메뉴 건너뛰기




Volumn 34, Issue 1, 1996, Pages 36-47

Plant profilins rescue the aberrant phenotype of profilin-deficient Dictyostelium cells

Author keywords

actin; actin binding protein; Dictyostelium; maize; mutant; profilin

Indexed keywords

PROFILIN;

EID: 0029883916     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0169(1996)34:1<36::AID-CM4>3.0.CO;2-G     Document Type: Article
Times cited : (54)

References (50)
  • 1
    • 0026905314 scopus 로고
    • The remarkable biology of pollen
    • Bedinger, P. (1992): The remarkable biology of pollen. Plant Cell 4:879-887.
    • (1992) Plant Cell , vol.4 , pp. 879-887
    • Bedinger, P.1
  • 2
    • 0027376752 scopus 로고
    • Mutagenesis of human profilin locates its poly(L-proline)-binding site to a Hydrophobic patch of aromatic amino acids
    • Björkegren, C., Rozycki, M., Schutt, C.E., Lindberg, U., and Karlsson, R. (1993): Mutagenesis of human profilin locates its poly(L-proline)-binding site to a Hydrophobic patch of aromatic amino acids. FEBS Lett. 333:123-126.
    • (1993) FEBS Lett. , vol.333 , pp. 123-126
    • Björkegren, C.1    Rozycki, M.2    Schutt, C.E.3    Lindberg, U.4    Karlsson, R.5
  • 4
    • 0001340764 scopus 로고
    • Electron microscopic mapping of monoclonal antibodies on the tail region of Dictyostelium myosin
    • Claviez, M., Pagh, K., Maruta, H., Baltes, W., Fisher, P., and Gerisch, G. (1982): Electron microscopic mapping of monoclonal antibodies on the tail region of Dictyostelium myosin. EMBO J. 1:1017-1022.
    • (1982) EMBO J , vol.1 , pp. 1017-1022
    • Claviez, M.1    Pagh, K.2    Maruta, H.3    Baltes, W.4    Fisher, P.5    Gerisch, G.6
  • 5
    • 0026041203 scopus 로고
    • Coronin, actin-binding protein of Dictyostelium discoideum localized to cell surface projections, has sequence similarities to G-protein β subunits
    • de Hostos, E.L., Bradtke, B., Lottspeich, F., Guggenheim, R., and Gerisch, G. (1991): Coronin, actin-binding protein of Dictyostelium discoideum localized to cell surface projections, has sequence similarities to G-protein β subunits. EMBO J. 10: 4097-4104.
    • (1991) EMBO J. , vol.10 , pp. 4097-4104
    • De Hostos, E.L.1    Bradtke, B.2    Lottspeich, F.3    Guggenheim, R.4    Gerisch, G.5
  • 6
    • 0027389812 scopus 로고
    • Dictyostelium mutants lacking the cytoskeletal protein coronin are defective in cytokinesis and cell motility
    • de Hostos, E.L., Rehfueß, C., Bradtke, B., Waddell, D.R., Albrecht, R., Murphy, J., and Gerisch, G. (1993): Dictyostelium mutants lacking the cytoskeletal protein coronin are defective in cytokinesis and cell motility. J. Cell Biol. 120:163-173.
    • (1993) J. Cell Biol. , vol.120 , pp. 163-173
    • De Hostos, E.L.1    Rehfueß, C.2    Bradtke, B.3    Waddell, D.R.4    Albrecht, R.5    Murphy, J.6    Gerisch, G.7
  • 7
    • 0028105664 scopus 로고
    • Inhibition of plant plasma membrane phosphoinositide phospholipase C by the actin-binding protein, profilin
    • Drøbak, B.K., Watkins, P.A.C., Valenta, R., Dove, S.K., Lloyd, C.W., and Staiger, C.J. (1994): Inhibition of plant plasma membrane phosphoinositide phospholipase C by the actin-binding protein, profilin. Plant J. 6:389-400.
    • (1994) Plant J. , vol.6 , pp. 389-400
    • Drøbak, B.K.1    Watkins, P.A.C.2    Valenta, R.3    Dove, S.K.4    Lloyd, C.W.5    Staiger, C.J.6
  • 8
    • 0024671747 scopus 로고
    • Hygromycin resistance as a selectable marker in Dictyostelium discoideum
    • Egelhoff, T.T., Brown, S.S., Manstein, D.J., and Spudich, J.A. (1989): Hygromycin resistance as a selectable marker in Dictyostelium discoideum. Mol. Cell Biol. 9:1965-1968.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 1965-1968
    • Egelhoff, T.T.1    Brown, S.S.2    Manstein, D.J.3    Spudich, J.A.4
  • 9
    • 0026650509 scopus 로고
    • Overexpression of the csA cell adhesion molecule under its own cAMP-regulated promoter impairs morphogenesis in Dictyostelium
    • Faix, J., Gerisch, G., and Noegel, A.A. (1992): Overexpression of the csA cell adhesion molecule under its own cAMP-regulated promoter impairs morphogenesis in Dictyostelium. J. Cell Sci. 102:203-214.
