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Volumn 47, Issue 4, 2006, Pages 491-500

Profilin tyrosine phosphorylation in poly-L-proline-binding regions inhibits binding to phosphoinositide 3-kinase in Phaseolus vulgaris

Author keywords

Plant PI3k; PLP binding sites; Profilin; Tyrosine phosphorylation

Indexed keywords

PLANT PI3K; PLP-BINDING SITES; PROFILIN; TYROSINE PHOSPHORYLATION;

EID: 33746536554     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2006.02787.x     Document Type: Article
Times cited : (24)

References (38)
  • 1
    • 0031739045 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase binds to profilin through the p85 alpha subunit and regulates cytoskeletal assembly
    • Bhargavi, V., Chari, V.B. and Singh, S.S. (1998) Phosphatidylinositol 3-kinase binds to profilin through the p85 alpha subunit and regulates cytoskeletal assembly. Biochem. Mol. Biol. Int. 46, 241-248.
    • (1998) Biochem. Mol. Biol. Int. , vol.46 , pp. 241-248
    • Bhargavi, V.1    Chari, V.B.2    Singh, S.S.3
  • 2
    • 0029148577 scopus 로고
    • Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells
    • Brown, W.J., DeWald, D.B., Emr, S.D., Plutner, H. and Balch, W.E. (1995) Role for phosphatidylinositol 3-kinase in the sorting and transport of newly synthesized lysosomal enzymes in mammalian cells. J. Cell Biol. 130, 781-796.
    • (1995) J. Cell Biol. , vol.130 , pp. 781-796
    • Brown, W.J.1    DeWald, D.B.2    Emr, S.D.3    Plutner, H.4    Balch, W.E.5
  • 4
    • 0037107491 scopus 로고    scopus 로고
    • Retromer function in endosome-to-Golgi retrograde transport is regulated by the yeast Vps34 PtdIns 3-kinase
    • Burda, P., Padilla, S.M., Sarkar, S. and Emr, S.D. (2002) Retromer function in endosome-to-Golgi retrograde transport is regulated by the yeast Vps34 PtdIns 3-kinase. J. Cell Sci. 115, 3889-3900.
    • (2002) J. Cell Sci. , vol.115 , pp. 3889-3900
    • Burda, P.1    Padilla, S.M.2    Sarkar, S.3    Emr, S.D.4
  • 5
    • 0035182260 scopus 로고    scopus 로고
    • Actin monoubiquitylation is induced in plants in response to pathogens and symbionts
    • Dantan-Gonzalez, E., Rosenstein, Y., Quinto, C. and Sanchez, F. (2001) Actin monoubiquitylation is induced in plants in response to pathogens and symbionts. Mol. Plant Microbe Interact. 14, 1267-1273.
    • (2001) Mol. Plant Microbe Interact. , vol.14 , pp. 1267-1273
    • Dantan-Gonzalez, E.1    Rosenstein, Y.2    Quinto, C.3    Sanchez, F.4
  • 6
    • 0028090666 scopus 로고
    • Identification of a phosphatidylinositol 3-hydroxy kinase in plant cells: Association with the cytoskeleton
    • Dove, S.K., Lloyd, C.W. and Drobak, B.K. (1994) Identification of a phosphatidylinositol 3-hydroxy kinase in plant cells: association with the cytoskeleton. Biochem. J. 303 (Pt 2), 347-350.
    • (1994) Biochem. J. , vol.303 , Issue.2 PART , pp. 347-350
    • Dove, S.K.1    Lloyd, C.W.2    Drobak, B.K.3
  • 7
    • 3042664547 scopus 로고    scopus 로고
    • The role of the actin cytoskeleton in plant cell signaling
    • Drøbak, B.K., Franklin-Tong, V.E. and Staiger, C.J. (2004) The role of the actin cytoskeleton in plant cell signaling. New Phytol. 163, 13-30.
    • (2004) New Phytol. , vol.163 , pp. 13-30
    • Drøbak, B.K.1    Franklin-Tong, V.E.2    Staiger, C.J.3
  • 8
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields, G.B. and Noble, R.L. (1990) Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Protein Res. 35, 161-214.
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 9
    • 0035945343 scopus 로고    scopus 로고
