메뉴 건너뛰기




Volumn 8, Issue 2, 1996, Pages 333-342

Tomato annexins p34 and p35 bind to F-actin and display nucleotide phosphodiesterase activity inhibited by phospholipid binding

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA; LYCOPERSICON ESCULENTUM; ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0030087919     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.8.2.333     Document Type: Article
Times cited : (84)

References (41)
  • 1
    • 0343879238 scopus 로고
    • Assay of inorganic phosphate, total phosphate and phosphatases
    • Ames, B.N. (1966). Assay of inorganic phosphate, total phosphate and phosphatases. Methods Enzymol. 8, 115-118.
    • (1966) Methods Enzymol. , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 2
    • 0027613542 scopus 로고
    • Cotton fiber annexins: A potential role in the regulation of callose synthase
    • Andrawis, A., Solomon, M., and Delmer, D.P. (1993). Cotton fiber annexins: A potential role in the regulation of callose synthase. Plant J. 3, 763-772.
    • (1993) Plant J. , vol.3 , pp. 763-772
    • Andrawis, A.1    Solomon, M.2    Delmer, D.P.3
  • 3
    • 84989741593 scopus 로고
    • Annexin-mediated secretory vesicle aggregation in plants
    • Blackbourn, H.D., and Battey, N.H. (1993). Annexin-mediated secretory vesicle aggregation in plants. Physiol. Plant. 89, 27-32.
    • (1993) Physiol. Plant. , vol.89 , pp. 27-32
    • Blackbourn, H.D.1    Battey, N.H.2
  • 5
    • 0001365730 scopus 로고
    • Identification of calcium-dependent phospholipid-binding proteins in higher plant cells
    • Boustead, C.M., Smallwood, M., Small, H., Bowles, D.J., and Walker, J.H. (1989). Identification of calcium-dependent phospholipid-binding proteins in higher plant cells. FEBS Lett. 244, 456-460.
    • (1989) FEBS Lett. , vol.244 , pp. 456-460
    • Boustead, C.M.1    Smallwood, M.2    Small, H.3    Bowles, D.J.4    Walker, J.H.5
  • 6
    • 0025310355 scopus 로고
    • Defense-related proteins in higher plants
    • Bowles, D.J. (1990). Defense-related proteins in higher plants. Annu. Rev. Biochem. 59, 873-907.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 873-907
    • Bowles, D.J.1
  • 7
    • 0027106118 scopus 로고
    • Purification and immunolocalization of an annexin-like protein in pea seedlings
    • Clark, G.B., Dauwalder, M., and Roux, S.J. (1992) Purification and immunolocalization of an annexin-like protein in pea seedlings. Planta 187, 1-9.
    • (1992) Planta , vol.187 , pp. 1-9
    • Clark, G.B.1    Dauwalder, M.2    Roux, S.J.3
  • 9
    • 0027520803 scopus 로고
    • The computed free energy change of hydrolysis of inorganic pyrophosphate and ATP: Apparent significance for inorganic-pyrophosphatase-driven reactions of intermediate metabolism
    • Davies, J.M., Poole, R.J., and Sanders, D. (1993). The computed free energy change of hydrolysis of inorganic pyrophosphate and ATP: Apparent significance for inorganic-pyrophosphatase-driven reactions of intermediate metabolism. Biochim. Biophys. Acta 1141, 29-36.
    • (1993) Biochim. Biophys. Acta , vol.1141 , pp. 29-36
    • Davies, J.M.1    Poole, R.J.2    Sanders, D.3
  • 10
    • 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
  • 11
    • 0025078951 scopus 로고
    • Roles of the amino acid side-chains in the actin-binding s-site of myosin heavy chain
    • Eto, M., Suzuki, R., Morita, F., Kuwayama, H., Nishi, N., and Tokura, S. (1990). Roles of the amino acid side-chains in the actin-binding s-site of myosin heavy chain. J. Biochem. 108, 499-504.
    • (1990) J. Biochem. , vol.108 , pp. 499-504
    • Eto, M.1    Suzuki, R.2    Morita, F.3    Kuwayama, H.4    Nishi, N.5    Tokura, S.6
  • 12
    • 0019739585 scopus 로고
    • Preparation of monoclonal antibodies: Strategies and procedures
    • Galfrè, G., and Milstein, C. (1981). Preparation of monoclonal antibodies: Strategies and procedures. Methods Enzymol. 73, 3-46.
    • (1981) Methods Enzymol. , vol.73 , pp. 3-46
    • Galfrè, G.1    Milstein, C.2
  • 13
    • 0021299594 scopus 로고
    • Identity ot p36k phosphorylated upon Rous-sarcoma virus transformation with a protein purified from brushborders - Calcium-dependent binding to non-erythroid spectrin and F-actin
    • Gerke, V., and Weber, K. (1984). Identity ot p36k phosphorylated upon Rous-sarcoma virus transformation with a protein purified from brushborders - Calcium-dependent binding to non-erythroid spectrin and F-actin. EMBO J. 3, 227-233.
