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Volumn 123, Issue 11, 2006, Pages 801-818

Drosophila α-actinin in ovarian follicle cells is regulated by EGFR and Dpp signalling and required for cytoskeletal remodelling

Author keywords

Actinin mutant; Dorsal appendages; Ena; Integrin; Oogenesis; Stress fibres; Usp

Indexed keywords

ALPHA ACTININ; DECAPENTAPLEGIC PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR; F ACTIN;

EID: 33750816535     PISSN: 09254773     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mod.2006.08.004     Document Type: Article
Times cited : (17)

References (66)
  • 1
    • 0035806975 scopus 로고    scopus 로고
    • The receptor tyrosine phosphatase Dlar and integrins organize actin filaments in the Drosophila follicular epithelium
    • Bateman J., Reddy R.S., Saito H., and Van Vactor D. The receptor tyrosine phosphatase Dlar and integrins organize actin filaments in the Drosophila follicular epithelium. Curr. Biol. 11 (2001) 1317-1327
    • (2001) Curr. Biol. , vol.11 , pp. 1317-1327
    • Bateman, J.1    Reddy, R.S.2    Saito, H.3    Van Vactor, D.4
  • 2
    • 0034785272 scopus 로고    scopus 로고
    • Spatial control of the actin cytoskeleton in Drosophila epithelial cells
    • Baum B., and Perrimon N. Spatial control of the actin cytoskeleton in Drosophila epithelial cells. Nat. Cell Biol. 3 (2001) 883-890
    • (2001) Nat. Cell Biol. , vol.3 , pp. 883-890
    • Baum, B.1    Perrimon, N.2
  • 3
    • 18344395156 scopus 로고    scopus 로고
    • Integrin-independent repression of cadherin transcription by talin during axis formation in Drosophila
    • Bécam I.E., Tanentzapf G., Lepesant J.A., Brown N.H., and Huynh J.R. Integrin-independent repression of cadherin transcription by talin during axis formation in Drosophila. Nat. Cell Biol. 7 (2005) 510-516
    • (2005) Nat. Cell Biol. , vol.7 , pp. 510-516
    • Bécam, I.E.1    Tanentzapf, G.2    Lepesant, J.A.3    Brown, N.H.4    Huynh, J.R.5
  • 4
    • 0036711804 scopus 로고    scopus 로고
    • Regulation of focal complex composition and disassembly by the calcium-dependent protease calpain
    • Bhatt A., Kaverina I., Otey C., and Huttenlocher A. Regulation of focal complex composition and disassembly by the calcium-dependent protease calpain. J. Cell Sci. 115 (2002) 3415-3425
    • (2002) J. Cell Sci. , vol.115 , pp. 3415-3425
    • Bhatt, A.1    Kaverina, I.2    Otey, C.3    Huttenlocher, A.4
  • 5
    • 0034235392 scopus 로고    scopus 로고
    • Integrins as mediators of morphogenesis in Drosophila
    • Brown N.H., Gregory S.L., and Martin-Bermudo M.D. Integrins as mediators of morphogenesis in Drosophila. Dev. Biol. 223 (2000) 1-16
    • (2000) Dev. Biol. , vol.223 , pp. 1-16
    • Brown, N.H.1    Gregory, S.L.2    Martin-Bermudo, M.D.3
  • 6
    • 0031805618 scopus 로고    scopus 로고
    • Signalling by the Drosophila epidermal growth factor receptor is required for the specification and diversification of embryonic muscle progenitors
    • Buff E., Carmena A., Gisselbrecht S., Jiménez F., and Michelson A.M. Signalling by the Drosophila epidermal growth factor receptor is required for the specification and diversification of embryonic muscle progenitors. Development 125 (1998) 2075-2086
    • (1998) Development , vol.125 , pp. 2075-2086
    • Buff, E.1    Carmena, A.2    Gisselbrecht, S.3    Jiménez, F.4    Michelson, A.M.5