    • Human VPS34 is required for internal vesicle formation within multivesicular endosomes
    • Futter, C.E., Collinson, L.M., Backer, J.M. and Hopkins, C.R. (2001) Human VPS34 is required for internal vesicle formation within multivesicular endosomes. J. Cell Biol. 155, 1251-1264.
    • (2001) J. Cell Biol. , vol.155 , pp. 1251-1264
    • Futter, C.E.1    Collinson, L.M.2    Backer, J.M.3    Hopkins, C.R.4
  • 10
    • 0141632907 scopus 로고    scopus 로고
    • Complex formation between the postsynaptic scaffolding protein gephyrin, profilin, and Mena: A possible link to the microfilament system
    • Giesemann, T., Schwarz, G., Nawrotzki, R. et al. (2003) Complex formation between the postsynaptic scaffolding protein gephyrin, profilin, and Mena: a possible link to the microfilament system. J. Neurosci. 23, 8330-8339.
    • (2003) J. Neurosci. , vol.23 , pp. 8330-8339
    • Giesemann, T.1    Schwarz, G.2    Nawrotzki, R.3
  • 11
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. and Peitsch, M.C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis, 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 12
    • 18144447988 scopus 로고    scopus 로고
    • Profilin in Phaseolus vulgaris is encoded by two genes (only one expressed in root nodules) but multiple isoforms are generated in vivo by phosphorylation on tyrosine residues
    • Guillen, G., Valdes-Lopez, V., Noguez, R., Olivares, J., Rodriguez-Zapata, L.C., Perez, H., Vidali, L., Villanueva, M.A. and Sanchez, F. (1999) Profilin in Phaseolus vulgaris is encoded by two genes (only one expressed in root nodules) but multiple isoforms are generated in vivo by phosphorylation on tyrosine residues. Plant J. 19, 497-508.
    • (1999) Plant J. , vol.19 , pp. 497-508
    • Guillen, G.1    Valdes-Lopez, V.2    Noguez, R.3    Olivares, J.4    Rodriguez-Zapata, L.C.5    Perez, H.6    Vidali, L.7    Villanueva, M.A.8    Sanchez, F.9
  • 13
    • 0028169625 scopus 로고
    • A phosphatidylinositol 3-kinase is induced during soybean nodule organogenesis and is associated with membrane proliferation
    • Hong, Z. and Verma, D.P. (1994) A phosphatidylinositol 3-kinase is induced during soybean nodule organogenesis and is associated with membrane proliferation. Proc. Natl Acad. Sci. USA, 91, 9617-9621.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9617-9621
    • Hong, Z.1    Verma, D.P.2
  • 14
    • 0033780016 scopus 로고    scopus 로고
    • Technical advance: Identification of plant actin-binding proteins by F-actin affinity chromatography
    • Hu, S., Brady, S.R., Kovar, D.R., Staiger, C.J., Clark, G.B., Roux, S.J. and Muday, G.K. (2000) Technical advance: identification of plant actin-binding proteins by F-actin affinity chromatography. Plant J. 24, 127-137.
    • (2000) Plant J. , vol.24 , pp. 127-137
    • Hu, S.1    Brady, S.R.2    Kovar, D.R.3    Staiger, C.J.4    Clark, G.B.5    Roux, S.J.6    Muday, G.K.7
  • 15
    • 0037193710 scopus 로고    scopus 로고
    • Actin-binding proteins in the Arabidopsis genome database: Properties of functionally distinct plant actin-depolymerizingfactors/cofilins
    • Hussey, P.J., Allwood, E.G. and Smertenko, A.P. (2002) Actin-binding proteins in the Arabidopsis genome database: properties of functionally distinct plant actin-depolymerizingfactors/cofilins. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 357, 791-798.
    • (2002) Philos. Trans. R. Soc. Lond. B. Biol. Sci. , vol.357 , pp. 791-798
    • Hussey, P.J.1    Allwood, E.G.2    Smertenko, A.P.3
  • 17
    • 0035098276 scopus 로고    scopus 로고