    • (1984) EMBO J. , vol.3 , pp. 227-233
    • Gerke, V.1    Weber, K.2
  • 14
    • 0021943945 scopus 로고
    • Calcium-dependent conformational-changes in the 36-kD subunit of intestinal protein-I related to the cellular 36-kD target of Rous-sarcoma virus tyrosine kinase
    • Gerke, V., and Weber, K. (1985). Calcium-dependent conformational-changes in the 36-kD subunit of intestinal protein-I related to the cellular 36-kD target of Rous-sarcoma virus tyrosine kinase. J. Biol. Chem. 260, 1688-1695.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1688-1695
    • Gerke, V.1    Weber, K.2
  • 16
    • 0021956617 scopus 로고
    • 2+-regulated events in the intestinal brush-border
    • 2+-regulated events in the intestinal brush-border. J. Cell Biol. 100, 754-763.
    • (1985) J. Cell Biol. , vol.100 , pp. 754-763
    • Glenney, J.R.1    Glenney, P.2
  • 17
    • 0023139338 scopus 로고
    • 2+-regulated phospholipid- And actin-binding proteins isolated from lung and placenta
    • 2+-regulated phospholipid- and actin-binding proteins isolated from lung and placenta. J. Cell Biol. 104, 503-511.
    • (1987) J. Cell Biol. , vol.104 , pp. 503-511
    • Glenney, J.R.1    Tack, B.2    Powell, M.A.3
  • 19
    • 0025000276 scopus 로고
    • The calcium binding sites in human annexin V by crystal structure analysis at 2.0 Å resolution
    • Huber, R., Romisch, J., and Paques, E.P. (1990). The calcium binding sites in human annexin V by crystal structure analysis at 2.0 Å resolution. EMBO J. 9, 3867-3874.
    • (1990) EMBO J. , vol.9 , pp. 3867-3874
    • Huber, R.1    Romisch, J.2    Paques, E.P.3
  • 20
    • 0025215463 scopus 로고
    • Calcium-dependent regulation of actin filament bundling by lipocortin-85
    • Ikebuchi, N.W., and Waisman, D.M. (1990). Calcium-dependent regulation of actin filament bundling by lipocortin-85. J. Biol. Chem. 265, 3392-3400.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3392-3400
    • Ikebuchi, N.W.1    Waisman, D.M.2
  • 21
    • 0026623535 scopus 로고
    • A nonapeptide to the putative F-actin binding site of annexin-II tetramer inhibits its calcium-dependent activation of actin filament bundling
    • Jones, P.G., Moore, G.J., and Waisman, D.M. (1992). A nonapeptide to the putative F-actin binding site of annexin-II tetramer inhibits its calcium-dependent activation of actin filament bundling. J. Biol. Chem. 267, 13993-13997.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13993-13997
    • Jones, P.G.1    Moore, G.J.2    Waisman, D.M.3
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0027416724 scopus 로고
    • Further characterization of the alpha-actinin-actin interface and comparison with filamin-binding sites on actin
    • Lebart, M.C., Mejean, C., Roustan, C., and Benyamin, Y. (1993). Further characterization of the alpha-actinin-actin interface and comparison with filamin-binding sites on actin. J. Biol. Chem. 268, 5642-5648.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5642-5648
    • Lebart, M.C.1    Mejean, C.2    Roustan, C.3    Benyamin, Y.4
  • 25
    • 0026514824 scopus 로고
    • Microdomains of high calcium-concentration in a presynaptic terminal
    • Llinas, R., Sugimori, M., and Silver, R.B. (1992). Microdomains of high calcium-concentration in a presynaptic terminal. Science 256, 677-678.
    • (1992) Science , vol.256 , pp. 677-678
    • Llinas, R.1    Sugimori, M.2    Silver, R.B.3
  • 26
    • 0028221436 scopus 로고
    • In vitro modulation of filament bundling in F-actin and keratins by annexin II and calcium
    • Ma, A.S.P., Bystol, M.E., and Tranvan, A. (1994) In vitro modulation of filament bundling in F-actin and keratins by annexin II and calcium. In Vitro Cell. Dev. Biol. 30A, 329-335.
    • (1994) In Vitro Cell. Dev. Biol. , vol.30 A , pp. 329-335
    • Ma, A.S.P.1    Bystol, M.E.2    Tranvan, A.3
  • 27
    • 0000169232 scopus 로고
    • An algorithm for least squares estimation of non-linear parameters
    • Marquardt, D.W. (1963) An algorithm for least squares estimation of non-linear parameters. J. Soc. Ind. Appl. Math. 11, 431-441.
    • (1963) J. Soc. Ind. Appl. Math. , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 28
    • 0028127073 scopus 로고
    • Identification and characterization of ATPase activity associated with maize (Zea mays) annexins
    • McClung, A.D., Carroll, A.D., and Battey, N.H. (1994) Identification and characterization of ATPase activity associated with maize (Zea mays) annexins. Biochem. J. 303, 709-712.