  • 7
    • 0026761010 scopus 로고
    • Characterization of mutant alleles of myospheroid, the gene encoding the β subunit of the Drosophila PS integrins
    • Bunch T.A., Salatino R., Engelsgjerd M.C., Mukai L., West R.F., and Brower D.L. Characterization of mutant alleles of myospheroid, the gene encoding the β subunit of the Drosophila PS integrins. Genetics 132 (1992) 519-528
    • (1992) Genetics , vol.132 , pp. 519-528
    • Bunch, T.A.1    Salatino, R.2    Engelsgjerd, M.C.3    Mukai, L.4    West, R.F.5    Brower, D.L.6
  • 8
    • 0019843141 scopus 로고
    • Non-muscle α-actinins are calcium-sensitive actin-binding proteins
    • Burridge K., and Feramisco J.R. Non-muscle α-actinins are calcium-sensitive actin-binding proteins. Nature 294 (1981) 565-567
    • (1981) Nature , vol.294 , pp. 565-567
    • Burridge, K.1    Feramisco, J.R.2
  • 9
    • 2342472716 scopus 로고    scopus 로고
    • Focal adhesion and actin dynamics: a place where kinases and proteases meet to promote invasion
    • Carragher N.O., and Frame M.C. Focal adhesion and actin dynamics: a place where kinases and proteases meet to promote invasion. Trends Cell Biol. 14 (2004) 241-249
    • (2004) Trends Cell Biol. , vol.14 , pp. 241-249
    • Carragher, N.O.1    Frame, M.C.2
  • 11
    • 0030660167 scopus 로고    scopus 로고
    • Two signalling pathways specify localised expression of the Broad-Complex in Drosophila eggshell patterning and morphogenesis
    • Deng W.M., and Bownes M. Two signalling pathways specify localised expression of the Broad-Complex in Drosophila eggshell patterning and morphogenesis. Development 124 (1997) 4639-4647
    • (1997) Development , vol.124 , pp. 4639-4647
    • Deng, W.M.1    Bownes, M.2
  • 12
    • 0034913736 scopus 로고    scopus 로고
    • Top-DER- and Dpp-dependent requirements for the Drosophila fos/kayak gene in follicular epithelium morphogenesis
    • Dequier E., Souid S., Pál M., Mároy P., Lepesant J.A., and Yanicostas C. Top-DER- and Dpp-dependent requirements for the Drosophila fos/kayak gene in follicular epithelium morphogenesis. Mech. Dev. 106 (2001) 47-60
    • (2001) Mech. Dev. , vol.106 , pp. 47-60
    • Dequier, E.1    Souid, S.2    Pál, M.3    Mároy, P.4    Lepesant, J.A.5    Yanicostas, C.6
  • 13
    • 0033588277 scopus 로고    scopus 로고
    • Structure of the α-actinin rod: molecular basis for cross-linking of actin filaments
    • Djinović-Carugo K., Young P., Gautel M., and Saraste M. Structure of the α-actinin rod: molecular basis for cross-linking of actin filaments. Cell 98 (1999) 537-546
    • (1999) Cell , vol.98 , pp. 537-546
    • Djinović-Carugo, K.1    Young, P.2    Gautel, M.3    Saraste, M.4
  • 14
    • 0346600281 scopus 로고    scopus 로고
    • bullwinkle is required for epithelial morphogenesis during Drosophila oogenesis
    • Dorman J.B., James K.E., Fraser S.E., Kiehart D.P., and Berg C.A. bullwinkle is required for epithelial morphogenesis during Drosophila oogenesis. Dev. Biol. 267 (2004) 320-341
    • (2004) Dev. Biol. , vol.267 , pp. 320-341
    • Dorman, J.B.1    James, K.E.2    Fraser, S.E.3    Kiehart, D.P.4    Berg, C.A.5
  • 15
    • 0033611140 scopus 로고    scopus 로고
    • Molecular dissection of zyxin function reveals its involvement in cell motility