    • Trafficking of phosphatidylinositol 3-phosphate from the trans-Golgi network to the lumen of the central vacuole in plant cells
    • Kim, D.H., Eu, Y.J., Yoo, C.M., Kim, Y.W., Pih, K.T., Jin, J.B., Kim, S.J., Stenmark, H. and Hwang, I. (2001) Trafficking of phosphatidylinositol 3-phosphate from the trans-Golgi network to the lumen of the central vacuole in plant cells. Plant Cell, 13, 287-301.
    • (2001) Plant Cell , vol.13 , pp. 287-301
    • Kim, D.H.1    Eu, Y.J.2    Yoo, C.M.3    Kim, Y.W.4    Pih, K.T.5    Jin, J.B.6    Kim, S.J.7    Stenmark, H.8    Hwang, I.9
  • 18
    • 0034067715 scopus 로고    scopus 로고
    • Maize profilin isoforms are functionally distinct
    • Kovar, D.R., Drobak, B.K. and Staiger, C.J. (2000) Maize profilin isoforms are functionally distinct. Plant Cell, 12, 583-598.
    • (2000) Plant Cell , vol.12 , pp. 583-598
    • Kovar, D.R.1    Drobak, B.K.2    Staiger, C.J.3
  • 19
    • 0035882162 scopus 로고    scopus 로고
    • The characterization of ligand-specific maize (Zea mays) profilin mutants
    • Kovar, D.R., Drobak, B.K., Collings, D.A. and Staiger, C.J. (2001) The characterization of ligand-specific maize (Zea mays) profilin mutants. Biochem. J. 358, 49-57.
    • (2001) Biochem. J. , vol.358 , pp. 49-57
    • Kovar, D.R.1    Drobak, B.K.2    Collings, D.A.3    Staiger, C.J.4
  • 20
    • 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
  • 22
    • 19344368318 scopus 로고    scopus 로고
    • Autophagy regulates programmed cell death during the plant innate immune response
    • Liu, Y., Schiff, M., Czymmek, K., Talloczy, Z., Levine, B. and Dinesh-Kumar, S.P. (2005) Autophagy regulates programmed cell death during the plant innate immune response. Cell, 121, 567-577.
    • (2005) Cell , vol.121 , pp. 567-577
    • Liu, Y.1    Schiff, M.2    Czymmek, K.3    Talloczy, Z.4    Levine, B.5    Dinesh-Kumar, S.P.6
  • 23
    • 0031889993 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of human platelet profilin complexed with an oligo proline peptide
    • Mahoney, N.M. and Almo, S.C. (1998) Crystallization and preliminary X-ray analysis of human platelet profilin complexed with an oligo proline peptide. Acta. Crystallogr. D Biol. Crystallogr. 54 (Pt 1), 108-110.
    • (1998) Acta. Crystallogr. D Biol. Crystallogr. , vol.54 , Issue.1 PART , pp. 108-110
    • Mahoney, N.M.1    Almo, S.C.2
  • 24
    • 0028981718 scopus 로고
    • Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells
    • Matsuoka, K., Bassham, D.C., Raikhel, N.V. and Nakamura, K. (1995) Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells. J. Cell Biol. 130, 1307-1318.
    • (1995) J. Cell Biol. , vol.130 , pp. 1307-1318
    • Matsuoka, K.1    Bassham, D.C.2    Raikhel, N.V.3    Nakamura, K.4
  • 25
    • 0033037447 scopus 로고    scopus 로고
    • The SH3 domain of Bruton's tyrosine kinase displays altered ligand binding properties when autophosphorylated in vitro
    • Morrogh, L.M., Hinshelwood, S., Costello, P., Cory, G.O. and Kinnon, C. (1999) The SH3 domain of Bruton's tyrosine kinase displays altered ligand binding properties when autophosphorylated in vitro. Eur. J. Immunol. 29, 2269-2279.
    • (1999) Eur. J. Immunol. , vol.29 , pp. 2269-2279
    • Morrogh, L.M.1    Hinshelwood, S.2    Costello, P.3    Cory, G.O.4    Kinnon, C.5
  • 26
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins, 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 27
  • 29
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N. and Peitsch, M.C. (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31, 3381-3385.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 30
