Oligomerization studies show that the kinase domain of the tomato pollen receptor kinase LePRK2 is necessary for interaction with LePRK1
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 b...
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2012
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09819428_v53_n_p40_Salem http://hdl.handle.net/20.500.12110/paper_09819428_v53_n_p40_Salem |
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paper:paper_09819428_v53_n_p40_Salem2023-06-08T15:59:14Z Oligomerization studies show that the kinase domain of the tomato pollen receptor kinase LePRK2 is necessary for interaction with LePRK1 Salem, Tamara Marcela Wengier, Diego Leonardo Muschietti, Jorge P. 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 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. Fil:Salem, T.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Wengier, D.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Muschietti, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2012 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09819428_v53_n_p40_Salem http://hdl.handle.net/20.500.12110/paper_09819428_v53_n_p40_Salem |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 Salem, Tamara Marcela Wengier, Diego Leonardo Muschietti, Jorge P. Oligomerization studies show that the kinase domain of the tomato pollen receptor kinase LePRK2 is necessary for interaction with LePRK1 |
| topic_facet |
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 |
| description |
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. |
| author |
Salem, Tamara Marcela Wengier, Diego Leonardo Muschietti, Jorge P. |
| author_facet |
Salem, Tamara Marcela Wengier, Diego Leonardo Muschietti, Jorge P. |
| author_sort |
Salem, Tamara Marcela |
| title |
Oligomerization studies show that the kinase domain of the tomato pollen receptor kinase LePRK2 is necessary for interaction with LePRK1 |
| title_short |
Oligomerization studies show that the kinase domain of the tomato pollen receptor kinase LePRK2 is necessary for interaction with LePRK1 |
| title_full |
Oligomerization studies show that the kinase domain of the tomato pollen receptor kinase LePRK2 is necessary for interaction with LePRK1 |
| title_fullStr |
Oligomerization studies show that the kinase domain of the tomato pollen receptor kinase LePRK2 is necessary for interaction with LePRK1 |
| title_full_unstemmed |
Oligomerization studies show that the kinase domain of the tomato pollen receptor kinase LePRK2 is necessary for interaction with LePRK1 |
| title_sort |
oligomerization studies show that the kinase domain of the tomato pollen receptor kinase leprk2 is necessary for interaction with leprk1 |
| publishDate |
2012 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09819428_v53_n_p40_Salem http://hdl.handle.net/20.500.12110/paper_09819428_v53_n_p40_Salem |
| work_keys_str_mv |
AT salemtamaramarcela oligomerizationstudiesshowthatthekinasedomainofthetomatopollenreceptorkinaseleprk2isnecessaryforinteractionwithleprk1 AT wengierdiegoleonardo oligomerizationstudiesshowthatthekinasedomainofthetomatopollenreceptorkinaseleprk2isnecessaryforinteractionwithleprk1 AT muschiettijorgep oligomerizationstudiesshowthatthekinasedomainofthetomatopollenreceptorkinaseleprk2isnecessaryforinteractionwithleprk1 |
| _version_ |
1768545747722043392 |