    • Drees B.E., Andrews K.M., and Beckerle M.C. Molecular dissection of zyxin function reveals its involvement in cell motility. J. Cell Biol. 147 (1999) 1549-1560
    • (1999) J. Cell Biol. , vol.147 , pp. 1549-1560
    • Drees, B.E.1    Andrews, K.M.2    Beckerle, M.C.3
  • 16
    • 0034495976 scopus 로고    scopus 로고
    • Genetic analysis of the requirements for α-actinin function
    • Dubreuil R.R., and Wang P. Genetic analysis of the requirements for α-actinin function. J. Muscle Res. Cell Motil. 21 (2000) 705-713
    • (2000) J. Muscle Res. Cell Motil. , vol.21 , pp. 705-713
    • Dubreuil, R.R.1    Wang, P.2
  • 17
    • 0025886649 scopus 로고
    • Structure, calmodulin-binding, and calcium-binding properties of recombinant α spectrin polypeptides
    • Dubreuil R.R., Brandin E., Reisberg J.H.S., Goldstein L.S.B., and Branton D. Structure, calmodulin-binding, and calcium-binding properties of recombinant α spectrin polypeptides. J. Biol. Chem. 266 (1991) 7189-7193
    • (1991) J. Biol. Chem. , vol.266 , pp. 7189-7193
    • Dubreuil, R.R.1    Brandin, E.2    Reisberg, J.H.S.3    Goldstein, L.S.B.4    Branton, D.5
  • 18
    • 0031816410 scopus 로고    scopus 로고
    • Identifying loci required for follicular patterning using directed mosaics
    • Duffy J.B., Harrison D.A., and Perrimon N. Identifying loci required for follicular patterning using directed mosaics. Development 125 (1998) 2263-2271
    • (1998) Development , vol.125 , pp. 2263-2271
    • Duffy, J.B.1    Harrison, D.A.2    Perrimon, N.3
  • 19
    • 0030069057 scopus 로고    scopus 로고
    • Mechanical perturbation elicits a phenotypic difference between Dictyostelium wild-type cells and cytoskeletal mutants
    • Eichinger L., Köppel B., Noegel A.A., Schleicher M., Schliwa M., Weijer K., Witke W., and Janmey P.A. Mechanical perturbation elicits a phenotypic difference between Dictyostelium wild-type cells and cytoskeletal mutants. Biophys. J. 70 (1996) 1054-1060
    • (1996) Biophys. J. , vol.70 , pp. 1054-1060
    • Eichinger, L.1    Köppel, B.2    Noegel, A.A.3    Schleicher, M.4    Schliwa, M.5    Weijer, K.6    Witke, W.7    Janmey, P.A.8
  • 21
    • 17644402480 scopus 로고    scopus 로고
    • Phosphoinositide binding regulates α-actinin dynamics: mechanism for modulating cytoskeletal remodeling
    • Fraley T.S., Pereira C.B., Tran T.C., Singleton C., and Greenwood J.A. Phosphoinositide binding regulates α-actinin dynamics: mechanism for modulating cytoskeletal remodeling. J. Biol. Chem. 280 (2005) 15479-15482
    • (2005) J. Biol. Chem. , vol.280 , pp. 15479-15482
    • Fraley, T.S.1    Pereira, C.B.2    Tran, T.C.3    Singleton, C.4    Greenwood, J.A.5
  • 22
    • 16244409866 scopus 로고    scopus 로고
    • The crystal structure of the actin binding domain from α-actinin in its closed conformation: structural insight into phospholipid regulation of α-actinin
    • Franzot G., Sjöblom B., Gautel M., and Djinović Carugo K. The crystal structure of the actin binding domain from α-actinin in its closed conformation: structural insight into phospholipid regulation of α-actinin. J. Mol. Biol. 348 (2005) 151-165
    • (2005) J. Mol. Biol. , vol.348 , pp. 151-165
    • Franzot, G.1    Sjöblom, B.2    Gautel, M.3    Djinović Carugo, K.4
  • 23
    • 0034851123 scopus 로고    scopus 로고