    • (1992) J. Cell Sci. , vol.102 , pp. 203-214
    • Faix, J.1    Gerisch, G.2    Noegel, A.A.3
  • 10
    • 0027965072 scopus 로고
    • X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates
    • Fedorov, A.A., Magnus, K.A., Graupe, M.H., Lattman, E.E., Pollard, T D., and Almo, S.C. (1994): X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates. Proc. Natl. Acad. Sci. U.S.A. 91:8636-8640.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 8636-8640
    • Fedorov, A.A.1    Magnus, K.A.2    Graupe, M.H.3    Lattman, E.E.4    Pollard, T.D.5    Almo, S.C.6
  • 12
    • 0025308055 scopus 로고
    • The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C
    • Goldschmidt-Clermont, P.J., Machesky, L.M., Baldassare, J.J., and Pollard, T.D. (1990): The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C. Science 247:1575-1578.
    • (1990) Science , vol.247 , pp. 1575-1578
    • Goldschmidt-Clermont, P.J.1    Machesky, L.M.2    Baldassare, J.J.3    Pollard, T.D.4
  • 13
  • 14
    • 0027104517 scopus 로고
    • The control of actin nucleotide exchange by thymosin β4 and profilin. A potential regulatory mechanism for actin polymerization in cells
    • Goldschmidt-Clermont, P.J., Furman, M.I., Wachsstock, D., Safer, D., Nachmias, V.T., and Pollard, T.D. (1992): The control of actin nucleotide exchange by thymosin β4 and profilin. A potential regulatory mechanism for actin polymerization in cells. Mol. Biol. Cell 3:1015-1024.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1015-1024
    • Goldschmidt-Clermont, P.J.1    Furman, M.I.2    Wachsstock, D.3    Safer, D.4    Nachmias, V.T.5    Pollard, T.D.6
  • 16
    • 0025950142 scopus 로고
    • Dictyosielium discoideum contains two profilin isoforms that differ in structure and function
    • Haugwitz, M., Noegel, A.A., Rieger, D., Lotspeich, F., and Schleicher, M. (1991): Dictyosielium discoideum contains two profilin isoforms that differ in structure and function. J. Cell Sci. 100:481-489.
    • (1991) J. Cell Sci. , vol.100 , pp. 481-489
    • Haugwitz, M.1    Noegel, A.A.2    Rieger, D.3    Lotspeich, F.4    Schleicher, M.5
  • 17
    • 0028004565 scopus 로고
    • Dictyosielium amoeba that lack G-actin-sequestering profilins show defects in F-actin content, cytokinesis, and development
    • Haugwitz, M., Noegel, A.A., Karakesisoglou, J., and Schleicher, M. (1994): Dictyosielium amoeba that lack G-actin-sequestering profilins show defects in F-actin content, cytokinesis, and development. Cell 79:303-314.
    • (1994) Cell , vol.79 , pp. 303-314
    • Haugwitz, M.1    Noegel, A.A.2    Karakesisoglou, J.3    Schleicher, M.4
  • 19
    • 0025878284 scopus 로고
    • Polyproline affinity method for purification of platelet profilin and modification with pyrene-maleimide
    • Janmey, P.A. (1991): Polyproline affinity method for purification of platelet profilin and modification with pyrene-maleimide. Methods Enzymol. 196:92-99.
    • (1991) Methods Enzymol. , vol.196 , pp. 92-99
    • Janmey, P.A.1
  • 20
    • 0022621479 scopus 로고
    • Purification and characterization of two isoforms of Acanthamoeba profilin
    • Kaiser, D.A., Sato, M., Ebert, R.F., and Pollard, T.D. (1986): Purification and characterization of two isoforms of Acanthamoeba profilin. J. Cell Biol. 102:221-226.
    • (1986) J. Cell Biol. , vol.102 , pp. 221-226
    • Kaiser, D.A.1    Sato, M.2    Ebert, R.F.3    Pollard, T.D.4
  • 21
    • 0022815791 scopus 로고
    • Developmental regulation of Dictyostelium discoideum actin gene fusions carried on low-copy and high-copy transformation vectors
    • Knecht, D.A., Cohen, S.M., Loomis, W.F., and Lodish, H.F. (1986): Developmental regulation of Dictyostelium discoideum actin gene fusions carried on low-copy and high-copy transformation vectors. Mol. Cell Biol. 6:3973-3983.
    • (1986) Mol. Cell Biol. , vol.6 , pp. 3973-3983
    • Knecht, D.A.1    Cohen, S.M.2    Loomis, W.F.3    Lodish, H.F.4
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970): Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0023854786 scopus 로고