    • (1994) Biochem. J. , vol.303 , pp. 709-712
    • McClung, A.D.1    Carroll, A.D.2    Battey, N.H.3
  • 29
    • 0001906480 scopus 로고
    • The annexins
    • S.E. Moss, ed (London: Portland Press)
    • Moss, S.E. (1992). The annexins. In The Annexins, S.E. Moss, ed (London: Portland Press), pp. 1-9.
    • (1992) The Annexins , pp. 1-9
    • Moss, S.E.1
  • 30
    • 0025044601 scopus 로고
    • A fluorescence spectroscopy study of the calpactin-I complex and its subunit-p11 and subunit-p36-calcium-dependent conformation changes
    • Pigault, C, Follénius-Wund, A., Lux, B., and Gérard, D. (1990). A fluorescence spectroscopy study of the calpactin-I complex and its subunit-p11 and subunit-p36-calcium-dependent conformation changes. Biochim. Biophys. Acta 1037, 106-114.
    • (1990) Biochim. Biophys. Acta , vol.1037 , pp. 106-114
    • Pigault, C.1    Follénius-Wund, A.2    Lux, B.3    Gérard, D.4
  • 31
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium-and phospholipid-binding proteins
    • Raynal, P., and Pollard, H.B. (1994). Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium-and phospholipid-binding proteins. Biochim. Biophys. Acta 1197, 63-93.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 32
    • 0023654670 scopus 로고
    • 2+-dependent phospholipid binding and phosphorylation of lipocortin I
    • 2+-dependent phospholipid binding and phosphorylation of lipocortin I. J Biol. Chem. 262, 6931-6937.
    • (1987) J Biol. Chem. , vol.262 , pp. 6931-6937
    • Schlaepfer, D.D.1    Haigler, H.T.2
  • 33
    • 0028676125 scopus 로고
    • A 42-kilodalton annexin-like protein is associated with plant vacuoles
    • Seals, D.F., Parrish, M.L., and Randall, S.K. (1994) A 42-kilodalton annexin-like protein is associated with plant vacuoles. Plant Physiol. 106, 1403-1412.
    • (1994) Plant Physiol. , vol.106 , pp. 1403-1412
    • Seals, D.F.1    Parrish, M.L.2    Randall, S.K.3
  • 36
    • 6944256578 scopus 로고
    • The pattern of plant gene expression
    • Smallwood, M.F., Keen, J.N., and Bowles, D.J. (1992) The pattern of plant gene expression. Biochem. J. 270, 157-161.
    • (1992) Biochem. J. , vol.270 , pp. 157-161
    • Smallwood, M.F.1    Keen, J.N.2    Bowles, D.J.3
  • 37
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction
    • Spudich, J.A., and Watt, S. (1971). The regulation of rabbit skeletal muscle contraction. J. Biol. Chem. 246, 4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 38
    • 0023664779 scopus 로고
    • F-actin-binding synthetic heptapeptide having the amino-acid sequence around the SH1 cysteinyl residue of myosin
    • Suzuki, R., Nishi, N., Tokura, S., and Morita, F. (1987). F-actin-binding synthetic heptapeptide having the amino-acid sequence around the SH1 cysteinyl residue of myosin. J. Biol. Chem. 262, 11410-11412.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11410-11412
    • Suzuki, R.1    Nishi, N.2    Tokura, S.3    Morita, F.4
  • 39
    • 0000698690 scopus 로고
    • Association of phosphatidylinositol kinase, phosphatidylinositol monophosphate kinase, and diacylglycerol kinase with the cytoskeleton and F-actin fractions of carrot (Daucus carota L.) cells grown in suspension culture
    • Tan, Z., and Boss, W.F. (1992). Association of phosphatidylinositol kinase, phosphatidylinositol monophosphate kinase, and diacylglycerol kinase with the cytoskeleton and F-actin fractions of carrot (Daucus carota L.) cells grown in suspension culture. Plant Physiol. 100, 2116-2120.
    • (1992) Plant Physiol. , vol.100 , pp. 2116-2120
    • Tan, Z.1    Boss, W.F.2
  • 40
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications
    • Towbin, H., Staehlin, T, and Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehlin, T.2    Gordon, J.3
  • 41
    • 0000514378 scopus 로고
    • Association of phosphatidylinositol 4-kinase with the plant cytoskeleton
    • Xu, P., Lloyd, C.W., Staiger, C.J., and Drøbak, B.K. (1992) Association of phosphatidylinositol 4-kinase with the plant cytoskeleton. Plant Cell 4, 941-951.
    • (1992) Plant Cell , vol.4 , pp. 941-951
    • Xu, P.1    Lloyd, C.W.2    Staiger, C.J.3    Drøbak, B.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.