E. (1991). Paxillin is a major phosphotyrosine-containing protein during embryonic development. J. Cell Biol. 115, 201-207.
    • (1991) J. Cell Biol. , vol.115 , pp. 201-207
    • Turner, C.E.1
  • 53
    • 0033666291 scopus 로고    scopus 로고
    • Paxillin and focal adhesion signalling
    • Turner, C.E. (2000a). Paxillin and focal adhesion signalling. Nat. Cell Biol. 2, E231-E236.
    • (2000) Nat. Cell Biol. , vol.2
    • Turner, C.E.1
  • 54
    • 0034529411 scopus 로고    scopus 로고
    • Paxillin interactions
    • Turner, C.E. (2000b). Paxillin interactions. J. Cell Sci. 113, 4139-4140.
    • (2000) J. Cell Sci , vol.113 , pp. 4139-4140
    • Turner, C.E.1
  • 55
    • 0035833251 scopus 로고    scopus 로고
    • The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL)
    • West, K.A., Zhang, H., Brown, M.C., Nikolopoulos, S.N., Riedy, M.C., Horwitz, A.F., and Turner, C.E. (2001). The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL). J. Cell Biol. 154, 161-176.
    • (2001) J. Cell Biol. , vol.154 , pp. 161-176
    • West, K.A.1    Zhang, H.2    Brown, M.C.3    Nikolopoulos, S.N.4    Riedy, M.C.5    Horwitz, A.F.6    Turner, C.E.7
  • 57
    • 0030220280 scopus 로고    scopus 로고
    • Fibronectin, mesodermal migration and gastrulation
    • Winklbauer, R., and Keller, R.E. (1996). Fibronectin, mesodermal migration and gastrulation. Dev. Biol. 177, 413-426.
    • (1996) Dev. Biol. , vol.177 , pp. 413-426
    • Winklbauer, R.1    Keller, R.E.2
  • 59
    • 0028102721 scopus 로고
    • Patterns of cell behaviour underlying somitogenesis and notochord formation in intact vertebrate embryos
    • Wood, A., and Thorogood, P. (1994). Patterns of cell behaviour underlying somitogenesis and notochord formation in intact vertebrate embryos. Dev. Dyn. 201, 151-167.
    • (1994) Dev. Dyn. , vol.201 , pp. 151-167
    • Wood, A.1    Thorogood, P.2
  • 60
    • 0029036264 scopus 로고
    • Expression of a type II collagen gene in the zebrafish embryonic axis
    • Yan, Y.L., Hatta, K., Riggleman, B., and Postlethwait, J.H. (1995). Expression of a type II collagen gene in the zebrafish embryonic axis. Dev. Dyn. 203, 363-376.
    • (1995) Dev. Dyn. , vol.203 , pp. 363-376
    • Yan, Y.L.1    Hatta, K.2    Riggleman, B.3    Postlethwait, J.H.4
  • 61
    • 0033571018 scopus 로고    scopus 로고
    • Overlapping and independent functions of fibronectin receptor integrins in early mesodermal development
    • Yang, J.T., Bader, B.L., Kreidberg, J.A., Ullman-Cullere, M., Trevithick, J.E., and Hynes, R.O. (1999). Overlapping and independent functions of fibronectin receptor integrins in early mesodermal development. Dev. Biol. 215, 264-277.
    • (1999) Dev. Biol. , vol.215 , pp. 264-277
    • Yang, J.T.1    Bader, B.L.2    Kreidberg, J.A.3    Ullman-Cullere, M.4    Trevithick, J.E.5    Hynes, R.O.6
  • 62
    • 0033374836 scopus 로고    scopus 로고
    • Cell adhesion and the actin cytoskeleton of the enveloping layer in the zebrafish embryo during epiboly
    • Zalik, S.E., Lewandowski, E., Kam, Z., and Geiger, B. (1999). Cell adhesion and the actin cytoskeleton of the enveloping layer in the zebrafish embryo during epiboly. Biochem. Cell Biol. 77, 527-542.
    • (1999) Biochem. Cell Biol. , vol.77 , pp. 527-542
    • Zalik, S.E.1    Lewandowski, E.2    Kam, Z.3    Geiger, B.4
  • 63
    • 0035082264 scopus 로고    scopus 로고
    • Type IIA procollagen in development of the human intervertebral disc: Regulated expression of the NH(2)-propeptide by enzymic processing reveals a unique developmental pathway
    • Zhu, Y., McAlinden, A., and Sandell, L.J. (2001). Type IIA procollagen in development of the human intervertebral disc: regulated expression of the NH(2)-propeptide by enzymic processing reveals a unique developmental pathway. Dev. Dyn. 220, 350-362.
    • (2001) Dev. Dyn. , vol.220 , pp. 350-362
    • Zhu, Y.1    McAlinden, A.2    Sandell, L.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.