    • The receptor-like tyrosine phosphatase Lar is required for epithelial planar polarity and for axis determination within Drosophila ovarian follicles
    • Frydman H.M., and Spradling A.C. The receptor-like tyrosine phosphatase Lar is required for epithelial planar polarity and for axis determination within Drosophila ovarian follicles. Development 128 (2001) 3209-3220
    • (2001) Development , vol.128 , pp. 3209-3220
    • Frydman, H.M.1    Spradling, A.C.2
  • 24
    • 0026756594 scopus 로고
    • Requirement of phosphatidylinositol 4,5-bisphosphate for α-actinin function
    • Fukami K., Furuhashi K., Inagaki M., Endo T., Hatano S., and Takenawa T. Requirement of phosphatidylinositol 4,5-bisphosphate for α-actinin function. Nature 359 (1992) 150-152
    • (1992) Nature , vol.359 , pp. 150-152
    • Fukami, K.1    Furuhashi, K.2    Inagaki, M.3    Endo, T.4    Hatano, S.5    Takenawa, T.6
  • 25
    • 0030043081 scopus 로고    scopus 로고
    • Identification of a phosphatidylinositol 4,5-bisphosphate-binding site in chicken skeletal muscle α-actinin
    • Fukami K., Sawada N., Endo T., and Takenawa T. Identification of a phosphatidylinositol 4,5-bisphosphate-binding site in chicken skeletal muscle α-actinin. J. Biol. Chem. 271 (1996) 2646-2650
    • (1996) J. Biol. Chem. , vol.271 , pp. 2646-2650
    • Fukami, K.1    Sawada, N.2    Endo, T.3    Takenawa, T.4
  • 26
    • 0025325694 scopus 로고
    • Molecular genetics of Drosophila alpha-actinin: mutant alleles disrupt Z disc integrity and muscle insertions
    • Fyrberg E., Kelly M., Ball E., Fyrberg C., and Reedy M.C. Molecular genetics of Drosophila alpha-actinin: mutant alleles disrupt Z disc integrity and muscle insertions. J. Cell Biol. 110 (1990) 1999-2011
    • (1990) J. Cell Biol. , vol.110 , pp. 1999-2011
    • Fyrberg, E.1    Kelly, M.2    Ball, E.3    Fyrberg, C.4    Reedy, M.C.5
  • 27
    • 0032434538 scopus 로고    scopus 로고
    • Characterization of lethal Drosophila melanogaster α-actinin mutants
    • Fyrberg C., Ketchum A., Ball E., and Fyrberg E. Characterization of lethal Drosophila melanogaster α-actinin mutants. Biochem. Genet. 36 (1998) 299-310
    • (1998) Biochem. Genet. , vol.36 , pp. 299-310
    • Fyrberg, C.1    Ketchum, A.2    Ball, E.3    Fyrberg, E.4
  • 28
    • 0037178784 scopus 로고    scopus 로고
    • Exploring the neighborhood: adhesion-coupled cell mechanosensors
    • Geiger B., and Bershadsky A. Exploring the neighborhood: adhesion-coupled cell mechanosensors. Cell 110 (2002) 139-142
    • (2002) Cell , vol.110 , pp. 139-142
    • Geiger, B.1    Bershadsky, A.2
  • 29
    • 0027506925 scopus 로고
    • Suppression of tumorigenicity in simian virus 40-transformed 3T3 cells transfected with α-actinin cDNA
    • Glück U., Kwiatkowski D.J., and Ben-Ze'ev A. Suppression of tumorigenicity in simian virus 40-transformed 3T3 cells transfected with α-actinin cDNA. Proc. Natl. Acad. Sci. USA 90 (1993) 383-387
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 383-387
    • Glück, U.1    Kwiatkowski, D.J.2    Ben-Ze'ev, A.3
  • 31
    • 0141930005 scopus 로고    scopus 로고
    • Cct1, a phosphatidylcholine biosynthesis enzyme, is required for Drosophila oogenesis and ovarian morphogenesis
    • Gupta T., and Schüpbach T. Cct1, a phosphatidylcholine biosynthesis enzyme, is required for Drosophila oogenesis and ovarian morphogenesis. Development 130 (2003) 6075-6087
