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Wengier, D.; Valsecchi, I.; Cabanas, M.L.; Tang, W.-H.; McCormick, S.; Muschietti, J. "The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract" (2003) Proceedings of the National Academy of Sciences of the United States of America. 100(11):6860-6865
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Abstract:

After pollen grains germinate on the stigma, pollen tubes traverse the extracellular matrix of the style on their way to the ovules. We previously characterized two pollen-specific, receptor-like kinases, LePRK1 and LePRK2, from tomato (Lycopersicon esculentum). Their structure and immunolocalization pattern and the specific dephosphorylation of LePRK2 suggested that these kinases might interact with signaling molecules in the style extracellular matrix. Here, we show that LePRK1 and LePRK2 can be coimmunoprecipitated from pollen or when expressed together in yeast. In yeast, their association requires LePRK2 kinase activity. In pollen, LePRK1 and LePRK2 are found in an ≈400-kDa protein complex that persists on pollen germination, but this complex is disrupted when pollen is germinated in vitro in the presence of style extract. In yeast, the addition of style extract also disrupts the interaction between LePRK1 and LePRK2. Fractionation of the style extract reveals that the disruption activity is enriched in the 3- to 10-kDa fraction. A component(s) in this fraction also is responsible for the specific dephosphorylation of LePRK2. The style component(s) that dephosphorylates LePRK2 is likely to be a heat-stable peptide that is present in exudate from the style. The generally accepted model of receptor kinase signaling involves binding of a ligand to extracellular domains of receptor kinases and subsequent activation of the signaling pathway by receptor autophosphorylation. In contrast to this typical scenario, we propose that a putative style ligand transduces the signal in pollen tubes by triggering the specific dephosphorylation of LePRK2, followed by dissociation of the LePRK complex.

Registro:

Documento: Artículo
Título:The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract
Autor:Wengier, D.; Valsecchi, I.; Cabanas, M.L.; Tang, W.-H.; McCormick, S.; Muschietti, J.
Filiación:Inst. de Ing. Genet. y Biol. Molec., Consejo Nac. Invest. Cie. Tec. ARG, Universidad de Buenos Aires, Obligado 2490, 1428 Buenos Aires, Argentina
Plant Gene Expression Center, U.S. Dept Agric. Agric. Res. Serv., University of California at Berkeley, 800 Buchanan Street, Albany, CA 94710, United States
Department of Medical Biochemistry, Uppsala University, SE-751 23 Uppsala, Sweden
Palabras clave:plant extract; protein kinase; protein LePRK1; protein LePRK2; unclassified drug; article; autophosphorylation; dephosphorylation; dissociation; enzyme activity; extracellular matrix; fractionation; germination; immunoprecipitation; molecular interaction; nonhuman; pistil style; pollen; pollen tube; priority journal; protein expression; protein stability; signal transduction; thermostability; tomato; yeast; Lycopersicon esculentum; Pollen; Protein Kinase C; Recombinant Proteins; Saccharomyces cerevisiae; Fungi; Lycopersicon; Lycopersicon esculentum
Año:2003
Volumen:100
Número:11
Página de inicio:6860
Página de fin:6865
DOI: http://dx.doi.org/10.1073/pnas.0631728100
Título revista:Proceedings of the National Academy of Sciences of the United States of America
Título revista abreviado:Proc. Natl. Acad. Sci. U. S. A.
ISSN:00278424
CODEN:PNASA
CAS:protein kinase, 9026-43-1; PKC-related kinase PRK2, EC 2.7.1.-; Protein Kinase C, EC 2.7.1.37; protein kinase N, EC 2.7.1.-; Recombinant Proteins
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v100_n11_p6860_Wengier

Referencias:

  • Shiu, S.H., Bleecker, A.B., (2001) Science STKE, 2001, pp. RE22
  • Clark, S.E., Williams, R.W., Meyerowitz, E.M., (1997) Cell, 89, pp. 575-585
  • Jinn, T.L., Stone, J.M., Walker, J.C., (2000) Genes Dev., 14, pp. 108-117
  • Zhao, D.Z., Wang, G.F., Speal, B., Ma, H., (2002) Genes Dev., 16, pp. 2021-2031
  • Canales, C., Bhatt, A.M., Scott, R., Dickinson, H., (2002) Curr. Biol., 12, pp. 1718-1727
  • Shah, K., Gadella, T.W., Van Erp, H., Hecht, V., De Vries, S.C., (2001) J. Mol. Biol., 309, pp. 641-655
  • Li, J., Chory, J., (1997) Cell, 90, pp. 929-938
  • Matsubayashi, Y., Ogawa, M., Morita, A., Sakagami, Y., (2002) Science, 296, pp. 1470-1472
  • Gomez-Gomez, L., Bauer, Z., Boller, T., (2001) Plant Cell, 13, pp. 1155-1163
  • Jeong, S., Trotochaud, A.E., Clark, S.E., (1999) Plant Cell, 11, pp. 1925-1934
  • Fletcher, J.C., Brand, U., Running, M.P., Simon, R., Meyerowitz, E.M., (1999) Science, 283, pp. 1911-1914
  • Trotochaud, A.E., Hao, T., Wu, G., Yang, Z., Clark, S.E., (1999) Plant Cell, 11, pp. 393-406
  • Trotochaud, A.E., Jeong, S., Clark, S.E., (2000) Science, 289, pp. 613-617
  • Li, J., Wen, J., Lease, K.A., Doke, J.T., Tax, F.E., Walker, J.C., (2002) Cell, 110, pp. 213-222
  • Nam, K.H., Li, J., (2002) Cell, 110, pp. 203-212
  • Park, A.R., Cho, S.K., Yun, U.J., Jin, M.Y., Lee, S.H., Sachetto Martins, G., Park, O.K., (2001) J. Biol. Chem., 276, pp. 26688-26693
  • Kachroo, A., Schopfer, C.R., Nasrallah, M.E., Nasrallah, J.B., (2001) Science, 293, pp. 1824-1826
  • Schopfer, C.R., Nasrallah, M.E., Nasrallah, J.B., (1999) Science, 286, pp. 1697-1700
  • Takayama, S., Shimosato, H., Shiba, H., Funato, M., Che, F.S., Watanabe, M., Iwano, M., Isogai, A., (2001) Nature, 413, pp. 534-548
  • Giranton, J.L., Dumas, C., Cock, J.M., Gaude, T., (2000) Proc. Natl. Acad. Sci. USA, 97, pp. 3759-3764
  • Wheeler, M.J., Franklin Tong, V.E., Franklin, F.C.H., (2001) New Phytol., 151, pp. 565-584
  • Franklin Tong, V.E., (1999) Curr. Opin. Plant Biol., 2, pp. 490-495
  • Feijo, J.A., Sainhas, J., Holdaway Clarke, T., Cordeiro, M.S., Kunkel, J.G., Hepler, P.K., (2001) BioEssays, 23, pp. 86-94
  • Muschietti, J., Eyal, Y., McCormick, S., (1998) Plant Cell, 10, pp. 319-330
  • Kim, H.U., Cotter, R., Johnson, S., Senda, M., Dodds, P., Kulikauskas, R., Tang, W., McCormick, S., (2002) Plant Mol. Biol., 50, pp. 1-16
  • Tang, W., Ezcurra, I., Muschietti, J., McCormick, S., (2002) Plant Cell, 14, pp. 2277-2287
  • Foreman, P.K., Davis, R.W., (1994) Gene, 144, pp. 63-68
  • Gietz, R.D., Woods, R.A., (2002) Methods Enzymol., 350, pp. 87-96
  • White, J.M., Rose, M.D., (2001) Curr. Biol., 11, pp. R16-R20
  • Muschietti, J., Dircks, L., Vancanneyt, G., McCormick, S., (1994) Plant J., 6, pp. 321-338
  • Mollet, J.C., Park, S.Y., Nothnagel, E.A., Lord, E.M., (2000) Plant Cell, 12, pp. 1737-1750
  • Park, S.Y., Jauh, G.Y., Mollet, J.C., Eckard, K.J., Nothnagel, E.A., Walling, L.L., Lord, E.M., (2000) Plant Cell, 12, pp. 151-164
  • Matsubayashi, Y., Yang, H., Sakagami, Y., (2001) Trends Plant Sci., 6, pp. 573-577
  • Wang, Z.Y., Seto, H., Fujioka, S., Yoshida, S., Chory, J., (2001) Nature, 410, pp. 380-383
  • Cabrillac, D., Cock, J.M., Dumas, C., Gaude, T., (2001) Nature, 410, pp. 220-223
  • Siegel, R.M., Frederiksen, J.K., Zacharias, D.A., Chan, F.K., Johnson, M., Lynch, D., Tsien, R.Y., Lenardo, M.J., (2000) Science, 288, pp. 2354-2357
  • Papoff, G., Hausler, P., Eramo, A., Pagano, M.G., Di Leve, G., Signore, A., Ruberti, G., (1999) J. Biol. Chem., 274, pp. 38241-38250
  • Krause, C.D., Mei, E., Xie, J., Jia, Y., Bopp, M.A., Hochstrasser, R.M., Pestka, S., (2002) Mol. Cell Protein, 1, pp. 805-815
  • Jin, M.H., Sawamoto, K., Ito, M., Okano, H., (2000) Mol. Cell. Biol., 20, pp. 2098-2107
  • Chang, C., Stadler, R., (2001) BioEssays, 23, pp. 619-627

Citas:

---------- APA ----------
Wengier, D., Valsecchi, I., Cabanas, M.L., Tang, W.-H., McCormick, S. & Muschietti, J. (2003) . The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract. Proceedings of the National Academy of Sciences of the United States of America, 100(11), 6860-6865.
http://dx.doi.org/10.1073/pnas.0631728100
---------- CHICAGO ----------
Wengier, D., Valsecchi, I., Cabanas, M.L., Tang, W.-H., McCormick, S., Muschietti, J. "The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract" . Proceedings of the National Academy of Sciences of the United States of America 100, no. 11 (2003) : 6860-6865.
http://dx.doi.org/10.1073/pnas.0631728100
---------- MLA ----------
Wengier, D., Valsecchi, I., Cabanas, M.L., Tang, W.-H., McCormick, S., Muschietti, J. "The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract" . Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 11, 2003, pp. 6860-6865.
http://dx.doi.org/10.1073/pnas.0631728100
---------- VANCOUVER ----------
Wengier, D., Valsecchi, I., Cabanas, M.L., Tang, W.-H., McCormick, S., Muschietti, J. The receptor kinases LePRK1 and LePRK2 associate in pollen and when expressed in yeast, but dissociate in the presence of style extract. Proc. Natl. Acad. Sci. U. S. A. 2003;100(11):6860-6865.
http://dx.doi.org/10.1073/pnas.0631728100