    • Evidence that the phosphatidylinositol cycle is linked to cell motility
    • Lassing, I., and Lindberg, U. (1988): Evidence that the phosphatidylinositol cycle is linked to cell motility. Exp. Cell Res. 174: 1-15.
    • (1988) Exp. Cell Res. , vol.174 , pp. 1-15
    • Lassing, I.1    Lindberg, U.2
  • 24
    • 0027358716 scopus 로고
    • Profilin as a potential mediator of membrane-cytoskeleton communication
    • Machesky, L.M., and Pollard, T.D. (1993): Profilin as a potential mediator of membrane-cytoskeleton communication. Trends Cell Biol. 3:381-385.
    • (1993) Trends Cell Biol. , vol.3 , pp. 381-385
    • Machesky, L.M.1    Pollard, T.D.2
  • 25
    • 0021715560 scopus 로고
    • The pIC plasmid and phage vectors with versatile cloning sites for recombinant selection by insertional inactivation
    • Marsh, J.L., Erfle, M., and Wykes, E.J. (1987): The pIC plasmid and phage vectors with versatile cloning sites for recombinant selection by insertional inactivation. Gene 32:481-485.
    • (1987) Gene , vol.32 , pp. 481-485
    • Marsh, J.L.1    Erfle, M.2    Wykes, E.J.3
  • 26
    • 0027138345 scopus 로고
    • Molecular mechanisms of pollen tube growth and differentiation
    • Mascarenhas, J.P. (1993): Molecular mechanisms of pollen tube growth and differentiation. Plant Cell 5:1303-1314.
    • (1993) Plant Cell , vol.5 , pp. 1303-1314
    • Mascarenhas, J.P.1
  • 27
    • 0027731196 scopus 로고
    • Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern
    • Metzler, W.J., Constantine, K.L., Friedrichs, M.S., Bell, A.J., Ernst, E.G., Lavoie, T.B., and Mueller, L. (1993): Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern. Biochemistry 32:13818-13829.
    • (1993) Biochemistry , vol.32 , pp. 13818-13829
    • Metzler, W.J.1    Constantine, K.L.2    Friedrichs, M.S.3    Bell, A.J.4    Ernst, E.G.5    Lavoie, T.B.6    Mueller, L.7
  • 28
    • 0028108647 scopus 로고
    • Identification of the poly-L-proline-binding site on human profilin
    • Metzler, W.J., Bell, A.J., Ernst, E., Lavoie, T.B., and Mueller, L. (1994): Identification of the poly-L-proline-binding site on human profilin. J. Biol. Chem. 269:4620-4625.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4620-4625
    • Metzler, W.J.1    Bell, A.J.2    Ernst, E.3    Lavoie, T.B.4    Mueller, L.5
  • 29
    • 0019194944 scopus 로고
    • Acantamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate
    • Mocknn, S., and Korn, E.D. (1980): Acantamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate. Biochemistry 19:5359-5362.
    • (1980) Biochemistry , vol.19 , pp. 5359-5362
    • Mocknn, S.1    Korn, E.D.2
  • 30
    • 0027772556 scopus 로고
    • How profiain promotes actin filament assembly in the presence of thymosin β4
    • Pantaloni, D., and Cartier, M.F. (1993): How profiain promotes actin filament assembly in the presence of thymosin β4. Cell 75: 1007-1014.
    • (1993) Cell , vol.75 , pp. 1007-1014
    • Pantaloni, D.1    Cartier, M.F.2
  • 31
    • 0001853866 scopus 로고
    • In situ localization of F-actin in pollen tubes
    • Perdue, T.D., and Parthasarathy. M.V. (1985): In situ localization of F-actin in pollen tubes. Eur. J. Cell Biol. 39:13-20.
    • (1985) Eur. J. Cell Biol. , vol.39 , pp. 13-20
    • Perdue, T.D.1    Parthasarathy, M.V.2
  • 32
    • 0001856603 scopus 로고
    • Organization of microfilaments and microtubules in pollen tubes grown in vitro or in vivo in various angiosperms
    • Pierson, E.S., Derksen, J., and Traas, J.A. (1986): Organization of microfilaments and microtubules in pollen tubes grown in vitro or in vivo in various angiosperms. Eur. J. Cell Biol. 41:14-18.
    • (1986) Eur. J. Cell Biol. , vol.41 , pp. 14-18
    • Pierson, E.S.1    Derksen, J.2    Traas, J.A.3
  • 33
    • 0021200245 scopus 로고
    • Polymerization of ADP-actin
    • Pollard, T.D. (1984): Polymerization of ADP-actin. J. Cell Biol. 99: 769-77.
    • (1984) J. Cell Biol. , vol.99 , pp. 769-777
    • Pollard, T.D.1
  • 34
    • 0021766640 scopus 로고
    • Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation
    • Pollard, T.D., and Cooper, J.A. (1984): Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation. Biochemistry 23:6631-6641.
    • (1984) Biochemistry , vol.23 , pp. 6631-6641
    • Pollard, T.D.1    Cooper, J.A.2
  • 35
    • 0028466669 scopus 로고
    • Profilins purified from higher plants bind to actin from cardiac muscle and to actin from a green alga
    • Ruhlandt, G., Lange, U., and Grolig, F. (1994): Profilins purified from higher plants bind to actin from cardiac muscle and to actin from a green alga. Plant Cell Physiol. 35:849-854.
    • (1994) Plant Cell Physiol. , vol.35 , pp. 849-854
    • Ruhlandt, G.1    Lange, U.2    Grolig, F.3
  • 38
    • 0028464361 scopus 로고
    • Profilin: At the crossroads of signal transduction and the actin cytoskeleton
    • Sohn, R.H., and Goldschmidt-Clermont, PJ. (1994): Profilin: At the crossroads of signal transduction and the actin cytoskeleton. BioEssays 16:465-472.
    • (1994) BioEssays , vol.16 , pp. 465-472
    • Sohn, R.H.1    Goldschmidt-Clermont, P.J.2
  • 39
    • 0029097309 scopus 로고
    • Localization of a binding site for phosphatidyhnositol 4,5-bisphosphate on human profilin
    • Sohn, R.H., Chen, J., Koblan, K.S., Bray, P.F., and Goldschmidt-Clermont, P.J. (1995): Localization of a binding site for phosphatidyhnositol 4,5-bisphosphate on human profilin. J. Biol. Chem. 270:21114-21120.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21114-21120
    • Sohn, R.H.1    Chen, J.2    Koblan, K.S.3    Bray, P.F.4    Goldschmidt-Clermont, P.J.5
  • 40
  • 41
    • 0028385716 scopus 로고
    • Microinjected profilin affects cytoplasmic streaming in plant cells by rapidly depolymerizing actin microfilaments
    • Staiger, C.J., Yuan, M., Valenta, R., Shaw, P.J., Warn, R., and Lloyd, C.W. (1994): Microinjected profilin affects cytoplasmic streaming in plant cells by rapidly depolymerizing actin microfilaments. Curr. Biol. 4:215-219.
    • (1994) Curr. Biol. , vol.4 , pp. 215-219
    • Staiger, C.J.1    Yuan, M.2    Valenta, R.3    Shaw, P.J.4    Warn, R.5    Lloyd, C.W.6
  • 42
    • 0023073916 scopus 로고
    • Cultivation and synchronous morphogenesis of Dictyostelium under controlled experimental conditions
    • Sussman, M. (1987): Cultivation and synchronous morphogenesis of Dictyostelium under controlled experimental conditions. Methods Cell Biol. 28:9-29.
    • (1987) Methods Cell Biol. , vol.28 , pp. 9-29
    • Sussman, M.1
  • 43
    • 0002936782 scopus 로고
    • Spatial and temporal organization of actin during hydration, activation, and germination of pollen in Pyrus communis L.: A population study
    • Tiwari, S.C., and Polito, V.S. (1988): Spatial and temporal organization of actin during hydration, activation, and germination of pollen in Pyrus communis L.: A population study. Protoplasma 147:5-15.
    • (1988) Protoplasma , vol.147 , pp. 5-15
    • Tiwari, S.C.1    Polito, V.S.2
  • 44
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1979): Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 47
    • 0024320518 scopus 로고
    • Structural principles of actin-binding proteins
    • Vandekerckhove, J. (1989): Structural principles of actin-binding proteins. Curr. Opin. Cell Biol. 1:15-22.
    • (1989) Curr. Opin. Cell Biol. , vol.1 , pp. 15-22
    • Vandekerckhove, J.1
  • 49
    • 0017282039 scopus 로고
    • A genetic study in the cellular slime mould Dictyostelium discoideum using complementation analysis
    • Williams, K.L., and Newell, P.C. (1976): A genetic study in the cellular slime mould Dictyostelium discoideum using complementation analysis. Genetics 82:287-307.
    • (1976) Genetics , vol.82 , pp. 287-307
    • Williams, K.L.1    Newell, P.C.2
  • 50
    • 0023661339 scopus 로고
    • Homologous recombination in the Dictyostelium α-actinin gene leads to an altered mRNA and lack of the protein
    • Witke, W., Nellen, W., and Noegel, A.A. (1987): Homologous recombination in the Dictyostelium α-actinin gene leads to an altered mRNA and lack of the protein. EMBO J. 6:4143-4148.
    • (1987) EMBO J. , vol.6 , pp. 4143-4148
    • Witke, W.1    Nellen, W.2    Noegel, A.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.