    • (2003) Development , vol.130 , pp. 6075-6087
    • Gupta, T.1    Schüpbach, T.2
  • 32
    • 0025611020 scopus 로고
    • The microfilament pattern in the somatic follicle cells of mid-vitellogenic ovarian follicles of Drosophila
    • Gutzeit H.O. The microfilament pattern in the somatic follicle cells of mid-vitellogenic ovarian follicles of Drosophila. Eur. J. Cell Biol. 53 (1990) 349-356
    • (1990) Eur. J. Cell Biol. , vol.53 , pp. 349-356
    • Gutzeit, H.O.1
  • 33
    • 0026281340 scopus 로고
    • Organization and in vitro activity of microfilament bundles associated with the basement membrane of Drosophila follicles
    • Gutzeit H.O. Organization and in vitro activity of microfilament bundles associated with the basement membrane of Drosophila follicles. Acta Histochem. Suppl. 41 (1992) 201-210
    • (1992) Acta Histochem. Suppl. , vol.41 , pp. 201-210
    • Gutzeit, H.O.1
  • 34
    • 0026323080 scopus 로고
    • Laminin and basement membrane-associated microfilaments in wild-type and mutant Drosophila ovarian follicles
    • Gutzeit H.O., Eberhardt W., and Gratwohl E. Laminin and basement membrane-associated microfilaments in wild-type and mutant Drosophila ovarian follicles. J. Cell Sci. 100 (1991) 781-788
    • (1991) J. Cell Sci. , vol.100 , pp. 781-788
    • Gutzeit, H.O.1    Eberhardt, W.2    Gratwohl, E.3
  • 35
    • 14644439208 scopus 로고    scopus 로고
    • Mass transit: epithelial morphogenesis in the Drosophila egg chamber
    • Horne-Badovinac S., and Bilder D. Mass transit: epithelial morphogenesis in the Drosophila egg chamber. Dev. Dyn. 232 (2005) 559-574
    • (2005) Dev. Dyn. , vol.232 , pp. 559-574
    • Horne-Badovinac, S.1    Bilder, D.2
  • 36
    • 0035800777 scopus 로고    scopus 로고
    • The cytoskeletal/non-muscle isoform of α-actinin is phosphorylated on its actin-binding domain by the focal adhesion kinase
    • Izaguirre G., Aguirre L., Hu Y.P., Lee H.Y., Schlaepfer D.D., Aneskievich B.J., and Haimovich B. The cytoskeletal/non-muscle isoform of α-actinin is phosphorylated on its actin-binding domain by the focal adhesion kinase. J. Biol. Chem. 276 (2001) 28676-28685
    • (2001) J. Biol. Chem. , vol.276 , pp. 28676-28685
    • Izaguirre, G.1    Aguirre, L.2    Hu, Y.P.3    Lee, H.Y.4    Schlaepfer, D.D.5    Aneskievich, B.J.6    Haimovich, B.7
  • 37
    • 0036340036 scopus 로고    scopus 로고
    • Mosaic analyses reveal the function of Drosophila Ras in embryonic dorsoventral patterning and dorsal follicle cell morphogenesis
    • James K.E., Dorman J.B., and Berg C.A. Mosaic analyses reveal the function of Drosophila Ras in embryonic dorsoventral patterning and dorsal follicle cell morphogenesis. Development 129 (2002) 2209-2222
    • (2002) Development , vol.129 , pp. 2209-2222
    • James, K.E.1    Dorman, J.B.2    Berg, C.A.3
  • 40
    • 0025131273 scopus 로고
    • Identification and localization of high molecular weight proteins in insect flight and leg muscle
    • Lakey A., Ferguson C., Labeit S., Reedy M., Larkins A., Butcher G., Leonard K., and Bullard B. Identification and localization of high molecular weight proteins in insect flight and leg muscle. EMBO J. 9 (1990) 3459-3467
    • (1990) EMBO J. , vol.9 , pp. 3459-3467
    • Lakey, A.1    Ferguson, C.2    Labeit, S.3    Reedy, M.4    Larkins, A.5    Butcher, G.6    Leonard, K.7    Bullard, B.8