    • 0242501529 scopus 로고    scopus 로고
    • Profilin I colocalizes with speckles and Cajal bodies: A possible role in pre-mRNA splicing
    • Skare, P., Kreivi, J.P., Bergstrom, A. and Karlsson, R. (2003) Profilin I colocalizes with speckles and Cajal bodies: a possible role in pre-mRNA splicing. Exp. Cell Res. 286, 12-21.
    • (2003) Exp. Cell Res. , vol.286 , pp. 12-21
    • Skare, P.1    Kreivi, J.P.2    Bergstrom, A.3    Karlsson, R.4
  • 32
    • 0028964232 scopus 로고
    • Vesicle-mediated protein transport: Regulatory interactions between the Vps15 protein kinase and the Vps34 PtdIns 3-kinase essential for protein sorting to the vacuole in yeast
    • Stack, J.H., DeWald, D.B., Takegawa, K. and Emr, S.D. (1995) Vesicle-mediated protein transport: regulatory interactions between the Vps15 protein kinase and the Vps34 PtdIns 3-kinase essential for protein sorting to the vacuole in yeast. J. Cell Biol. 129, 321-334.
    • (1995) J. Cell Biol. , vol.129 , pp. 321-334
    • Stack, J.H.1    DeWald, D.B.2    Takegawa, K.3    Emr, S.D.4
  • 34
    • 0025938876 scopus 로고
    • Formation of phosphatidylinositol 3-phosphate by isomerization from phosphatidylinositol 4-phosphate
    • Walsh, J.P., Caldwell, K.K. and Majerus, P.W. (1991) Formation of phosphatidylinositol 3-phosphate by isomerization from phosphatidylinositol 4-phosphate. Proc. Natl Acad. Sci. USA, 88, 9184-9187.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 9184-9187
    • Walsh, J.P.1    Caldwell, K.K.2    Majerus, P.W.3
  • 35
    • 0027942615 scopus 로고
    • AtVPS34, a phosphatidylinositol 3-kinase of Arabidopsis thaliana, is an essential protein with homology to a calcium-dependent lipid binding domain
    • Welters, P., Takegawa, K., Emr, S.D. and Chrispeels, M.J. (1994) AtVPS34, a phosphatidylinositol 3-kinase of Arabidopsis thaliana, is an essential protein with homology to a calcium-dependent lipid binding domain. Proc. Natl Acad. Sci. USA 91, 11398-11402.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 11398-11402
    • Welters, P.1    Takegawa, K.2    Emr, S.D.3    Chrispeels, M.J.4
  • 36
    • 4143120075 scopus 로고    scopus 로고
    • The role of profilin complexes in cell motility and other cellular processes
    • Witke, W. (2004) The role of profilin complexes in cell motility and other cellular processes. Trends Cell Biol. 14, 461-469.
    • (2004) Trends Cell Biol. , vol.14 , pp. 461-469
    • Witke, W.1
  • 37
    • 0032481313 scopus 로고    scopus 로고
    • In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly
    • Witke, W., Podtelejnikov, A.V., Di Nardo, A., Sutherland, J.D., Gurniak, C.B., Dotti, C. and Mann, M. (1998) In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly. EMBO J. 17, 967-976.
    • (1998) EMBO J. , vol.17 , pp. 967-976
    • Witke, W.1    Podtelejnikov, A.V.2    Di Nardo, A.3    Sutherland, J.D.4    Gurniak, C.B.5    Dotti, C.6    Mann, M.7
  • 38
    • 0032515170 scopus 로고    scopus 로고
    • PSTPIP 2, a second tyrosine phosphorylated, cytoskeletal-associated protein that binds a PEST-type protein-tyrosine phosphatase
    • Wu, Y., Dowbenko, D. and Lasky, L.A. (1998) PSTPIP 2, a second tyrosine phosphorylated, cytoskeletal-associated protein that binds a PEST-type protein-tyrosine phosphatase. J. Biol. Chem. 273, 30487-30496.
    • (1998) J. Biol. Chem. , vol.273 , pp. 30487-30496
    • Wu, Y.1    Dowbenko, D.2    Lasky, L.A.3


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