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Abstract:

LePRK1 and LePRK2 are two pollen-specific receptor-like kinases from Solanum lycopersicum that are involved in signaling during pollen-pistil communication. Previously, we showed that both proteins interact in pollen and when expressed in yeast. We also showed that pollen tube length was regulated by phosphorylation of specific residues in the juxtamembrane domain of LePRK2. To determine the domains responsible for the interaction between LePRK1 and LePRK2, we constructed a series of deletions, expressed them in yeast and determined their association by co-immunoprecipitation assays. We show that deletions containing extracellular domains of LePRK1 and LePRK2 were glycosylated in yeast and were sufficient for interaction with the corresponding full-length receptor. The juxtamembrane domain of LePRK1 was sufficient for its interaction with LePRK2, whereas LePRK2 required its kinase domain for interaction with LePRK1. These findings suggest a role for the juxtamembrane domain of LePRK2 in mediating intracellular dimerization and thus receptor kinase phosphorylation. © 2012 Elsevier Masson SAS.

Registro:

Documento: Artículo
Título:Oligomerization studies show that the kinase domain of the tomato pollen receptor kinase LePRK2 is necessary for interaction with LePRK1
Autor:Salem, T.M.; Barberini, M.L.; Wengier, D.L.; Cabanas, M.L.; de Paz, P.; Muschietti, J.
Filiación:Instituto de Ingeniería Genética y Biología Molecular INGEBI, Consejo Nacional de Investigaciones Científicas y Técnicas, 1428 Buenos Aires, Argentina
Departamento de Biodiversidad y Biología Experimental, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina
Palabras clave:Deletion domains; Immunoprecipitation; Pollen; Receptor kinases; Yeast; protein kinase C; protein kinase N; vegetable protein; article; dimerization; enzyme specificity; genetics; glycosylation; immunoprecipitation; metabolism; mutation; phosphorylation; pollen; protein tertiary structure; signal transduction; tomato; yeast; Dimerization; Glycosylation; Immunoprecipitation; Lycopersicon esculentum; Mutation; Phosphorylation; Plant Proteins; Pollen; Protein Kinase C; Protein Structure, Tertiary; Signal Transduction; Substrate Specificity; Yeasts; Lycopersicon esculentum
Año:2012
Volumen:53
Página de inicio:40
Página de fin:45
DOI: http://dx.doi.org/10.1016/j.plaphy.2012.01.008
Título revista:Plant Physiology and Biochemistry
Título revista abreviado:Plant Physiol. Biochem.
ISSN:09819428
CODEN:PPBIE
CAS:protein kinase C, 141436-78-4; Plant Proteins; Protein Kinase C, 2.7.11.13; protein kinase N, 2.7.1.-
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09819428_v53_n_p40_Salem

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Citas:

---------- APA ----------
Salem, T.M., Barberini, M.L., Wengier, D.L., Cabanas, M.L., de Paz, P. & Muschietti, J. (2012) . Oligomerization studies show that the kinase domain of the tomato pollen receptor kinase LePRK2 is necessary for interaction with LePRK1. Plant Physiology and Biochemistry, 53, 40-45.
http://dx.doi.org/10.1016/j.plaphy.2012.01.008
---------- CHICAGO ----------
Salem, T.M., Barberini, M.L., Wengier, D.L., Cabanas, M.L., de Paz, P., Muschietti, J. "Oligomerization studies show that the kinase domain of the tomato pollen receptor kinase LePRK2 is necessary for interaction with LePRK1" . Plant Physiology and Biochemistry 53 (2012) : 40-45.
http://dx.doi.org/10.1016/j.plaphy.2012.01.008
---------- MLA ----------
Salem, T.M., Barberini, M.L., Wengier, D.L., Cabanas, M.L., de Paz, P., Muschietti, J. "Oligomerization studies show that the kinase domain of the tomato pollen receptor kinase LePRK2 is necessary for interaction with LePRK1" . Plant Physiology and Biochemistry, vol. 53, 2012, pp. 40-45.
http://dx.doi.org/10.1016/j.plaphy.2012.01.008
---------- VANCOUVER ----------
Salem, T.M., Barberini, M.L., Wengier, D.L., Cabanas, M.L., de Paz, P., Muschietti, J. Oligomerization studies show that the kinase domain of the tomato pollen receptor kinase LePRK2 is necessary for interaction with LePRK1. Plant Physiol. Biochem. 2012;53:40-45.
http://dx.doi.org/10.1016/j.plaphy.2012.01.008