  • 41
    • 0042829312 scopus 로고    scopus 로고
    • blistery encodes Drosophila tensin protein and interacts with integrin and the JNK signaling pathway during wing development
    • Lee S.B., Cho K.S., Kim E., and Chung J. blistery encodes Drosophila tensin protein and interacts with integrin and the JNK signaling pathway during wing development. Development 130 (2003) 4001-4010
    • (2003) Development , vol.130 , pp. 4001-4010
    • Lee, S.B.1    Cho, K.S.2    Kim, E.3    Chung, J.4
  • 42
    • 0024965992 scopus 로고
    • The function of PS integrins during Drosophila embryogenesis
    • Leptin M., Bogaert T., Lehmann R., and Wilcox M. The function of PS integrins during Drosophila embryogenesis. Cell 56 (1989) 401-408
    • (1989) Cell , vol.56 , pp. 401-408
    • Leptin, M.1    Bogaert, T.2    Lehmann, R.3    Wilcox, M.4
  • 43
    • 0027368350 scopus 로고
    • The Drosophila dorsoventral patterning gene gurken produces a dorsally localized RNA and encodes a TGFα-like protein
    • Neuman-Silberberg F.S., and Schüpbach T. The Drosophila dorsoventral patterning gene gurken produces a dorsally localized RNA and encodes a TGFα-like protein. Cell 75 (1993) 165-174
    • (1993) Cell , vol.75 , pp. 165-174
    • Neuman-Silberberg, F.S.1    Schüpbach, T.2
  • 44
    • 0025091575 scopus 로고
    • Relationship between the product of the Drosophila ultraspiracle locus and the vertebrate retinoid X receptor
    • Oro A.E., McKeown M., and Evans R.M. Relationship between the product of the Drosophila ultraspiracle locus and the vertebrate retinoid X receptor. Nature 347 (1990) 298-301
    • (1990) Nature , vol.347 , pp. 298-301
    • Oro, A.E.1    McKeown, M.2    Evans, R.M.3
  • 45
    • 2442481067 scopus 로고    scopus 로고
    • α-Actinin revisited: a fresh look at an old player
    • Otey C.A., and Carpen O. α-Actinin revisited: a fresh look at an old player. Cell Motil. Cytoskeleton 58 (2004) 104-111
    • (2004) Cell Motil. Cytoskeleton , vol.58 , pp. 104-111
    • Otey, C.A.1    Carpen, O.2
  • 47
    • 0025734407 scopus 로고
    • Disruption of the actin cytoskeleton after microinjection of proteolytic fragments of α-actinin
    • Pavalko F.M., and Burridge K. Disruption of the actin cytoskeleton after microinjection of proteolytic fragments of α-actinin. J. Cell Biol. 114 (1991) 481-491
    • (1991) J. Cell Biol. , vol.114 , pp. 481-491
    • Pavalko, F.M.1    Burridge, K.2
  • 48
    • 0034010706 scopus 로고    scopus 로고
    • Combined activities of Gurken and Decapentaplegic specify dorsal chorion structures of the Drosophila egg
    • Peri F., and Roth S. Combined activities of Gurken and Decapentaplegic specify dorsal chorion structures of the Drosophila egg. Development 127 (2000) 841-850
    • (2000) Development , vol.127 , pp. 841-850
    • Peri, F.1    Roth, S.2
  • 49
    • 0345434983 scopus 로고    scopus 로고
    • Local Gurken signaling and dynamic MAPK activation during Drosophila oogenesis
    • Peri F., Bökel C., and Roth S. Local Gurken signaling and dynamic MAPK activation during Drosophila oogenesis. Mech. Dev. 81 (1999) 75-85
    • (1999) Mech. Dev. , vol.81 , pp. 75-85
    • Peri, F.1    Bökel, C.2    Roth, S.3
  • 50
    • 0033993893 scopus 로고    scopus 로고
    • Severe developmental defects in Dictyostelium null mutants for actin-binding proteins
    • Ponte E., Rivero F., Fechheimer M., Noegel A., and Bozzaro S. Severe developmental defects in Dictyostelium null mutants for actin-binding proteins. Mech. Dev. 91 (2000) 153-161
    • (2000) Mech. Dev. , vol.91 , pp. 153-161
    • Ponte, E.1    Rivero, F.2    Fechheimer, M.3    Noegel, A.4    Bozzaro, S.5
  • 51
    • 0024544624 scopus 로고
    • The maternal ventralizing locus torpedo is allelic to faint little ball, an embryonic lethal, and encodes the Drosophila EGF receptor homolog
    • Price J.V., Clifford R.J., and Schüpbach T. The maternal ventralizing locus torpedo is allelic to faint little ball, an embryonic lethal, and encodes the Drosophila EGF receptor homolog. Cell 56 (1989) 1085-1092
    • (1989) Cell , vol.56 , pp. 1085-1092
    • Price, J.V.1    Clifford, R.J.2    Schüpbach, T.3
  • 52
    • 0030782345 scopus 로고    scopus 로고
    • Ectopic activation of torpedo/Egfr, a Drosophila receptor tyrosine kinase, dorsalizes both the eggshell and the embryo
    • Queenan A.M., Ghabrial A., and Schüpbach T. Ectopic activation of torpedo/Egfr, a Drosophila receptor tyrosine kinase, dorsalizes both the eggshell and the embryo. Development 124 (1997) 3871-3880
    • (1997) Development , vol.124 , pp. 3871-3880
    • Queenan, A.M.1    Ghabrial, A.2    Schüpbach, T.3
  • 53
    • 0036228954 scopus 로고    scopus 로고
    • Dissecting the link between stress fibres and focal adhesions by CALI with EGFP fusion proteins
    • Rajfur Z., Roy P., Otey C., Romer L., and Jacobson K. Dissecting the link between stress fibres and focal adhesions by CALI with EGFP fusion proteins. Nat. Cell Biol. 4 (2002) 286-293
    • (2002) Nat. Cell Biol. , vol.4 , pp. 286-293
    • Rajfur, Z.1    Roy, P.2    Otey, C.3    Romer, L.4    Jacobson, K.5
  • 54
    • 0029859177 scopus 로고    scopus 로고
    • The role of the cortical cytoskeleton: F-actin crosslinking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development
    • Rivero F., Köppel B., Peracino B., Bozzaro S., Siegert F., Weijer C.J., Schleicher M., Albrecht R., and Noegel A.A. The role of the cortical cytoskeleton: F-actin crosslinking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development. J. Cell Sci. 109 (1996) 2679-2691
    • (1996) J. Cell Sci. , vol.109 , pp. 2679-2691
    • Rivero, F.1    Köppel, B.2    Peracino, B.3    Bozzaro, S.4    Siegert, F.5    Weijer, C.J.6    Schleicher, M.7    Albrecht, R.8    Noegel, A.A.9
  • 55
    • 0026573230 scopus 로고
    • Perturbations of Drosophila α-actinin cause muscle paralysis, weakness, and atrophy but do not confer obvious nonmuscle phenotypes
    • Roulier E.M., Fyrberg C., and Fyrberg E. Perturbations of Drosophila α-actinin cause muscle paralysis, weakness, and atrophy but do not confer obvious nonmuscle phenotypes. J. Cell Biol. 116 (1992) 911-922
    • (1992) J. Cell Biol. , vol.116 , pp. 911-922
    • Roulier, E.M.1    Fyrberg, C.2    Fyrberg, E.3
  • 56
    • 0034029935 scopus 로고    scopus 로고
    • The RXR ortholog USP suppresses early metamorphic processes in Drosophila in the absence of ecdysteroids
    • Schubiger M., and Truman J.W. The RXR ortholog USP suppresses early metamorphic processes in Drosophila in the absence of ecdysteroids. Development 127 (2000) 1151-1159
    • (2000) Development , vol.127 , pp. 1151-1159
    • Schubiger, M.1    Truman, J.W.2
  • 57
    • 0030002451 scopus 로고    scopus 로고
    • Proteolytic cleavage of α-actinin by calpain in T cells stimulated with anti-CD3 monoclonal antibody
    • Selliah N., Brooks W.H., and Roszman T.L. Proteolytic cleavage of α-actinin by calpain in T cells stimulated with anti-CD3 monoclonal antibody. J. Immunol. 156 (1996) 3215-3221
    • (1996) J. Immunol. , vol.156 , pp. 3215-3221
    • Selliah, N.1    Brooks, W.H.2    Roszman, T.L.3
  • 59
    • 2442676448 scopus 로고    scopus 로고
    • Molecular evolution and structure of α-actinin
    • Virel A., and Backman L. Molecular evolution and structure of α-actinin. Mol. Biol. Evol. 21 (2004) 1024-1031
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 1024-1031
    • Virel, A.1    Backman, L.2
  • 60
    • 5344275878 scopus 로고    scopus 로고
    • Drosophila non-muscle α-actinin is localized in nurse cell actin bundles and ring canals, but is not required for fertility
    • Wahlström G., Lahti V.P., Pispa J., Roos C., and Heino T.I. Drosophila non-muscle α-actinin is localized in nurse cell actin bundles and ring canals, but is not required for fertility. Mech. Dev. 121 (2004) 1377-1391
    • (2004) Mech. Dev. , vol.121 , pp. 1377-1391
    • Wahlström, G.1    Lahti, V.P.2    Pispa, J.3    Roos, C.4    Heino, T.I.5
  • 62
    • 12344302324 scopus 로고    scopus 로고
    • Juxtaposition between two cell types is necessary for dorsal appendage tube formation
    • Ward E.J., and Berg C.A. Juxtaposition between two cell types is necessary for dorsal appendage tube formation. Mech. Dev. 122 (2005) 241-255
    • (2005) Mech. Dev. , vol.122 , pp. 241-255
    • Ward, E.J.1    Berg, C.A.2
  • 63
    • 0032582797 scopus 로고    scopus 로고
    • An autoregulatory cascade of EGF receptor signaling patterns the Drosophila egg
    • Wasserman J.D., and Freeman M. An autoregulatory cascade of EGF receptor signaling patterns the Drosophila egg. Cell 95 (1998) 355-364
    • (1998) Cell , vol.95 , pp. 355-364
    • Wasserman, J.D.1    Freeman, M.2
  • 64
    • 0032802338 scopus 로고    scopus 로고
    • Computer-assisted morphometry of cell-substratum contacts
    • Weber I. Computer-assisted morphometry of cell-substratum contacts. Croat. Med. J. 40 (1999) 334-339
    • (1999) Croat. Med. J. , vol.40 , pp. 334-339
    • Weber, I.1
  • 65
    • 0344465841 scopus 로고    scopus 로고
    • Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells
    • Zaidel-Bar R., Ballestrem C., Kam Z., and Geiger B. Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells. J. Cell Sci. 116 (2003) 4605-4613
    • (2003) J. Cell Sci. , vol.116 , pp. 4605-4613
    • Zaidel-Bar, R.1    Ballestrem, C.2    Kam, Z.3    Geiger, B.4
  • 66
    • 33644977113 scopus 로고    scopus 로고
    • Phosphorylated α-actinin and protein-tyrosine phosphatase 1B coregulate the disassembly of the focal adhesion kinase × Src complex and promote cell migration
    • Zhang Z., Lin S.Y., Neel B.G., and Haimovich B. Phosphorylated α-actinin and protein-tyrosine phosphatase 1B coregulate the disassembly of the focal adhesion kinase × Src complex and promote cell migration. J. Biol. Chem. 218 (2006) 1746-1754
    • (2006) J. Biol. Chem. , vol.218 , pp. 1746-1754
    • Zhang, Z.1    Lin, S.Y.2    Neel, B.G.3    Haimovich, B.4


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